|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-1419 |
0e+00 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 2635.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1 MGKEQKEKKD-----GNLSIKEEVEKELNKKSTAELFRKIKNEKISFFLPFKCLPAQHRKLLFISFVCAVLSGGTLPFFI 75
Cdd:PTZ00265 1 MKKDQRQKKDnnsggGNLSIKDEVEKELNKKGTFELYKKIKTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 76 SVFGVILKNMNLGDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYLRSVFYQDGQFHDNNPGSKLRSDL 155
Cdd:PTZ00265 81 SVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 156 DFYLEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVCGVICNKKVKLNKKTSLLYNNNTMSIIE 235
Cdd:PTZ00265 161 DFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 236 EALMGIRTVASYCGEKTILNKFNLSETFYSKYILKANFVEALHIGLINGLILVSYAFGFWYGTRIIINSATNQYPNNDFN 315
Cdd:PTZ00265 241 EALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 316 GASVISILLGVLISMFMLTIILPNITEYMKALEATNSLYEIINRKPLVENNDDGETLPNIKKIEFKNVRFHYDTRKDVEI 395
Cdd:PTZ00265 321 GGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 396 YKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 475
Cdd:PTZ00265 401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 476 KYSLYSLKDLEAMENYYEENTNDTYENKN------------FSLISNSMTSNELLEMKKEYQTIKDSDVVDVSKKVLIHD 543
Cdd:PTZ00265 481 KYSLYSLKDLEALSNYYNEDGNDSQENKNkrnscrakcagdLNDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKKVLIHD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 544 FVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 623
Cdd:PTZ00265 561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 624 STIRYANTIFVLSNRERSDNNNNNNNDDNNNNNNNNNNKI-----------------NNEGSYIIEQGTHDSLMKNKNGI 686
Cdd:PTZ00265 641 STIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKnnkddnnnnnnnnnnkiNNAGSYIIEQGTHDALMKNKNGI 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 687 YHLMINNQKISSNKSSNNGNDNGSDNKSSAYKDSDTGNDADNMNSLSIHENENISNNRNCK----NTAENEKEEKVPFFK 762
Cdd:PTZ00265 721 YYTMINNQKVSSKKSSNNDNDKDSDMKSSAYKDSERGYDPDEMNGNSKHENESASNKKSCKmsdeNASENNAGGKLPFLR 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 763 RMFRRKKKAPNNLRIIYKEIFSYKKDVTIIFFSILVAGGLYPVFALLYARYVSTLFDFANLEYNSNKYSIYILLIAIAMF 842
Cdd:PTZ00265 801 NLFKRKPKAPNNLRIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIAMF 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 843 ISETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFDQDKNTPGVLSAHINRDVHLLKTGLVNNIVIFSHFIMLFLVSM 922
Cdd:PTZ00265 881 ISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSM 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 923 VMSFYFCPIVAAVLTFIYFINMRVFAVRARLTKSKEIEKKE-NMSSGVFAFSSDDEMFKDPSFLIQEAFYNMHTVINYGL 1001
Cdd:PTZ00265 961 VMSFYFCPIVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEiNQPGTVFAYNSDDEIFKDPSFLIQEAFYNMNTVIIYGL 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1002 EDYFCNLIEKAIDYKNKGQKRRIIVNAALWGFSQSAQLFINSFAYWFGSFLIKRGTILVDDFMKSLFTFIFTGSYAGKLM 1081
Cdd:PTZ00265 1041 EDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLM 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1082 SLKGDSENAKLSFEKYYPLMIRKSNIDVRDDGGIRI-NKNLIKGKVDIKDVNFRYISRPNVPIYKNLSFTCDSKKTTAIV 1160
Cdd:PTZ00265 1121 SLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIkNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIV 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1161 GETGSGKSTFMNLLLRFYDLKNDHIIL-----KNDMTNFQDYQNNNNNSLVLKNVNEFS--NQSGSAEDYTVFNNNGEIL 1233
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYDLKNDHHIVfknehTNDMTNEQDYQGDEEQNVGMKNVNEFSltKEGGSGEDSTVFKNSGKIL 1280
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1234 LDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLS 1313
Cdd:PTZ00265 1281 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLS 1360
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1314 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRNGTF 1393
Cdd:PTZ00265 1361 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTGSF 1440
|
1450 1460
....*....|....*....|....*.
gi 124506379 1394 VQSHGTHDELLSAQDGIYKKYVKLAK 1419
Cdd:PTZ00265 1441 VQAHGTHEELLSVQDGVYKKYVKLAK 1466
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-694 |
5.69e-133 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 422.27 E-value: 5.69e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 25 KKSTAELFRKIknekISFFLPfkclpaqHRKLLFISFVCAVLSGGTLPFFISVFGVILKNMNLGDD---INPIILSLVSI 101
Cdd:COG1132 2 SKSPRKLLRRL----LRYLRP-------YRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDlsaLLLLLLLLLGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 102 GLVQFILSMISSYCMDVITSKILKTLKLEYLRSVFYQDGQFHDNNPGSKLRSDLDFYLEQVSSGIGTKFITIFTYASSFL 181
Cdd:COG1132 71 ALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 182 GLYIWSLIKNARLTLCITCVFPLIYVCGVICNKKVKLNKKTSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNKFN-LS 260
Cdd:COG1132 151 GALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFReAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 261 ETFYSKYIlKANFVEALHIGLINGLILVSYAFGFWYGTRIIINSatnqypnndfngasviSILLGVLISMFMLTIILPN- 339
Cdd:COG1132 231 EELRRANL-RAARLSALFFPLMELLGNLGLALVLLVGGLLVLSG----------------SLTVGDLVAFILYLLRLFGp 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 340 -------ITEYMKALEATNSLYEIINRKPLVENNDDGETLPNIK-KIEFKNVRFHYDTRKDVeiYKDLSFTLKEGKTYAF 411
Cdd:COG1132 294 lrqlanvLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPPVRgEIEFENVSFSYPGDRPV--LKDISLTIPPGETVAL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 412 VGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdleameny 491
Cdd:COG1132 372 VGPSGSGKSTLVNLLLRFYDPTSGRILIDG-VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYG------------- 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 492 yeentndtyeNKNFSlisnsmtsnellemkkeyqtikDSDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRI 571
Cdd:COG1132 438 ----------RPDAT----------------------DEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRI 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 572 SIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNRErsdnnnnnnndd 651
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAHRLSTIRNADRILVLDDGR------------ 551
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 124506379 652 nnnnnnnnnnkinnegsyIIEQGTHDSLMKnKNGIYHLMINNQ 694
Cdd:COG1132 552 ------------------IVEQGTHEELLA-RGGLYARLYRLQ 575
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
764-1417 |
6.70e-132 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 419.57 E-value: 6.70e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 764 MFRRKKKApnnLRIIYKEIFSYKKDVTIIFFSILVAGGLYPVFALLYARYVSTLFDFANLEYnSNKYSIYILLIAIAMFI 843
Cdd:COG1132 1 MSKSPRKL---LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA-LLLLLLLLLGLALLRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 844 SETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFDqdKNTPGVLSAHINRDVHLLKTGLVNNIVIFSHFIMLFLVSMV 923
Cdd:COG1132 77 LSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 924 MSFYFCP---IVAAVLTFIYFINMRVFAVRARLTKSKEIEKKENMSSgvfafssddemfkdpsfLIQEAFYNMHTVINYG 1000
Cdd:COG1132 155 VLFVIDWrlaLIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNG-----------------RLQESLSGIRVVKAFG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1001 LEDYFCNLIEKAIDYKNKGQKRRIIVNAALWGFSQSAQLFINSFAYWFGSFLIKRGTILVDDFMksLFTFIFTGSYA--G 1078
Cdd:COG1132 218 REERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLV--AFILYLLRLFGplR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1079 KLMSLKGDSENAKLSFEKYYPLMIRKSNIDVRDDGgirINKNLIKGKVDIKDVNFRYisRPNVPIYKNLSFTCDSKKTTA 1158
Cdd:COG1132 296 QLANVLNQLQRALASAERIFELLDEPPEIPDPPGA---VPLPPVRGEIEFENVSFSY--PGDRPVLKDISLTIPPGETVA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1159 IVGETGSGKSTFMNLLLRFYDlkndhiilkndmtnfqdyqnnnnnslvlknVNEfsnqsgsaedytvfnnnGEILLDDIN 1238
Cdd:COG1132 371 LVGPSGSGKSTLVNLLLRFYD------------------------------PTS-----------------GRILIDGVD 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1239 ICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQ 1318
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQ 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1319 RIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNnpdrNGTFVQShG 1398
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTIRNADRILVLD----DGRIVEQ-G 556
|
650
....*....|....*....
gi 124506379 1399 THDELLsAQDGIYKKYVKL 1417
Cdd:COG1132 557 THEELL-ARGGLYARLYRL 574
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
378-694 |
1.23e-115 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 362.24 E-value: 1.23e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLKWWRSKI 457
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG-VDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSNSIKNNIKYSLYSLKDLEAMEnyyeentndtyenknfslisnsmtsnellemkkeyqtikdsdvvdVSK 537
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEE---------------------------------------------AAK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 KVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITI 617
Cdd:cd03249 115 KANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTI 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 618 IIAHRLSTIRYANTIFVLSNrersdnnnnnnnddnnnnnnnnnnkinnegSYIIEQGTHDSLMKNKnGIYHLMINNQ 694
Cdd:cd03249 193 VIAHRLSTIRNADLIAVLQN------------------------------GQVVEQGTHDELMAQK-GVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1126-1418 |
2.42e-114 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 358.78 E-value: 2.42e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVS 1285
Cdd:cd03249 56 ----------------------TSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1286 KFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTI 1365
Cdd:cd03249 114 KKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTT 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 124506379 1366 ITIAHRIASIKRSDKIVVFNNpdrngTFVQSHGTHDELLsAQDGIYKKYVKLA 1418
Cdd:cd03249 192 IVIAHRLSTIRNADLIAVLQN-----GQVVEQGTHDELM-AQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
765-1416 |
1.12e-105 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 352.21 E-value: 1.12e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 765 FRRKKKAPNNLRIIYKEIFSYKKDVTIIFFSILVAGglypVFALLYARYVSTLFDFAnlEYNSNKYSIYILLIAIAM--- 841
Cdd:COG2274 134 FDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLIN----LLALATPLFTQVVIDRV--LPNQDLSTLWVLAIGLLLall 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 842 --FISETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFDQdkNTPGVLSAHInRDVHLLKTGLVNNIV-IFSHFIMLF 918
Cdd:COG2274 208 feGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFES--RSVGDLASRF-RDVESIREFLTGSLLtALLDLLFVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 919 LVSMVMSFY---FCPIVAAVLTFIYFINMRVFAVRARLTKsKEIEKKENMSSgvfafssddemfkdpsfLIQEAFYNMHT 995
Cdd:COG2274 285 IFLIVLFFYsppLALVVLLLIPLYVLLGLLFQPRLRRLSR-EESEASAKRQS-----------------LLVETLRGIET 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 996 VINYGLEDYFCNLIEKAI-DYKNKGQKRRIIVNAALWgFSQSAQLFINSFAYWFGSFLIKRGTIlvddfmkSLFTFIFTG 1074
Cdd:COG2274 347 IKALGAESRFRRRWENLLaKYLNARFKLRRLSNLLST-LSGLLQQLATVALLWLGAYLVIDGQL-------TLGQLIAFN 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1075 SYAG-------KLMSLKGDSENAKLSFEKYYPLMirksNIDV-RDDGGIRINKNLIKGKVDIKDVNFRYiSRPNVPIYKN 1146
Cdd:COG2274 419 ILSGrflapvaQLIGLLQRFQDAKIALERLDDIL----DLPPeREEGRSKLSLPRLKGDIELENVSFRY-PGDSPPVLDN 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1147 LSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDlkndhiilkndmtnfqdyqnnnnnslvlknvnefsnqsgsaedytvf 1226
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE----------------------------------------------- 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1227 NNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVSKFAAIDEFIESLPNKYDTNVG 1306
Cdd:COG2274 527 PTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVG 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1307 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNn 1386
Cdd:COG2274 607 EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRLADRIIVLD- 683
|
650 660 670
....*....|....*....|....*....|
gi 124506379 1387 pdrNGTFVQShGTHDELLsAQDGIYKKYVK 1416
Cdd:COG2274 684 ---KGRIVED-GTHEELL-ARKGLYAELVQ 708
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
33-694 |
1.61e-100 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 337.96 E-value: 1.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 33 RKIKNEKISFFLPFkcLpAQHRKLLFISFVCAVLSGG---TLPFFI-SVFGVILKNMNLgDDINPIILSLVSIGLVQFIL 108
Cdd:COG2274 137 RGEKPFGLRWFLRL--L-RRYRRLLLQVLLASLLINLlalATPLFTqVVIDRVLPNQDL-STLWVLAIGLLLALLFEGLL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 109 SMISSYCMDVITSKILKTLKLEYLRSVFY-QDGQFHDNNPG---SKLRSdldfyLEQVSSGIGTKFITIFTYA-SSFLGL 183
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLRLSSRFFRHLLRlPLSFFESRSVGdlaSRFRD-----VESIREFLTGSLLTALLDLlFVLIFL 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 184 YIWSLIkNARLTLCITCVFPLIYVCGVICNKK-VKLNKKTSLLYNNNTmSIIEEALMGIRTVASYCGEKTILNKFNLSET 262
Cdd:COG2274 288 IVLFFY-SPPLALVVLLLIPLYVLLGLLFQPRlRRLSREESEASAKRQ-SLLVETLRGIETIKALGAESRFRRRWENLLA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 263 FYSKYILKANFVEALHIGLINGLILVSYAFGFWYGTRIIINsatnqypnNDFN-GASV-ISILLGVLISmFMLTIILpNI 340
Cdd:COG2274 366 KYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVID--------GQLTlGQLIaFNILSGRFLA-PVAQLIG-LL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 341 TEYMKALEATNSLYEIINRKPLVENNDDGETLPNIK-KIEFKNVRFHYDTRkDVEIYKDLSFTLKEGKTYAFVGESGCGK 419
Cdd:COG2274 436 QRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKgDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 420 STILKLIERLYDPTEGDIIVNDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdleAMENyyeentndt 499
Cdd:COG2274 515 STLLKLLLGLYEPTSGRILIDG-IDLRQIDPASLRRQIGVVLQDVFLFSGTIRENI-----------TLGD--------- 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 500 yenknfslisnsmtsnellemkkeyQTIKDSDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMR 579
Cdd:COG2274 574 -------------------------PDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLR 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 580 NPKILILDEATSSLDNKSEYLVQKTINNLKGneNRITIIIAHRLSTIRYANTIFVLSNRErsdnnnnnnnddnnnnnnnn 659
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGR-------------------- 686
|
650 660 670
....*....|....*....|....*....|....*
gi 124506379 660 nnkinnegsyIIEQGTHDSLMKnKNGIYHLMINNQ 694
Cdd:COG2274 687 ----------IVEDGTHEELLA-RKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
53-687 |
2.84e-82 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 281.99 E-value: 2.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 53 HRKLLFISFVCAVLSGGTLPFFISVFGVILKNMNLGDDINPII---LSLVSIGLVQFILSMISSYCMDVITSKILKTLKL 129
Cdd:TIGR02203 12 YKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWwvpLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 130 EYLRSVFYQDGQFHDNNPGSKLRSDLDFYLEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVCG 209
Cdd:TIGR02203 92 RMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 210 VICNKKVK-LNKKTSLLyNNNTMSIIEEALMGIRTVASYCGEKTILNKFNLSETFYSKYILKANFVEALHIGLINGLILV 288
Cdd:TIGR02203 172 RRVSKRLRrISKEIQNS-MGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 289 SYAFgfwygtriIINSATNQypnnDFNGASVISILLGVLISMFMLTIILPNITE----YMKALEATNSLYEIINRKPlvE 364
Cdd:TIGR02203 251 ALAV--------VLFIALFQ----AQAGSLTAGDFTAFITAMIALIRPLKSLTNvnapMQRGLAAAESLFTLLDSPP--E 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 365 NNDDGETLPNIK-KIEFKNVRFHYDTRkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSH 443
Cdd:TIGR02203 317 KDTGTRAIERARgDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL-DGH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 444 NLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdleamenyyeentndtyenknfslisnsmtsnellemkkE 523
Cdd:TIGR02203 395 DLADYTLASLRRQVALVSQDVVLFNDTIANNIAYG--------------------------------------------R 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 524 YQTIKDSDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQK 603
Cdd:TIGR02203 431 TEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 604 TINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrersdnnnnnnnddnnnnnnnnnnkinnEGSYIIEQGTHDSLMkNK 683
Cdd:TIGR02203 511 ALERLM--QGRTTLVIAHRLSTIEKADRIVVM------------------------------DDGRIVERGTHNELL-AR 557
|
....
gi 124506379 684 NGIY 687
Cdd:TIGR02203 558 NGLY 561
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
828-1417 |
2.44e-80 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 276.58 E-value: 2.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 828 NKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFDqdKNTPGVLSAHINRDVHLLKTGLVNN 907
Cdd:TIGR02204 58 NRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVIGSS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 908 IVIFSHFIMLFLVSMVMSFYFCPIVAA-VLTFIYFINMRVFAVRARLTK-SKEiekkenmssgvfafSSDdeMFKDPSFL 985
Cdd:TIGR02204 136 LSMALRNALMCIGGLIMMFITSPKLTSlVLLAVPLVLLPILLFGRRVRKlSRE--------------SQD--RIADAGSY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 986 IQEAFYNMHTVINYGLEDY----FCNLIEKAIDYKNKGQKRRIIVNAALWGFSQSAQLFInsfaYWFGSFLIKRGTILVD 1061
Cdd:TIGR02204 200 AGETLGAIRTVQAFGHEDAersrFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGV----LWVGAHDVIAGKMSAG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1062 DFMKSLFTFIFTGSYAGKLMSLKGDSENAKLSFEKYYPLMIRKSniDVRDDGGIRINKNLIKGKVDIKDVNFRYISRPNV 1141
Cdd:TIGR02204 276 TLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEP--DIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQ 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1142 PIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDlkndhiilkndmtnfqdyqnnnnnslvlknvnefsNQSGSae 1221
Cdd:TIGR02204 354 PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYD-----------------------------------PQSGR-- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1222 dytvfnnngeILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVSKFAAIDEFIESLPNKY 1301
Cdd:TIGR02204 397 ----------ILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGY 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1302 DTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKI 1381
Cdd:TIGR02204 467 DTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETL--MKGRTTLIIAHRLATVLKADRI 544
|
570 580 590
....*....|....*....|....*....|....*.
gi 124506379 1382 VVFNnpdrNGTFVQShGTHDELLsAQDGIYKKYVKL 1417
Cdd:TIGR02204 545 VVMD----QGRIVAQ-GTHAELI-AKGGLYARLARL 574
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
378-687 |
3.01e-80 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 263.71 E-value: 3.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSKI 457
Cdd:cd03251 1 VEFKNVTFRYP-GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI-DGHDVRDYTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSNSIKNNIKYSlyslkdleamenyyeeNTNDTYEnknfslisnsmtsnellemkkeyqtikdsDVVDVSK 537
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIAYG----------------RPGATRE-----------------------------EVEEAAR 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 KVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITI 617
Cdd:cd03251 114 AANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM--KNRTTF 191
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 618 IIAHRLSTIRYANTIFVLSNRErsdnnnnnnnddnnnnnnnnnnkinnegsyIIEQGTHDSLMKnKNGIY 687
Cdd:cd03251 192 VIAHRLSTIENADRIVVLEDGK------------------------------IVERGTHEELLA-QGGVY 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1126-1414 |
1.19e-79 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 262.17 E-value: 1.19e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPNvPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDV------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnQSGSaedytvfnnngeILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVS 1285
Cdd:cd03251 55 ----------DSGR------------ILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIAYGRPGATREEVEEAA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1286 KFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDK--ADK 1363
Cdd:cd03251 113 RAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAAL----ERlmKNR 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 124506379 1364 TIITIAHRIASIKRSDKIVVFNnpdrNGTFVQsHGTHDELLsAQDGIYKKY 1414
Cdd:cd03251 189 TTFVIAHRLSTIENADRIVVLE----DGKIVE-RGTHEELL-AQGGVYAKL 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
58-689 |
1.02e-78 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 275.83 E-value: 1.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 58 FISFVCAVLSGGTLPFFIS-VFGVILKNMNLGDDINPI-ILSLVSIGlvQFILSMISSYCMDVITSKILKTLKLEYLRSV 135
Cdd:TIGR00958 167 FVFLTLSSLGEMFIPFYTGrVIDTLGGDKGPPALASAIfFMCLLSIA--SSVSAGLRGGSFNYTMARINLRIREDLFRSL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 136 FYQDGQFHDNNPGSKLRSDLDFYLEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVCGVICNKK 215
Cdd:TIGR00958 245 LRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKR 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 216 V-KLNKKT--SLLYNNNtmsIIEEALMGIRTVASYCGEKTILNKFN--LSETF---YSKYILKANFV---EALHIGLING 284
Cdd:TIGR00958 325 YqLLSEELqeAVAKANQ---VAEEALSGMRTVRSFAAEEGEASRFKeaLEETLqlnKRKALAYAGYLwttSVLGMLIQVL 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 285 LIlvsyafgfWYGTRIIINSAtnqypnndFNGASVISILL---------GVLISMFmltiilpniTEYMKALEATNSLYE 355
Cdd:TIGR00958 402 VL--------YYGGQLVLTGK--------VSSGNLVSFLLyqeqlgeavRVLSYVY---------SGMMQAVGASEKVFE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 356 IINRKPLVENNddGETLP-NIK-KIEFKNVRFHYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPT 433
Cdd:TIGR00958 457 YLDRKPNIPLT--GTLAPlNLEgLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 434 EGDIIVnDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdleameNYYEentndtyenknfslisnsmt 513
Cdd:TIGR00958 535 GGQVLL-DGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGL----------TDTP-------------------- 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 514 snellemkkeyqtikDSDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSL 593
Cdd:TIGR00958 584 ---------------DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 594 DNKSEYLVQktinNLKGNENRITIIIAHRLSTIRYANTIFVLsnrersdnnnnnnnddnnnnnnnnnnkinNEGSyIIEQ 673
Cdd:TIGR00958 649 DAECEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVL-----------------------------KKGS-VVEM 694
|
650
....*....|....*.
gi 124506379 674 GTHDSLMKNKNGIYHL 689
Cdd:TIGR00958 695 GTHKQLMEDQGCYKHL 710
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
378-694 |
1.11e-76 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 253.69 E-value: 1.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKdvEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSKI 457
Cdd:cd03253 1 IEFENVTFAYDPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI-DGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSNSIKNNIKYSlyslkdleamenyyeeNTNDTyenknfslisnsmtsnellemkkeyqtikDSDVVDVSK 537
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYG----------------RPDAT-----------------------------DEEVIEAAK 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 KVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITI 617
Cdd:cd03253 113 AAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTI 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 618 IIAHRLSTIRYANTIFVLSNrersdnnnnnnnddnnnnnnnnnnkinnegSYIIEQGTHDSLMkNKNGIYHLMINNQ 694
Cdd:cd03253 191 VIAHRLSTIVNADKIIVLKD------------------------------GRIVERGTHEELL-AKGGLYAEMWKAQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1124-1411 |
5.38e-75 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 262.06 E-value: 5.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1124 GKVDIKDVNFRYisRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnn 1203
Cdd:COG5265 356 GEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV----------------------- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1204 slvlknvnefsnqsgsaedytvfnNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKR 1283
Cdd:COG5265 411 ------------------------TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1284 VSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADK 1363
Cdd:COG5265 467 AARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV--ARGR 544
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 124506379 1364 TIITIAHRIASIKRSDKIVVFnnpdRNGTFVQsHGTHDELLsAQDGIY 1411
Cdd:COG5265 545 TTLVIAHRLSTIVDADEILVL----EAGRIVE-RGTHAELL-AQGGLY 586
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
326-694 |
1.29e-74 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 260.91 E-value: 1.29e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 326 VLISMFMLTIILP-NI--TEY--MK-ALEATNSLYEIINRKPLVENNDDGETLP-NIKKIEFKNVRFHYDTRKdvEIYKD 398
Cdd:COG5265 299 VLVNAYLIQLYIPlNFlgFVYreIRqALADMERMFDLLDQPPEVADAPDAPPLVvGGGEVRFENVSFGYDPER--PILKG 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 399 LSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYS 478
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI-DGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 479 lyslkDLEAmenyyeentndtyenknfslisnsmtsnellemkkeyqtiKDSDVVDVSKKVLIHDFVSSLPDKYDTLVGS 558
Cdd:COG5265 456 -----RPDA----------------------------------------SEEEVEAAARAAQIHDFIESLPDGYDTRVGE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 559 NASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnr 638
Cdd:COG5265 491 RGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA--RGRTTLVIAHRLSTIVDADEILVL--- 565
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 639 ersdnnnnnnnddnnnnnnnnnnkinnEGSYIIEQGTHDSLMKnKNGIYHLMINNQ 694
Cdd:COG5265 566 ---------------------------EAGRIVERGTHAELLA-QGGLYAQMWARQ 593
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1124-1409 |
3.96e-74 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 245.98 E-value: 3.96e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1124 GKVDIKDVNFRYisRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDlkndhiilkndmtnfqdyqnnnnn 1203
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD------------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1204 slvlknvnefsnqsgsaedytvfNNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKR 1283
Cdd:cd03254 55 -----------------------PQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLGRPNATDEEVIE 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1284 VSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDK 1363
Cdd:cd03254 112 AAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GR 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 124506379 1364 TIITIAHRIASIKRSDKIVVFNnpdrNGTFVQsHGTHDELLsAQDG 1409
Cdd:cd03254 190 TSIIIAHRLSTIKNADKILVLD----DGKIIE-EGTHDELL-AKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1126-1413 |
1.22e-72 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 242.14 E-value: 1.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:cd03253 1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDV------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnQSGSaedytvfnnngeILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVS 1285
Cdd:cd03253 54 ----------SSGS------------ILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1286 KFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTI 1365
Cdd:cd03253 112 KAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTT 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 124506379 1366 ITIAHRIASIKRSDKIVVFNnpdrNGTFVQShGTHDELLsAQDGIYKK 1413
Cdd:cd03253 190 IVIAHRLSTIVNADKIIVLK----DGRIVER-GTHEELL-AKGGLYAE 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
791-1415 |
6.32e-72 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 255.80 E-value: 6.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 791 IIFFSILVAGGLYPVFALLY-ARYVSTLF-DFAnleYNSNKYSIYIL-LIAIAMFISETLKNYYNNKIGEKVEKTMKRRL 867
Cdd:TIGR00958 164 ISAFVFLTLSSLGEMFIPFYtGRVIDTLGgDKG---PPALASAIFFMcLLSIASSVSAGLRGGSFNYTMARINLRIREDL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 868 FENILYQEMSFFDQDKNtpGVLSAHINRDVHLLKTGLVNNIVIFshfiMLFLVSMVMSFYFCPIVAAVLTFIYFINM--- 944
Cdd:TIGR00958 241 FRSLLRQDLGFFDENKT--GELTSRLSSDTQTMSRSLSLNVNVL----LRNLVMLLGLLGFMLWLSPRLTMVTLINLplv 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 945 ----RVFAVRARLTkSKEIEKKENMSSGVfafssddemfkdpsflIQEAFYNMHTVINYGLEDYFCNLIEKAIDYKNKGQ 1020
Cdd:TIGR00958 315 flaeKVFGKRYQLL-SEELQEAVAKANQV----------------AEEALSGMRTVRSFAAEEGEASRFKEALEETLQLN 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1021 KRRIIVNAALWGFSQSAQLFINSFAYWFGSFLIKRGTILVDDFMKSLFTFIFTGSYAGKLMSLKGDSENAKLSFEKYYPL 1100
Cdd:TIGR00958 378 KRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1101 MIRKSNIDvrDDGGIRiNKNLiKGKVDIKDVNFRYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDl 1180
Cdd:TIGR00958 458 LDRKPNIP--LTGTLA-PLNL-EGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1181 kndhiilkndmtnfqdyqnnnnnslvlknvnefsnqsgsaedytvfNNNGEILLDDINICDYNLRDLRNLFSIVSQEPML 1260
Cdd:TIGR00958 533 ----------------------------------------------PTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVL 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1261 FNMSIYENIKFGREDATLEDVKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1340
Cdd:TIGR00958 567 FSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 1341 SLDSNSEKLIEktivDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRNGTFVQShGTHDELLsAQDGIYKKYV 1415
Cdd:TIGR00958 647 ALDAECEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVL----KKGSVVEM-GTHKQLM-EDQGCYKHLV 711
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
377-685 |
2.27e-71 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 238.28 E-value: 2.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 377 KIEFKNVRFHYDtrKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSK 456
Cdd:cd03254 2 EIEFENVNFSYD--EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI-DGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSNSIKNNIKYSlyslkdleamenyyeentndtyenknfslisnsmtsnellemkkeYQTIKDSDVVDVS 536
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG---------------------------------------------RPNATDEEVIEAA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 537 KKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRIT 616
Cdd:cd03254 114 KEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL--MKGRTS 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 617 IIIAHRLSTIRYANTIFVLSNRErsdnnnnnnnddnnnnnnnnnnkinnegsyIIEQGTHDSLMKnKNG 685
Cdd:cd03254 192 IIIAHRLSTIKNADKILVLDDGK------------------------------IIEEGTHDELLA-KKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1126-1407 |
3.41e-70 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 246.98 E-value: 3.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPNVPiyKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYdlkndhiilkndmtnfQDYQnnnnnsl 1205
Cdd:COG4988 337 IELEDVSFSYPGGRPAL--DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL----------------PPYS------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnnnGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVS 1285
Cdd:COG4988 392 ------------------------GSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAAL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1286 KFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTI 1365
Cdd:COG4988 448 EAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTV 525
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 124506379 1366 ITIAHRIASIKRSDKIVVFNnpdrNGTFVQShGTHDELLSAQ 1407
Cdd:COG4988 526 ILITHRLALLAQADRILVLD----DGRIVEQ-GTHEELLAKN 562
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
344-683 |
1.31e-68 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 242.36 E-value: 1.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 344 MKALEATNSLYEIINR-KPLVENNDDGETLPNIKKIEFKNVRFHYDTRKdvEIYKDLSFTLKEGKTYAFVGESGCGKSTI 422
Cdd:COG4988 302 ANGIAAAEKIFALLDApEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 423 LKLIERLYDPTEGDIIVNDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdleamenyyeentndtyen 502
Cdd:COG4988 380 LNLLLGFLPPYSGSILING-VDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL--------------------------- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 503 knfsLISNSMTSnellemkkeyqtikDSDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPK 582
Cdd:COG4988 432 ----RLGRPDAS--------------DEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAP 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 583 ILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNRErsdnnnnnnnddnnnnnnnnnnk 662
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRLALLAQADRILVLDDGR----------------------- 548
|
330 340
....*....|....*....|.
gi 124506379 663 innegsyIIEQGTHDSLMKNK 683
Cdd:COG4988 549 -------IVEQGTHEELLAKN 562
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
834-1413 |
6.71e-68 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 240.69 E-value: 6.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 834 ILLIAIAMFISetlkNYYNNKIGEKVEKTMKRRLFENILYQEMSFFDQdkNTPGVLSAHINRD---VHLLKTGLVNNIV- 909
Cdd:PRK11176 75 MILRGITSFIS----SYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDK--QSTGTLLSRITYDseqVASSSSGALITVVr 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 910 ----IFSHFIMLFLVSMVMSfyfcpIVAAVLTFIYFINMRVFAVRARltkskEIEKKENMSSGVFAFSSDdEMFKDpsfl 985
Cdd:PRK11176 149 egasIIGLFIMMFYYSWQLS-----LILIVIAPIVSIAIRVVSKRFR-----NISKNMQNTMGQVTTSAE-QMLKG---- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 986 iqeafynmH-TVINYG---LE----DYFCNliekaiDYKNKGQKrriIVNAAlwGFSQSAQLFINSFAYWFGSFLIKrgt 1057
Cdd:PRK11176 214 --------HkEVLIFGgqeVEtkrfDKVSN------RMRQQGMK---MVSAS--SISDPIIQLIASLALAFVLYAAS--- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1058 ilVDDFMKSL----FTFIFTGSYAgkLMS-LKGDSeNAKLSFEK-------YYPLMIRKSNidvRDDGGIRINKnlIKGK 1125
Cdd:PRK11176 272 --FPSVMDTLtagtITVVFSSMIA--LMRpLKSLT-NVNAQFQRgmaacqtLFAILDLEQE---KDEGKRVIER--AKGD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRpNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:PRK11176 342 IEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI------------------------- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDA-TLEDVKRV 1284
Cdd:PRK11176 396 ----------------------DEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1285 SKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKT 1364
Cdd:PRK11176 454 ARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRT 531
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 124506379 1365 IITIAHRIASIKRSDKIVVFNnpdrNGTFVQsHGTHDELLsAQDGIYKK 1413
Cdd:PRK11176 532 SLVIAHRLSTIEKADEILVVE----DGEIVE-RGTHAELL-AQNGVYAQ 574
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
378-637 |
2.12e-67 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 224.57 E-value: 2.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLKWWRSKI 457
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG-VDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSNSIKNNIkyslyslkdleamenyyeentndtyenknfslisnsmtsnellemkkeyqtikdsdvvdvsk 537
Cdd:cd03228 79 AYVPQDPFLFSGTIRENI-------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 kvlihdfvsslpdkydtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGneNRITI 617
Cdd:cd03228 97 -------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVI 149
|
250 260
....*....|....*....|
gi 124506379 618 IIAHRLSTIRYANTIFVLSN 637
Cdd:cd03228 150 VIAHRLSTIRDADRIIVLDD 169
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
91-687 |
2.78e-67 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 238.83 E-value: 2.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 91 INPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYLRSVFYQDGQFHDNNPGSKLRSDLDFYLEQVSSGIGTKF 170
Cdd:TIGR02204 57 LNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 171 ITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVCGVICNKKVKLNKKTSLLYNNNTMSIIEEALMGIRTVASYCGE 250
Cdd:TIGR02204 137 SMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 251 KTILNKFNLS-ETFYsKYILKANFVEALHIGLINGLILVSYAFGFWYGTRIIINSAtnqypnndFNGASVISILLGVLIS 329
Cdd:TIGR02204 217 DAERSRFGGAvEKAY-EAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGK--------MSAGTLGQFVFYAVMV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 330 MFMLTIILPNITEYMKALEATNSLYEIINRKPLVENNDDGETLPN--IKKIEFKNVRFHYDTRKDVEIYKDLSFTLKEGK 407
Cdd:TIGR02204 288 AGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVplRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 408 TYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkDLEA 487
Cdd:TIGR02204 368 TVALVGPSGAGKSTLFQLLLRFYDPQSGRILL-DGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG-----RPDA 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 488 menyyeentndtyenknfslisnsmtsnellemkkeyqtiKDSDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQ 567
Cdd:TIGR02204 442 ----------------------------------------TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 568 KQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNRErsdnnnnn 647
Cdd:TIGR02204 482 RQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLM--KGRTTLIIAHRLATVLKADRIVVMDQGR-------- 551
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 124506379 648 nnddnnnnnnnnnnkinnegsyIIEQGTHDSLMKnKNGIY 687
Cdd:TIGR02204 552 ----------------------IVAQGTHAELIA-KGGLY 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
94-687 |
4.08e-65 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 232.60 E-value: 4.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 94 IILSLVSIGL--VQFILSMISSYCMDVITSKILKTLKLEYLRSVFYQDGQFHDNNPGSKLRSDLDFYLEQVSSGIGTKFI 171
Cdd:PRK11176 65 KWMPLVVIGLmiLRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 172 TIFTYASSFLGLYIWSLIKNARLTLCITCVFPLI-YVCGVICNKKVKLNKKTsllynNNTM----SIIEEALMGIRTVAS 246
Cdd:PRK11176 145 TVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVsIAIRVVSKRFRNISKNM-----QNTMgqvtTSAEQMLKGHKEVLI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 247 YCGEKTILNKFNLSETFYSKYILK---ANFVEALHIGLINGLIL--VSYAFGFwygtRIIINSATnqypnndfngASVIS 321
Cdd:PRK11176 220 FGGQEVETKRFDKVSNRMRQQGMKmvsASSISDPIIQLIASLALafVLYAASF----PSVMDTLT----------AGTIT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 322 IllgVLISMFMLTIILPNIT----EYMKALEATNSLYEIINRKPlvENNDDGETLPNIK-KIEFKNVRFHYDTrKDVEIY 396
Cdd:PRK11176 286 V---VFSSMIALMRPLKSLTnvnaQFQRGMAACQTLFAILDLEQ--EKDEGKRVIERAKgDIEFRNVTFTYPG-KEVPAL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIK 476
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-DGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIA 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 477 YSlyslkdleamenyyeenTNDTYenknfslisnsmtSNEllemkkeyqtikdsDVVDVSKKVLIHDFVSSLPDKYDTLV 556
Cdd:PRK11176 439 YA-----------------RTEQY-------------SRE--------------QIEEAARMAYAMDFINKMDNGLDTVI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 557 GSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLs 636
Cdd:PRK11176 475 GENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEKADEILVV- 551
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 124506379 637 nrersdnnnnnnnddnnnnnnnnnnkinnEGSYIIEQGTHDSLMkNKNGIY 687
Cdd:PRK11176 552 -----------------------------EDGEIVERGTHAELL-AQNGVY 572
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
778-1411 |
3.11e-64 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 229.60 E-value: 3.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 778 IYKEIFSYKKDVTIIFFSILVAGGLY----PVFALLYARYVSTLFDFANLEYNSNKYSIYILLIA---IAMFISetlkNY 850
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVaateSTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVlrgICSFVS----TY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 851 YNNKIGEKVEKTMKRRLFENILYQEMSFFDqdKNTPGVLSAHINRDVH--------LLKTGLVNNIVIFSHFIMLFLVSM 922
Cdd:TIGR02203 77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEqvasaatdAFIVLVRETLTVIGLFIVLLYYSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 923 VMSFyfcpIVAAVLTFIYFInMRVFAVRARlTKSKEIEKkenmssgvfafssddeMFKDPSFLIQEAFYNMHTVINYGLE 1002
Cdd:TIGR02203 155 QLTL----IVVVMLPVLSIL-MRRVSKRLR-RISKEIQN----------------SMGQVTTVAEETLQGYRVVKLFGGQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1003 DYFCNLIEkAIDYKNKGQKRRIIVNAALwgFSQSAQLFIN---SFAYWFGSFLIKRGTILVDDFMKSLFTFIFTGSYAGK 1079
Cdd:TIGR02203 213 AYETRRFD-AVSNRNRRLAMKMTSAGSI--SSPITQLIASlalAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1080 LMSLKGDSENAKLSFEKYYPLMirkSNIDVRDDGGIRINKnlIKGKVDIKDVNFRYISRpNVPIYKNLSFTCDSKKTTAI 1159
Cdd:TIGR02203 290 LTNVNAPMQRGLAAAESLFTLL---DSPPEKDTGTRAIER--ARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVAL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1160 VGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnnslvlknvnefsnqsgsaedytvfnNNGEILLDDINI 1239
Cdd:TIGR02203 364 VGRSGSGKSTLVNLIPRFYEP-----------------------------------------------DSGQILLDGHDL 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1240 CDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGR-EDATLEDVKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQ 1318
Cdd:TIGR02203 397 ADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQ 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1319 RIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNnpdrNGTFVQsHG 1398
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMD----DGRIVE-RG 549
|
650
....*....|...
gi 124506379 1399 THDELLsAQDGIY 1411
Cdd:TIGR02203 550 THNELL-ARNGLY 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1126-1386 |
6.27e-63 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 211.86 E-value: 6.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPNvPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDlkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD-------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfNNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIkfgredatledvkrvs 1285
Cdd:cd03228 54 ---------------------PTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIRENI---------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1286 kfaaidefieslpnkydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTI 1365
Cdd:cd03228 97 --------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTV 148
|
250 260
....*....|....*....|.
gi 124506379 1366 ITIAHRIASIKRSDKIVVFNN 1386
Cdd:cd03228 149 IVIAHRLSTIRDADRIIVLDD 169
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1126-1417 |
2.96e-61 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 220.79 E-value: 2.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPNvPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:COG4987 334 LELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP------------------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVS 1285
Cdd:COG4987 388 ----------------------QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAAL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1286 KFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTI 1365
Cdd:COG4987 446 ERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA--LAGRTV 523
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 124506379 1366 ITIAHRIASIKRSDKIVVFnnpdRNGTFVQShGTHDELLsAQDGIYKKYVKL 1417
Cdd:COG4987 524 LLITHRLAGLERMDRILVL----EDGRIVEQ-GTHEELL-AQNGRYRQLYQR 569
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1108-1419 |
1.46e-60 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 219.45 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1108 DVRDDGGIRINKNLiKGKVDIKDVNFRYI-SRPNVpiyKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDlkndhii 1186
Cdd:PRK13657 318 DVRDPPGAIDLGRV-KGAVEFDDVSFSYDnSRQGV---EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1187 lkndmtnfqdyqnnnnnslvlknvnefsNQSGSaedytvfnnngeILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIY 1266
Cdd:PRK13657 387 ----------------------------PQSGR------------ILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1267 ENIKFGREDATLEDVKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1346
Cdd:PRK13657 427 DNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124506379 1347 EKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNnpdrNGTFVQShGTHDElLSAQDGiykKYVKLAK 1419
Cdd:PRK13657 507 EAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFD----NGRVVES-GSFDE-LVARGG---RFAALLR 568
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
377-635 |
2.17e-60 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 206.55 E-value: 2.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 377 KIEFKNVRFHYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSK 456
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL-DGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSNSIKNNIKYSLyslkdleamenyyeentndtyenknfslisnsmtsnellemkkeyQTIKDSDVVDVS 536
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGL---------------------------------------------QSCSFECVKEAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 537 KKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNlkGNENRIT 616
Cdd:cd03248 125 QKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD--WPERRTV 202
|
250
....*....|....*....
gi 124506379 617 IIIAHRLSTIRYANTIFVL 635
Cdd:cd03248 203 LVIAHRLSTVERADQILVL 221
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
57-353 |
8.47e-60 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 207.71 E-value: 8.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 57 LFISFVCAVLSGGTLPFFISVFGVILKNMN-----------LGDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILK 125
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsgesspdeFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 126 TLKLEYLRSVFYQDGQFHDNNPGSKLRSDLDFYLEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLI 205
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 206 YVCGVICNKKVKLNKKTSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNKFN--LSETfySKYILKANFVEALHIGLIN 283
Cdd:cd18577 161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSkaLEKA--RKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 284 GLILVSYAFGFWYGTRIIInsatnqypNNDFNGASVISILLGVLISMFMLTIILPNITEYMKALEATNSL 353
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVR--------DGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1122-1383 |
3.31e-59 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 203.47 E-value: 3.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1122 IKGKVDIKDVNFRYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNdhiilkndmtnfqdyqnnn 1201
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQG------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1202 nnslvlknvnefsnqsgsaedytvfnnnGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDV 1281
Cdd:cd03248 69 ----------------------------GQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1282 KRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikDKA 1361
Cdd:cd03248 121 KEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD--WPE 198
|
250 260
....*....|....*....|..
gi 124506379 1362 DKTIITIAHRIASIKRSDKIVV 1383
Cdd:cd03248 199 RRTVLVIAHRLSTVERADQILV 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
378-694 |
1.94e-58 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 201.56 E-value: 1.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYdtRKD-VEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSK 456
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV-DGHDLALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSNSIKNNIkyslySLKDlEAMEnyyeentndtyenknfslisnsmtsnelleMKKeyqtikdsdVVDVS 536
Cdd:cd03252 78 VGVVLQENVLFNRSIRDNI-----ALAD-PGMS------------------------------MER---------VIEAA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 537 KKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRIT 616
Cdd:cd03252 113 KLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDI--CAGRTV 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 617 IIIAHRLSTIRYANTIFVLsnrersdnnnnnnnddnnnnnnnnnnkinnEGSYIIEQGTHDSLMKnKNGIYHLMINNQ 694
Cdd:cd03252 191 IIIAHRLSTVKNADRIIVM------------------------------EKGRIVEQGSHDELLA-ENGLYAYLYQLQ 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
315-690 |
1.25e-57 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 210.01 E-value: 1.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 315 NGASVISILL------------GVLISMFMLTII--------LPN-ITEYMKALEATNSLYEIINRKPLVENNDDGETLP 373
Cdd:COG4987 250 AGLAVVAVLWlaaplvaagalsGPLLALLVLAALalfealapLPAaAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 374 NIKKIEFKNVRFHYDTRkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLKWW 453
Cdd:COG4987 330 GGPSLELEDVSFRYPGA-GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG-VDLRDLDEDDL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 454 RSKIGVVSQDPLLFSNSIKNNIKyslysLKDLEAmenyyeentndtyenknfslisnsmtsnellemkkeyqtiKDSDVV 533
Cdd:COG4987 408 RRRIAVVPQRPHLFDTTLRENLR-----LARPDA----------------------------------------TDEELW 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 DVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTInnLKGNEN 613
Cdd:COG4987 443 AALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL--LEALAG 520
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 614 RITIIIAHRLSTIRYANTIFVLSNRErsdnnnnnnnddnnnnnnnnnnkinnegsyIIEQGTHDSLMKNKNGIYHLM 690
Cdd:COG4987 521 RTVLLITHRLAGLERMDRILVLEDGR------------------------------IVEQGTHEELLAQNGRYRQLY 567
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
792-1107 |
2.55e-57 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 201.14 E-value: 2.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 792 IFFSIlVAGGLYPVFALLYARYVSTLF--DFANLEYNSNKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFE 869
Cdd:cd18578 15 LIGAI-IAGAVFPVFAILFSKLISVFSlpDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 870 NILYQEMSFFDQDKNTPGVLSAHINRDVHLLKTGLVNNIVIFSHFIMLFLVSMVMSFYFCPIVAAV-LTFIYFInmrVFA 948
Cdd:cd18578 94 AILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVgLATVPLL---LLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 949 VRARLTKSKEIEKKENmssgvfafssddEMFKDPSFLIQEAFYNMHTVINYGLEDYFCNLIEKAIDYKNKGQKRRIIVNA 1028
Cdd:cd18578 171 GYLRMRLLSGFEEKNK------------KAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 1029 ALWGFSQSAQLFINSFAYWFGSFLIKRGTILVDDFMKSLFTFIFTGSYAGKLMSLKGDSENAKLSFEKYYPLMIRKSNI 1107
Cdd:cd18578 239 LGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
353-637 |
3.16e-57 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 209.43 E-value: 3.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 353 LYEIINRKPLVENNDDGETLPNIK-KIEFKNVRFHYD-TRKDVEiykDLSFTLKEGKTYAFVGESGCGKSTILKLIERLY 430
Cdd:PRK13657 309 FFEVEDAVPDVRDPPGAIDLGRVKgAVEFDDVSFSYDnSRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 431 DPTEGDIIVnDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKyslyslkdleamenyyeentndtyenknfslisn 510
Cdd:PRK13657 386 DPQSGRILI-DGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR---------------------------------- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 511 smtsnelleMKKEYQTikDSDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEAT 590
Cdd:PRK13657 431 ---------VGRPDAT--DEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 124506379 591 SSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN 637
Cdd:PRK13657 500 SALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRNADRILVFDN 544
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
40-694 |
5.14e-54 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 202.28 E-value: 5.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 40 ISFFLP-FKCLPAQHRKLLFISFVCAVLSGGTLPFFISVFGVILKNMNLgDDINPIILSLVSIGLVQFILSMISSYCMDV 118
Cdd:TIGR01846 127 FSWFIPaIIRYRKQFREVLLISLALQLFALVTPLLFQVVIDKVLVHRGL-STLSVLALAMLAVAIFEPALGGLRTYLFAH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 119 ITSKI-----------LKTLKLEYLRSVFYQD--------GQFHDNNPGSKLRSDLDFYLEQVssgigtkFITI-FTYAS 178
Cdd:TIGR01846 206 LTSRIdvelgarlyrhLLGLPLGYFESRRVGDtvarvrelEQIRNFLTGSALTVVLDLLFVVV-------FLAVmFFYSP 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 179 SFLGLYIWSLIknarltlcitCVFPLIYVCGVICNKKVKLNKKTSllynNNTMSIIEEALMGIRTVASYCGEKTILNKFN 258
Cdd:TIGR01846 279 TLTGVVIGSLV----------CYALLSVFVGPILRKRVEDKFERS----AAATSFLVESVTGIETIKATATEPQFQNRWD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 259 LSETFY---SKYILKANFVEALHIGLINGLilvSYAFGFWYGTRIIINSAtnqypnndfngasvISILLGVLISMFMLTI 335
Cdd:TIGR01846 345 RQLAAYvaaSFRVTNLGNIAGQAIELIQKL---TFAILLWFGAHLVIGGA--------------LSPGQLVAFNMLAGRV 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 336 ILPNI------TEYMKALEATNSLYEIINRKplVENNDDGE-TLPNIK-KIEFKNVRFHYDtRKDVEIYKDLSFTLKEGK 407
Cdd:TIGR01846 408 TQPVLrlaqlwQDFQQTGIALERLGDILNSP--TEPRSAGLaALPELRgAITFENIRFRYA-PDSPEVLSNLNLDIKPGE 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 408 TYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKyslyslkdlea 487
Cdd:TIGR01846 485 FIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLV-DGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIA----------- 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 488 menyyeentndtyenknfslISNSMTSNEllemkkeyqtikdsDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQ 567
Cdd:TIGR01846 553 --------------------LCNPGAPFE--------------HVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQ 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 568 KQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIRYANTIFVLsnrersdnnnnn 647
Cdd:TIGR01846 599 RQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREI--CRGRTVIIIAHRLSTVRACDRIIVL------------ 664
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 124506379 648 nnddnnnnnnnnnnkinnEGSYIIEQGTHDSLMKnKNGIYHLMINNQ 694
Cdd:TIGR01846 665 ------------------EKGQIAESGRHEELLA-LQGLYARLWQQQ 692
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1124-1386 |
5.53e-53 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 185.39 E-value: 5.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1124 GKVDIKDVNFRYisRPN-VPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnn 1202
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1203 nslvlknvnefsnqsgsaedytvfnNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIK-FGRedATLEDV 1281
Cdd:cd03244 57 -------------------------SSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLDpFGE--YSDEEL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1282 KRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTivdIKDK- 1360
Cdd:cd03244 110 WQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKT---IREAf 186
|
250 260
....*....|....*....|....*.
gi 124506379 1361 ADKTIITIAHRIASIKRSDKIVVFNN 1386
Cdd:cd03244 187 KDCTVLTIAHRLDTIIDSDRILVLDK 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1126-1417 |
5.27e-51 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 180.37 E-value: 5.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisRPNVP-IYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYdlkndhiilkndmtnfqdyqnnnnns 1204
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY-------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1205 lvlknVNEfsnqsgsaedytvfnnNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRV 1284
Cdd:cd03252 53 -----VPE----------------NGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDNIALADPGMSMERVIEA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1285 SKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKT 1364
Cdd:cd03252 112 AKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDI--CAGRT 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 124506379 1365 IITIAHRIASIKRSDKIVVFNnpdrNGTFVQShGTHDELLSAQdGIYKKYVKL 1417
Cdd:cd03252 190 VIIIAHRLSTVKNADRIIVME----KGRIVEQ-GSHDELLAEN-GLYAYLYQL 236
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
834-1413 |
1.18e-50 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 191.88 E-value: 1.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 834 ILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFDQDKNTPGVLSAHINRDVHLLKTGLVNNIVIFSH 913
Cdd:TIGR01846 185 MLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRELEQIRNFLTGSALTVVLDLL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 914 FIMLFLVSMvmsFYFCPIVAAVLTF---IYFinMRVFAVRARLtkSKEIEKKenmssgvFAFSSDDEmfkdpSFLIqEAF 990
Cdd:TIGR01846 265 FVVVFLAVM---FFYSPTLTGVVIGslvCYA--LLSVFVGPIL--RKRVEDK-------FERSAAAT-----SFLV-ESV 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 991 YNMHTVINYGLEDYFCNLIEKAI-DYKNKGQKrriIVNAALWGfSQSAQLfIN--SFA--YWFGSFLIKRGTILVDdfmk 1065
Cdd:TIGR01846 325 TGIETIKATATEPQFQNRWDRQLaAYVAASFR---VTNLGNIA-GQAIEL-IQklTFAilLWFGAHLVIGGALSPG---- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1066 SLFTF-IFTGSYAG---KLMSLKGDSENAKLSFEKYYPlmIRKSNIDVRDDGGIRINKnlIKGKVDIKDVNFRYisRPNV 1141
Cdd:TIGR01846 396 QLVAFnMLAGRVTQpvlRLAQLWQDFQQTGIALERLGD--ILNSPTEPRSAGLAALPE--LRGAITFENIRFRY--APDS 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1142 P-IYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYdlkndhiilkndmtnfqdyqnnnnnslvlknvnefsnqsgsa 1220
Cdd:TIGR01846 470 PeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLY------------------------------------------ 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1221 edytvFNNNGEILLD--DINICDYNLrdLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVSKFAAIDEFIESLP 1298
Cdd:TIGR01846 508 -----TPQHGQVLVDgvDLAIADPAW--LRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELP 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1299 NKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRS 1378
Cdd:TIGR01846 581 QGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREI--CRGRTVIIIAHRLSTVRAC 658
|
570 580 590
....*....|....*....|....*....|....*
gi 124506379 1379 DKIVVFNnpdrNGTFVQShGTHDELLsAQDGIYKK 1413
Cdd:TIGR01846 659 DRIIVLE----KGQIAES-GRHEELL-ALQGLYAR 687
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
57-324 |
1.31e-50 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 180.53 E-value: 1.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 57 LFISFVCAVLSGGTLPFFISVFGVILKNMNLGDD-----INPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEY 131
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDpetqaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 132 LRSVFYQDGQFHDNNPGSKLRSDLDFYLEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVCGVI 211
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 212 CNKKVKLNKKTSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNKFNLSETFYSKYILKANFVEALHIGLINGLILVSYA 291
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|...
gi 124506379 292 FGFWYGTRIIINsatNQYPNNDFNGASVISILL 324
Cdd:pfam00664 241 LALWFGAYLVIS---GELSVGDLVAFLSLFAQL 270
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1124-1386 |
1.09e-48 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 172.77 E-value: 1.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1124 GKVDIKDVNFRYisrPNVPI--YKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDlkndhiilkndmtnfqdyqnnn 1201
Cdd:cd03245 1 GRIEFRNVSFSY---PNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK---------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1202 nnslvlknvnefsNQSGSaedytvfnnngeILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDV 1281
Cdd:cd03245 56 -------------PTSGS------------VLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNITLGAPLADDERI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1282 KRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE-KLIEKtivdIKD- 1359
Cdd:cd03245 111 LRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEeRLKER----LRQl 186
|
250 260
....*....|....*....|....*..
gi 124506379 1360 KADKTIITIAHRIASIKRSDKIVVFNN 1386
Cdd:cd03245 187 LGDKTLIIITHRPSLLDLVDRIIVMDS 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
344-635 |
5.89e-48 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 180.56 E-value: 5.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 344 MKALEATNSLYEIINRKPLVENNDDGETLPNIKKIEFKNVRFHYDTRKDVeiYKDLSFTLKEGKTYAFVGESGCGKSTIL 423
Cdd:TIGR02857 288 ADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 424 KLIERLYDPTEGDIIVNDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKyslysLKDLEAmenyyeentndtyenk 503
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGV-PLADADADSWRDQIAWVPQHPFLFAGTIAENIR-----LARPDA---------------- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 504 nfslisnsmtsnellemkkeyqtiKDSDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKI 583
Cdd:TIGR02857 424 ------------------------SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 124506379 584 LILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 635
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
789-1073 |
1.72e-47 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 171.29 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 789 VTIIFFSILVAGGLYPVFALLYARYVSTLFDFANLEYN-SNKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRL 867
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 868 FENILYQEMSFFDQdkNTPGVLSAHINRDVHLLKTGLVNNIVIFSHFIMLFLVSMVMSFYFCPIVAAVLTFIYFINMRVF 947
Cdd:pfam00664 81 FKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 948 AVRARLTKSKEIEKKENMSsgvfafssddemfkDPSFLIQEAFYNMHTVINYGLEDYFCNLIEKAIDYKNKGQKRRIIVN 1027
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVA--------------KASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVAN 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 124506379 1028 AALWGFSQSAQLFINSFAYWFGSFLIKRGTILVDDF--MKSLFTFIFT 1073
Cdd:pfam00664 225 GLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLvaFLSLFAQLFG 272
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
364-687 |
5.80e-47 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 180.91 E-value: 5.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 364 ENNDDGETLPNIK---KIEFKNVRFHYdTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVn 440
Cdd:TIGR03796 461 PEGSAATSEPPRRlsgYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILF- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 441 DSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslySLKDleamenyyeentndtyenknfslisnsmtsnellem 520
Cdd:TIGR03796 539 DGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNL-----TLWD------------------------------------ 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 521 kkeyQTIKDSDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYL 600
Cdd:TIGR03796 578 ----PTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKI 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 601 VqktINNLKgneNR--ITIIIAHRLSTIRYANTIFVLsnrERSDnnnnnnnddnnnnnnnnnnkinnegsyIIEQGTHDS 678
Cdd:TIGR03796 654 I---DDNLR---RRgcTCIIVAHRLSTIRDCDEIIVL---ERGK---------------------------VVQRGTHEE 697
|
....*....
gi 124506379 679 LMkNKNGIY 687
Cdd:TIGR03796 698 LW-AVGGAY 705
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
377-635 |
5.54e-46 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 165.07 E-value: 5.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 377 KIEFKNVRFHYDTRKDVEIyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSK 456
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL-DGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSNSIKNNIKYSlyslkdleamenyyeentndtyenknfslisnsmtsnellemkkeYQTIKDSDVVDVS 536
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLG---------------------------------------------APLADDERILRAA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 537 KKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGneNRIT 616
Cdd:cd03245 115 ELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTL 192
|
250
....*....|....*....
gi 124506379 617 IIIAHRLSTIRYANTIFVL 635
Cdd:cd03245 193 IIITHRPSLLDLVDRIIVM 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
377-637 |
5.71e-46 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 164.97 E-value: 5.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 377 KIEFKNVRFHYdtRKDVE-IYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRS 455
Cdd:cd03244 2 DIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI-DGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 456 KIGVVSQDPLLFSNSIKNNIK-YSLYSlkdleamenyyeentndtyenknfslisnsmtsnellemkkeyqtikDSDVVD 534
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDpFGEYS-----------------------------------------------DEELWQ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 535 VSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTI-NNLKgneN 613
Cdd:cd03244 112 ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFK---D 188
|
250 260
....*....|....*....|....
gi 124506379 614 RITIIIAHRLSTIRYANTIFVLSN 637
Cdd:cd03244 189 CTVLTIAHRLDTIIDSDRILVLDK 212
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
53-361 |
8.73e-46 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 168.01 E-value: 8.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 53 HRKLLFISFVCAVLSGGTLPFFISVFGVILKNMNLGDD------INPIILSLVSIGLVQFILSMISSYCMDVITSKILKT 126
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDdelrseANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 127 LKLEYLRSVFYQDGQFHD---NNPGSkLRSDLDFYLEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFP 203
Cdd:cd18578 87 LRKLAFRAILRQDIAWFDdpeNSTGA-LTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 204 LIYVCGVIcnkKVKLNKKTSLLYNN---NTMSIIEEALMGIRTVASYCGEKTILNKFN--LSETFysKYILKANFVEALH 278
Cdd:cd18578 166 LLLLAGYL---RMRLLSGFEEKNKKayeESSKIASEAVSNIRTVASLTLEDYFLEKYEeaLEEPL--KKGLRRALISGLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 279 IGLINGLILVSYAFGFWYGTRIIInsatnqypNNDFNGASVISILLGVLISMFMLTIILPNITEYMKALEATNSLYEIIN 358
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVA--------NGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLD 312
|
...
gi 124506379 359 RKP 361
Cdd:cd18578 313 RKP 315
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1126-1383 |
8.69e-45 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 170.93 E-value: 8.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPNVPiyKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydlkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPAL--RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF---------------------------- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsAEDYTvfnnnGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVS 1285
Cdd:TIGR02857 372 --------------VDPTE-----GSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREAL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1286 KFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTI 1365
Cdd:TIGR02857 433 ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTV 510
|
250
....*....|....*...
gi 124506379 1366 ITIAHRIASIKRSDKIVV 1383
Cdd:TIGR02857 511 LLVTHRLALAALADRIVV 528
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
368-635 |
1.69e-43 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 168.53 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 368 DGETLPNIK-KIEFKNVRFHY-DTRKDVeiyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNL 445
Cdd:TIGR01192 324 DAPELPNVKgAVEFRHITFEFaNSSQGV---FDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILI-DGIDI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 446 KDINLKWWRSKIGVVSQDPLLFSNSIKNNIKyslyslkdleamenyyeentndtyenknfslisnsmtsnelleMKKEYQ 525
Cdd:TIGR01192 400 NTVTRESLRKSIATVFQDAGLFNRSIRENIR-------------------------------------------LGREGA 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 526 TikDSDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTI 605
Cdd:TIGR01192 437 T--DEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAI 514
|
250 260 270
....*....|....*....|....*....|
gi 124506379 606 NNLKgnENRITIIIAHRLSTIRYANTIFVL 635
Cdd:TIGR01192 515 DALR--KNRTTFIIAHRLSTVRNADLVLFL 542
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
201-1415 |
2.47e-43 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 173.62 E-value: 2.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 201 VFPLIYVCGVICNKKVKLNKKtSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNKFNLSETFYSKYILKANFVEALHIG 280
Cdd:PLN03232 450 LFLLIPLQTLIVRKMRKLTKE-GLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSF 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 281 LINGLILVSYAFGFwyGTRIIINSatNQYPNNDFNGASVISILLGVLiSMfmltiiLPNITEymKALEATNSLYEI---- 356
Cdd:PLN03232 529 ILNSIPVVVTLVSF--GVFVLLGG--DLTPARAFTSLSLFAVLRSPL-NM------LPNLLS--QVVNANVSLQRIeell 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 357 INRKPLVENNDDGEtlPNIKKIEFKNVRFHYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGD 436
Cdd:PLN03232 596 LSEERILAQNPPLQ--PGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 437 IIVndshnlkdinlkwWRSKIGVVSQDPLLFSNSIKNNIKYSlyslKDLEAmENYYEentndtyenknfslisnsmtsne 516
Cdd:PLN03232 674 SVV-------------IRGSVAYVPQVSWIFNATVRENILFG----SDFES-ERYWR----------------------- 712
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 517 llemkkeyqtikdsdVVDVSkkVLIHDfVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNK 596
Cdd:PLN03232 713 ---------------AIDVT--ALQHD-LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 597 SEYLVQKTI--NNLKGnenRITIIIAHRLSTIRYANTIFVLSnrersdnnnnnnnddnnnnnnnnnnkinnEGsYIIEQG 674
Cdd:PLN03232 775 VAHQVFDSCmkDELKG---KTRVLVTNQLHFLPLMDRIILVS-----------------------------EG-MIKEEG 821
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 675 THDSLMKNKNGIYHLMINNQKISSNKssnngndngsdnkssaykdsDTGNDADNMNSLSIHENENISNnRNCKNTAENeK 754
Cdd:PLN03232 822 TFAELSKSGSLFKKLMENAGKMDATQ--------------------EVNTNDENILKLGPTVTIDVSE-RNLGSTKQG-K 879
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 755 EEKVPFFKRMFRRKKKAPNNLRIIYKEIFSYKKDVTIIFFSILvaggLYPVFALLYARYVSTLFDFANLEYNSNKYsiYI 834
Cdd:PLN03232 880 RGRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYL----TTEVLRVSSSTWLSIWTDQSTPKSYSPGF--YI 953
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 835 LLIAIAMF--ISETLKN-YYNNKIGEKVEKTMKRRLFENILYQEMSFFDqdKNTPGVLSAHINRDVHLLKTGLVNNIVIF 911
Cdd:PLN03232 954 VVYALLGFgqVAVTFTNsFWLISSSLHAAKRLHDAMLNSILRAPMLFFH--TNPTGRVINRFSKDIGDIDRNVANLMNMF 1031
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 912 --------SHFIMLFLVSMVMSFYFCPIVAAVL-TFIYFINMrvfavrarltkSKEIEKKENMS-SGVFAfssddemfkd 981
Cdd:PLN03232 1032 mnqlwqllSTFALIGTVSTISLWAIMPLLILFYaAYLYYQST-----------SREVRRLDSVTrSPIYA---------- 1090
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 982 psfLIQEAFYNMHTVINYGLEDYFCNLIEKAIDyknkGQKRRIIVNAALWGFSQSAQLFINSFAYWF-GSF-LIKRGTIL 1059
Cdd:PLN03232 1091 ---QFGEALNGLSSIRAYKAYDRMAKINGKSMD----NNIRFTLANTSSNRWLTIRLETLGGVMIWLtATFaVLRNGNAE 1163
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1060 VDDFMKSLFTFIFtgSYAGKLMSL-------KGDSENAKLSFEkyyplmiRKSN-IDVRDDGGIRINKNL------IKGK 1125
Cdd:PLN03232 1164 NQAGFASTMGLLL--SYTLNITTLlsgvlrqASKAENSLNSVE-------RVGNyIDLPSEATAIIENNRpvsgwpSRGS 1234
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisRPNVP-IYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNdhiilkndmtnfqdyqnnnnns 1204
Cdd:PLN03232 1235 IKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEK---------------------- 1290
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1205 lvlknvnefsnqsgsaedytvfnnnGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGRE--DATL-EDV 1281
Cdd:PLN03232 1291 -------------------------GRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEhnDADLwEAL 1345
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1282 KRvskfAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikDKA 1361
Cdd:PLN03232 1346 ER----AHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFK 1419
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|....
gi 124506379 1362 DKTIITIAHRIASIKRSDKIVVFNNPDrngtfVQSHGTHDELLSAQDGIYKKYV 1415
Cdd:PLN03232 1420 SCTMLVIAHRLNTIIDCDKILVLSSGQ-----VLEYDSPQELLSRDTSAFFRMV 1468
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
321-635 |
3.31e-43 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 167.20 E-value: 3.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 321 SILLGVLIS--MFMLTIILP--------NITEYMKAleATNSLYEIINRKPLVenNDDGETLPNIKKIEFKNVR-FHYDT 389
Cdd:PRK10789 250 SLTLGQLTSfvMYLGLMIWPmlalawmfNIVERGSA--AYSRIRAMLAEAPVV--KDGSEPVPEGRGELDVNIRqFTYPQ 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 390 rKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLKWWRSKIGVVSQDPLLFSN 469
Cdd:PRK10789 326 -TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD-IPLTKLQLDSWRSRLAVVSQTPFLFSD 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 470 SIKNNIkyslySLKDLEAMENYYEEntndtyenknfslisnsmtsnellemkkeyqtikdsdvvdVSKKVLIHDFVSSLP 549
Cdd:PRK10789 404 TVANNI-----ALGRPDATQQEIEH----------------------------------------VARLASVHDDILRLP 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 550 DKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYlvqKTINNLKG-NENRITIIIAHRLSTIRY 628
Cdd:PRK10789 439 QGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH---QILHNLRQwGEGRTVIISAHRLSALTE 515
|
....*..
gi 124506379 629 ANTIFVL 635
Cdd:PRK10789 516 ASEILVM 522
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1145-1412 |
8.47e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 166.17 E-value: 8.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydlkndhiiLKndmtnfqdYQnnnnnslvlknvnefsnqsgsaedyt 1224
Cdd:PRK11174 367 GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF---------LP--------YQ-------------------------- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1225 vfnnnGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVSKFAAIDEFIESLPNKYDTN 1304
Cdd:PRK11174 404 -----GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTP 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1305 VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVF 1384
Cdd:PRK11174 479 IGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHQLEDLAQWDQIWVM 556
|
250 260
....*....|....*....|....*...
gi 124506379 1385 nnpdRNGTFVQsHGTHDElLSAQDGIYK 1412
Cdd:PRK11174 557 ----QDGQIVQ-QGDYAE-LSQAGGLFA 578
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1130-1412 |
3.09e-42 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 164.12 E-value: 3.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1130 DVNFRYISRP--NVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnnslvl 1207
Cdd:PRK10789 315 DVNIRQFTYPqtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV--------------------------- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqsgsaedytvfnNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVSKF 1287
Cdd:PRK10789 368 --------------------SEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARL 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1288 AAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKadKTIIT 1367
Cdd:PRK10789 428 ASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVII 505
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 124506379 1368 IAHRIASIKRSDKIVVFNnpdrNGTFVQsHGTHDElLSAQDGIYK 1412
Cdd:PRK10789 506 SAHRLSALTEASEILVMQ----HGHIAQ-RGNHDQ-LAQQSGWYR 544
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
396-591 |
6.44e-42 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 150.88 E-value: 6.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 396 YKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLKWWRSKIGVVSQDPLLFSN-SIKNN 474
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDG-QDLTDDERKSLRKEIGYVFQDPQLFPRlTVREN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 475 IKYSLYslkdleamenyyeentndtyenknfslisnsmtsnelleMKKEYQTIKDSDVVDVSKKVlihdfvsSLPDKYDT 554
Cdd:pfam00005 80 LRLGLL---------------------------------------LKGLSKREKDARAEEALEKL-------GLGDLADR 113
|
170 180 190
....*....|....*....|....*....|....*..
gi 124506379 555 LVGSNASKLSGGQKQRISIARAIMRNPKILILDEATS 591
Cdd:pfam00005 114 PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1001-1413 |
6.12e-41 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 162.60 E-value: 6.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1001 LEDYFCNLIEKAIDYknkgQKRRIIVNAalwgFSQSAQLFINSFAYWFGSFLIKRGTILVDdfmkSLFTFIFTGSY---- 1076
Cdd:TIGR01193 360 IDSEFGDYLNKSFKY----QKADQGQQA----IKAVTKLILNVVILWTGAYLVMRGKLTLG----QLITFNALLSYfltp 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1077 AGKLMSLKGDSENAKLSFEKYYPLMIRKSNIDvrdDGGIRINKNLIKGKVDIKDVNFRYisRPNVPIYKNLSFTCDSKKT 1156
Cdd:TIGR01193 428 LENIINLQPKLQAARVANNRLNEVYLVDSEFI---NKKKRTELNNLNGDIVINDVSYSY--GYGSNILSDISLTIKMNSK 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1157 TAIVGETGSGKSTFMNLLLRFYdlkndhiilkndmtnfqdyqnnnnnslvlknvnefsnQSGSaedytvfnnnGEILLDD 1236
Cdd:TIGR01193 503 TTIVGMSGSGKSTLAKLLVGFF-------------------------------------QARS----------GEILLNG 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1237 INICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFG-REDATLEDVKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGG 1315
Cdd:TIGR01193 536 FSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGG 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1316 QKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdkaDKTIITIAHRIASIKRSDKIVVFNnpdrNGTFVQ 1395
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ---DKTIIFVAHRLSVAKQSDKIIVLD----HGKIIE 688
|
410
....*....|....*...
gi 124506379 1396 ShGTHDELLsAQDGIYKK 1413
Cdd:TIGR01193 689 Q-GSHDELL-DRNGFYAS 704
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
378-639 |
1.91e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.81 E-value: 1.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDShNLKDINLKWWRSKI 457
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGK-PLSAMPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSNSIKNNIKYSlYSLKDLEAmenyyeentndtyenknfslisNSMTSNELLEMkkeyqtikdsdvVDVSK 537
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFP-FQLRERKF----------------------DRERALELLER------------LGLPP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 KVLihdfvsslpDKydtlvgsNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 617
Cdd:COG4619 122 DIL---------DK-------PVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVL 185
|
250 260
....*....|....*....|...
gi 124506379 618 IIAHRLSTI-RYANTIFVLSNRE 639
Cdd:COG4619 186 WVSHDPEQIeRVADRVLTLEAGR 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
378-635 |
1.92e-40 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 149.58 E-value: 1.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKD-VEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDINLKWWR 454
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgkDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 455 SKIGVVSQDPLLFSN---SIKNNIKYSLYSLKDLEAMENYYEentndtyenknfslisnsmtsNELLEMKKeyqtikdsd 531
Cdd:cd03257 82 KEIQMVFQDPMSSLNprmTIGEQIAEPLRIHGKLSKKEARKE---------------------AVLLLLVG--------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 532 vVDVSKKVLihdfvsslpDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgN 611
Cdd:cd03257 132 -VGLPEEVL---------NRY-------PHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQ-E 193
|
250 260
....*....|....*....|....*.
gi 124506379 612 ENRITII-IAHRLSTIRY-ANTIFVL 635
Cdd:cd03257 194 ELGLTLLfITHDLGVVAKiADRVAVM 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1123-1417 |
3.75e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 158.06 E-value: 3.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1123 KGKVDIKDVNFRYISRPNvPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnn 1202
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP---------------------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1203 nslvlknvnefsnqsgsaedytvfnNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVK 1282
Cdd:PRK11160 393 -------------------------QQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALI 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1283 RVSKFAAIDEFIESlPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKAD 1362
Cdd:PRK11160 448 EVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQN 524
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 1363 KTIITIAHRIASIKRSDKIVVFNnpdrNGTFVQShGTHDELLSAQDGIYKKYVKL 1417
Cdd:PRK11160 525 KTVLMITHRLTGLEQFDRICVMD----NGQIIEQ-GTHQELLAQQGRYYQLKQRL 574
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1121-1414 |
2.05e-39 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 156.03 E-value: 2.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1121 LIKGKVDIKDVNFRYisRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnn 1200
Cdd:PRK10790 336 LQSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL-------------------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1201 nnnslvlknvnefsnqsgsaedytvfnNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGReDATLED 1280
Cdd:PRK10790 394 ---------------------------TEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1281 VKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1360
Cdd:PRK10790 446 VWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH 525
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 124506379 1361 AdkTIITIAHRIASIKRSDKIVVFNnpdrNGTFVQsHGTHDELLSAQDGIYKKY 1414
Cdd:PRK10790 526 T--TLVVIAHRLSTIVEADTILVLH----RGQAVE-QGTHQQLLAAQGRYWQMY 572
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1123-1406 |
5.94e-39 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 154.14 E-value: 5.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1123 KGKVDIKDVNFRYisrP--NVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLrfydlkndhiilkndmtnfqdyqnn 1200
Cdd:COG4618 328 KGRLSVENLTVVP---PgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLV------------------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1201 nnnslvlknvnefsnqsGSAEDYtvfnnNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENI-KFGreDATLE 1279
Cdd:COG4618 380 -----------------GVWPPT-----AGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1280 DVKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKd 1359
Cdd:COG4618 436 KVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK- 514
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 124506379 1360 KADKTIITIAHRIASIKRSDKIVVFnnpdRNGTfVQSHGTHDELLSA 1406
Cdd:COG4618 515 ARGATVVVITHRPSLLAAVDKLLVL----RDGR-VQAFGPRDEVLAR 556
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
317-688 |
8.56e-39 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 155.50 E-value: 8.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 317 ASVISILLGVLISM--FM-----LTIILPNITEYMKALEATNSLYEIINR-KPLVE---NNDDGETLPNI--KKIEFKNV 383
Cdd:TIGR03797 378 AAAISLLGGAGLSLgsFLafntaFGSFSGAVTQLSNTLISILAVIPLWERaKPILEalpEVDEAKTDPGKlsGAIEVDRV 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 384 RFHYdtRKD-VEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSKIGVVSQ 462
Cdd:TIGR03797 458 TFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFY-DGQDLAGLDVQAVRRQLGVVLQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 463 DPLLFSNSIKNNIkyslyslkdleamenyyeentndtyenknfsLISNSMTSNELLEmkkeyqtikdsdvvdVSKKVLIH 542
Cdd:TIGR03797 535 NGRLMSGSIFENI-------------------------------AGGAPLTLDEAWE---------------AARMAGLA 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 543 DFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnritIIIAHR 622
Cdd:TIGR03797 569 EDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR----IVIAHR 644
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 623 LSTIRYANTIFVLsnrersdnnnnnnnddnnnnnnnnnnkinNEGSyIIEQGTHDSLMkNKNGIYH 688
Cdd:TIGR03797 645 LSTIRNADRIYVL-----------------------------DAGR-VVQQGTYDELM-AREGLFA 679
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1016-1416 |
4.58e-38 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 153.57 E-value: 4.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1016 KNKGQKRRIIVNAALWG-----FSQSAQLFINSFAYWFGSFLIKRGTILVDDFMKslFTFIFtGSYAGKLMSLKG---DS 1087
Cdd:TIGR03797 342 KLFSRQRKLELSAQRIEnlltvFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLA--FNTAF-GSFSGAVTQLSNtliSI 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1088 ENAKLSFEKYYPLMIRKSNIDvrddgGIRINKNLIKGKVDIKDVNFRYisRPNVP-IYKNLSFTCDSKKTTAIVGETGSG 1166
Cdd:TIGR03797 419 LAVIPLWERAKPILEALPEVD-----EAKTDPGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSG 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1167 KSTFMNLLLRFydlkndhiilkndmtnfqdyqnnnnnslvlknvnefsNQSGSaedytvfnnnGEILLDDINICDYNLRD 1246
Cdd:TIGR03797 492 KSTLLRLLLGF-------------------------------------ETPES----------GSVFYDGQDLAGLDVQA 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1247 LRNLFSIVSQEPMLFNMSIYENIKfGREDATLEDVKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARAL 1326
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1327 LREPKILLLDEATSSLDSNSEKLIEKTIvdikDKADKTIITIAHRIASIKRSDKIVVFNnpdrNGTFVQShGTHDELLsA 1406
Cdd:TIGR03797 604 VRKPRILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRLSTIRNADRIYVLD----AGRVVQQ-GTYDELM-A 673
|
410
....*....|
gi 124506379 1407 QDGIYKKYVK 1416
Cdd:TIGR03797 674 REGLFAQLAR 683
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
210-1416 |
4.92e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 156.44 E-value: 4.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 210 VICNKKVKLNKKtSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNKFNLSETFYSKYILKANFVEALHIGLINGL-ILV 288
Cdd:PLN03130 459 FIISKMQKLTKE-GLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIpVLV 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 289 SY-AFGFWygTRIiinsATNQYPNNDFNGASVISILLgvlISMFMLtiilPN-ITEYMKALEATNSLYE-------IINR 359
Cdd:PLN03130 538 TVvSFGVF--TLL----GGDLTPARAFTSLSLFAVLR---FPLFML----PNlITQAVNANVSLKRLEElllaeerVLLP 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 360 KPLVEnnddgetlPNIKKIEFKNVRFHYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGK-STILKLIERLYDPTEGDII 438
Cdd:PLN03130 605 NPPLE--------PGLPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVV 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 439 VndshnlkdinlkwwRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdleamenyyeentndtyenknfslisnsmtsnell 518
Cdd:PLN03130 677 I--------------RGTVAYVPQVSWIFNATVRDNILFGS--------------------------------------- 703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 519 emkkEYQTIKDSDVVDVSKkvLIHDfVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLD-NKS 597
Cdd:PLN03130 704 ----PFDPERYERAIDVTA--LQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDaHVG 776
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 598 EYLVQKTINNLKGNENRItiIIAHRLSTIRYANTIFVLSnrersdnnnnnnnddnnnnnnnnnnkinnEGSyIIEQGTHD 677
Cdd:PLN03130 777 RQVFDKCIKDELRGKTRV--LVTNQLHFLSQVDRIILVH-----------------------------EGM-IKEEGTYE 824
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 678 SLMKNKNGIYHLMINNQKISSnkssnngndngsdnkssaYKDSDTGNDADNMNSLSIhENENISNNRNCKNTAENEKEEK 757
Cdd:PLN03130 825 ELSNNGPLFQKLMENAGKMEE------------------YVEENGEEEDDQTSSKPV-ANGNANNLKKDSSSKKKSKEGK 885
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 758 VPFFKRMFRRKKKAPNNLRIIYKEIFSYKKDVTIIFFSILvaggLYPVFALLYARYVSTLFDFANLEYNSNKYsiYILLI 837
Cdd:PLN03130 886 SVLIKQEERETGVVSWKVLERYKNALGGAWVVMILFLCYV----LTEVFRVSSSTWLSEWTDQGTPKTHGPLF--YNLIY 959
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 838 AIAMF--ISETLKNYYNNKIGE-KVEKTMKRRLFENILYQEMSFF-----------------DQDKNTPGVLSAHINRDV 897
Cdd:PLN03130 960 ALLSFgqVLVTLLNSYWLIMSSlYAAKRLHDAMLGSILRAPMSFFhtnplgriinrfakdlgDIDRNVAVFVNMFLGQIF 1039
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 898 HLLKT----GLVNNIVIFShfIMLFLVSmvmsFYfcpivAAVLtfiYFINMrvfavrarltkSKEIEKKENMS-SGVFA- 971
Cdd:PLN03130 1040 QLLSTfvliGIVSTISLWA--IMPLLVL----FY-----GAYL---YYQST-----------AREVKRLDSITrSPVYAq 1094
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 972 FSsddemfkdpsfliqEAFYNMHTVINYGLEDYFCNLIEKAIDYK------NKGQKRRIIVNAALWG-----FSQSAQLF 1040
Cdd:PLN03130 1095 FG--------------EALNGLSTIRAYKAYDRMAEINGRSMDNNirftlvNMSSNRWLAIRLETLGglmiwLTASFAVM 1160
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1041 INSFAYWFGSFLIKRGTILVddfmkslFTFIFTGSYAG--KLMSLKGDSENAKLSFEKYyplmirksnIDVRDDGGIRIN 1118
Cdd:PLN03130 1161 QNGRAENQAAFASTMGLLLS-------YALNITSLLTAvlRLASLAENSLNAVERVGTY---------IDLPSEAPLVIE 1224
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1119 KNL------IKGKVDIKDVNFRYisRPNVP-IYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNdhiilkndm 1191
Cdd:PLN03130 1225 NNRpppgwpSSGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELER--------- 1293
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1192 tnfqdyqnnnnnslvlknvnefsnqsgsaedytvfnnnGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKF 1271
Cdd:PLN03130 1294 --------------------------------------GRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDP 1335
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1272 GRE--DATL-EDVKRvskfAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1348
Cdd:PLN03130 1336 FNEhnDADLwESLER----AHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 1349 LIEKTIVDikDKADKTIITIAHRIASIKRSDKIVVFNNPDrngtfVQSHGTHDELLSAQDGIYKKYVK 1416
Cdd:PLN03130 1412 LIQKTIRE--EFKSCTMLIIAHRLNTIIDCDRILVLDAGR-----VVEFDTPENLLSNEGSAFSKMVQ 1472
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
310-1418 |
6.80e-38 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 155.87 E-value: 6.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 310 PNN--DFNGASVISILLGVL-ISMFMLTIILPNITE---YMKALEATNSLYEI----INRKPLvennDDGETlpniKKIE 379
Cdd:TIGR00957 567 ENNilDAEKAFVSLALFNILrFPLNILPMVISSIVQasvSLKRLRIFLSHEELepdsIERRTI----KPGEG----NSIT 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 380 FKNVRFHYdTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDShnlkdinlkwwrskIGV 459
Cdd:TIGR00957 639 VHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAY 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 460 VSQDPLLFSNSIKNNIKYSlyslKDLEamENYYEENTNDTyenknfSLISNsmtsnelLEMkkeyqtikdsdvvdvskkv 539
Cdd:TIGR00957 704 VPQQAWIQNDSLRENILFG----KALN--EKYYQQVLEAC------ALLPD-------LEI------------------- 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 540 lihdfvssLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNK-SEYLVQKTINNLKGNENRITII 618
Cdd:TIGR00957 746 --------LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPEGVLKNKTRIL 817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 619 IAHRLSTIRYANTIFVLSnrersdnnnnnnnddnnnnnnnnnnkinneGSYIIEQGTHDSLMKnKNGIYHLMINNqkiss 698
Cdd:TIGR00957 818 VTHGISYLPQVDVIIVMS------------------------------GGKISEMGSYQELLQ-RDGAFAEFLRT----- 861
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 699 nksSNNGNDNGSDNKSSAYKDSDTGNDADNM-NSLSI------HENENISN--------NRNCKNTAENEKEEKVPFFKR 763
Cdd:TIGR00957 862 ---YAPDEQQGHLEDSWTALVSGEGKEAKLIeNGMLVtdvvgkQLQRQLSAsssdsgdqSRHHGSSAELQKAEAKEETWK 938
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 764 MFRRKKKAPNNLRI-IYkeiFSYKKDV--TIIFFSILVAGGLYpVFALLYARYVSTLFD--FANLEYNSNKY--SIY--- 833
Cdd:TIGR00957 939 LMEADKAQTGQVELsVY---WDYMKAIglFITFLSIFLFVCNH-VSALASNYWLSLWTDdpMVNGTQNNTSLrlSVYgal 1014
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 834 -------ILLIAIAMFISetlknyynnkiGEKVEKTMKRRLFENILYQEMSFFDQdknTP-GVLSAHINRDVHLLKTGLV 905
Cdd:TIGR00957 1015 gilqgfaVFGYSMAVSIG-----------GIQASRVLHQDLLHNKLRSPMSFFER---TPsGNLVNRFSKELDTVDSMIP 1080
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 906 NNIVIFSHFIMLFLVSMVMSFYFCPIVAAV---LTFIYFINMRVFAvrarlTKSKEIEKKENMS-SGVFAFSSddemfkd 981
Cdd:TIGR00957 1081 PVIKMFMGSLFNVIGALIVILLATPIAAVIippLGLLYFFVQRFYV-----ASSRQLKRLESVSrSPVYSHFN------- 1148
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 982 psfliqEAFYNMHTVINYGLEDYFCNLIEKAIDYKNKGQKRRIIVNAalwgfsqsaqlfinsfayWFGSFLIKRGTILVd 1061
Cdd:TIGR00957 1149 ------ETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANR------------------WLAVRLECVGNCIV- 1203
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1062 dFMKSLFTFIFTGSYAGKLMSLkgdSENAKLSFEKYYPLMIR-----KSNI----------DVRDDGGIRINKNLI---- 1122
Cdd:TIGR00957 1204 -LFAALFAVISRHSLSAGLVGL---SVSYSLQVTFYLNWLVRmssemETNIvaverlkeysETEKEAPWQIQETAPpsgw 1279
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1123 --KGKVDIKDVNFRYisRPNVP-IYKNLSFTCDSKKTTAIVGETGSGKSTFmnlllrfydlkndhiilkndmtnfqdyqn 1199
Cdd:TIGR00957 1280 ppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSL----------------------------- 1328
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1200 nnnnSLVLKNVNEfsnqsgSAEdytvfnnnGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIK-FGREDAtl 1278
Cdd:TIGR00957 1329 ----TLGLFRINE------SAE--------GEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQYSD-- 1388
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1279 EDVKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1358
Cdd:TIGR00957 1389 EEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQF 1468
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1359 DkaDKTIITIAHRIASIKRSDKIVVFNNPDrngtfVQSHGTHDELLsAQDGIYKKYVKLA 1418
Cdd:TIGR00957 1469 E--DCTVLTIAHRLNTIMDYTRVIVLDKGE-----VAEFGAPSNLL-QQRGIFYSMAKDA 1520
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
378-637 |
1.10e-37 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 141.70 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLKWWRSKI 457
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG-KDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPL--LFSNSIKNNIKYSLyslkdleamenyyeentndtyenKNFSLisnsmtSNEllEMKKEyqtikdsdVVDV 535
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAFGP-----------------------ENLGL------PRE--EIRER--------VEEA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 536 SKKV-LIHdfvssLPDKydtlvgsNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENR 614
Cdd:COG1122 119 LELVgLEH-----LADR-------PPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL--NKEG 184
|
250 260
....*....|....*....|....*
gi 124506379 615 ITIIIA-HRLSTI-RYANTIFVLSN 637
Cdd:COG1122 185 KTVIIVtHDLDLVaELADRVIVLDD 209
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
38-693 |
3.31e-37 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 151.05 E-value: 3.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 38 EKISFFLPFKCLPAQHRKLLFISFVCAVLS-----GGTLpFFISVFGVILKNMNLGddinpiILSLVSIGLV-----QFI 107
Cdd:TIGR01193 139 EKENSLLKFIPLITRQKKLIVNIVIAAIIVtlisiAGSY-YLQKIIDTYIPHKMMG------TLGIISIGLIiayiiQQI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 108 LSMISSYCMDVITSKILKTLKLEYLRSVFYQDGQFHDNNPGSKLRS---DLDFYLEQVSSGIGTKF--ITIFTYASSFLG 182
Cdd:TIGR01193 212 LSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSrftDASSIIDALASTILSLFldMWILVIVGLFLV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 183 LyiwsliKNARLTLCITCVFPlIYVCGVICNKKV--KLNKKTslLYNNNTM-SIIEEALMGIRTVASYCGEKTILNKFnl 259
Cdd:TIGR01193 292 R------QNMLLFLLSLLSIP-VYAVIIILFKRTfnKLNHDA--MQANAVLnSSIIEDLNGIETIKSLTSEAERYSKI-- 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 260 sETFYSKYiLKANFV----EALHIGLINGLILVSYAFGFWYGTRIIInsaTNQypnndfngasvisILLGVLISMFML-- 333
Cdd:TIGR01193 361 -DSEFGDY-LNKSFKyqkaDQGQQAIKAVTKLILNVVILWTGAYLVM---RGK-------------LTLGQLITFNALls 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 334 --TIILPNITEYMKALEATNSLYEIINRKPLV--ENNDDGE----TLPNiKKIEFKNVRFHYDTRKdvEIYKDLSFTLKE 405
Cdd:TIGR01193 423 yfLTPLENIINLQPKLQAARVANNRLNEVYLVdsEFINKKKrtelNNLN-GDIVINDVSYSYGYGS--NILSDISLTIKM 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 406 GKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNdSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKyslyslkdL 485
Cdd:TIGR01193 500 NSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN-GFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLL--------L 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 486 EAMENYYEEntndtyenknfslisnsmtsnellemkkeyqtikdsDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSG 565
Cdd:TIGR01193 571 GAKENVSQD------------------------------------EIWAACEIAEIKDDIENMPLGYQTELSEEGSSISG 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 566 GQKQRISIARAIMRNPKILILDEATSSLDNKSEylvQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSnrersdnnn 645
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLD--------- 682
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 124506379 646 nnnnddnnnnnnnnnnkinnEGSyIIEQGTHDSLMkNKNGIYHLMINN 693
Cdd:TIGR01193 683 --------------------HGK-IIEQGSHDELL-DRNGFYASLIHN 708
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
345-635 |
2.10e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 145.82 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 345 KALEATNSLYEiiNRKPLVENNDDGETLpnikkIEFKNVRFHYDTRK--DVEIYKDLSFTLKEGKTYAFVGESGCGKSTI 422
Cdd:COG1123 235 QALAAVPRLGA--ARGRAAPAAAAAEPL-----LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 423 LKLIERLYDPTEGDIIVN--DSHNLKDINLKWWRSKIGVVSQDPL--LF-SNSIKNNIKYSLYSLKDLEAMEnyYEENTn 497
Cdd:COG1123 308 ARLLLGLLRPTSGSILFDgkDLTKLSRRSLRELRRRVQMVFQDPYssLNpRMTVGDIIAEPLRLHGLLSRAE--RRERV- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 498 dtyenknfslisnsmtsNELLEMkkeyqtikdsdvVDVSKKVLihdfvsslpDKYdtlvgsnASKLSGGQKQRISIARAI 577
Cdd:COG1123 385 -----------------AELLER------------VGLPPDLA---------DRY-------PHELSGGQRQRVAIARAL 419
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124506379 578 MRNPKILILDEATSSLDnkseYLVQKTI-NNLKG--NENRITII-IAHRLSTIRY-ANTIFVL 635
Cdd:COG1123 420 ALEPKLLILDEPTSALD----VSVQAQIlNLLRDlqRELGLTYLfISHDLAVVRYiADRVAVM 478
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1124-1383 |
2.24e-36 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 137.16 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1124 GKVDIKDVNFRYisRPNVP-IYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDlkndhiilkndmtnfqdyqnnnn 1202
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE----------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1203 nslvlknvnefsnqsgsAEdytvfnnNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENI-KFGR-EDATLED 1280
Cdd:cd03369 60 -----------------AE-------EGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLdPFDEySDEEIYG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1281 VKRVSkfaaidefiESlpnkydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDK 1360
Cdd:cd03369 116 ALRVS---------EG------------GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIR--EEF 172
|
250 260
....*....|....*....|...
gi 124506379 1361 ADKTIITIAHRIASIKRSDKIVV 1383
Cdd:cd03369 173 TNSTILTIAHRLRTIIDYDKILV 195
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
379-637 |
4.23e-36 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 136.44 E-value: 4.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 379 EFKNVRFHYDtRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDShNLKDINLKWWRSKIG 458
Cdd:cd03225 1 ELKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGK-DLTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 459 VVSQDP--LLFSNSIKNNIKYSLyslkdleamENYYEENTndtyenknfslisnsmtsnellEMKKEyqtikdsdVVDVS 536
Cdd:cd03225 79 LVFQNPddQFFGPTVEEEVAFGL---------ENLGLPEE----------------------EIEER--------VEEAL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 537 KKVLIhdfvSSLPDKydtlvgsNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRIT 616
Cdd:cd03225 120 ELVGL----EGLRDR-------SPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLK--AEGKT 186
|
250 260
....*....|....*....|...
gi 124506379 617 IIIA-HRLSTIR-YANTIFVLSN 637
Cdd:cd03225 187 IIIVtHDLDLLLeLADRVIVLED 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1126-1386 |
8.40e-36 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 136.16 E-value: 8.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPnvpIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDL------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedYTVFNNNGEILLDDINIC--DYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGredATLEDVKR 1283
Cdd:cd03260 53 -----------------IPGAPDEGEVLLDGKDIYdlDVDVLELRRRVGMVFQKPNPFPGSIYDNVAYG---LRLHGIKL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1284 VSKFAAIDEfiESL-----PNKYDTNVGPYGksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1358
Cdd:cd03260 113 KEELDERVE--EALrkaalWDEVKDRLHALG--LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELK 188
|
250 260
....*....|....*....|....*....
gi 124506379 1359 DkaDKTIITIAHRIASIKR-SDKIVVFNN 1386
Cdd:cd03260 189 K--EYTIVIVTHNMQQAARvADRTAFLLN 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
378-637 |
1.85e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.19 E-value: 1.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYdtrKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDiNLKWWRSKI 457
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG-EDVAR-DPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSN-SIKNNIKY--SLYSLKDLEAMENYyeentndtyenknfslisnsmtsNELLEMkkeyqtikdsdvVD 534
Cdd:COG1131 76 GYVPQEPALYPDlTVRENLRFfaRLYGLPRKEARERI-----------------------DELLEL------------FG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 535 vskkvlihdfvssLPDKYDTLVGsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENR 614
Cdd:COG1131 121 -------------LTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELA--AEG 181
|
250 260
....*....|....*....|....*
gi 124506379 615 ITIIIA-HRLSTI-RYANTIFVLSN 637
Cdd:COG1131 182 KTVLLStHYLEEAeRLCDRVAIIDK 206
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
355-689 |
2.52e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 143.43 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 355 EIINRKPLVENNDDGETLPNIKKIEFKNVRFHYDTRKDVEIyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTE 434
Cdd:PRK11160 316 EITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 435 GDIIVNDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKyslyslkdleamenyyeentndtyenknfsLISNSMTS 514
Cdd:PRK11160 395 GEILLNG-QPIADYSEAALRQAISVVSQRVHLFSATLRDNLL------------------------------LAAPNASD 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 515 NELLEmkkeyqtikdsdvvdVSKKVLIHDFVSSlPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK11160 444 EALIE---------------VLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 595 NKSEylvQKTINNL-KGNENRITIIIAHRLSTIRYANTIFVLsnrersdnnnnnnnddnnnnnnnnnnkinnEGSYIIEQ 673
Cdd:PRK11160 508 AETE---RQILELLaEHAQNKTVLMITHRLTGLEQFDRICVM------------------------------DNGQIIEQ 554
|
330
....*....|....*.
gi 124506379 674 GTHDSLMKNKNGIYHL 689
Cdd:PRK11160 555 GTHQELLAQQGRYYQL 570
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
399-694 |
8.50e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 141.91 E-value: 8.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 399 LSFTLKEGKTYAFVGESGCGKSTILKLIerL-YDPTEGDIIVNDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIky 477
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNAL--LgFLPYQGSLKING-IELRELDPESWRKHLSWVGQNPQLPHGTLRDNV-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 478 slyslkdleamenyyeentndtyenknfsLISNSMTSNELLEmkkeyQTIKDSDVvdvskkvliHDFVSSLPDKYDTLVG 557
Cdd:PRK11174 444 -----------------------------LLGNPDASDEQLQ-----QALENAWV---------SEFLPLLPQGLDTPIG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 558 SNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsn 637
Cdd:PRK11174 481 DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQWDQIWVM-- 556
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 638 rersdnnnnnnnddnnnnnnnnnnkinnEGSYIIEQGTHDSLMKNKNGIYHLMINNQ 694
Cdd:PRK11174 557 ----------------------------QDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
397-637 |
1.39e-34 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 141.04 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDinlkWWRSK----IGVVSQDPLLFSNSIK 472
Cdd:COG4618 349 RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL-DGADLSQ----WDREElgrhIGYLPQDVELFDGTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 473 NNIkyslyslkdleAMenyyeentndtyenknfslisnsmtsnellemkkeYQTIKDSDVVDVSKKVLIHDFVSSLPDKY 552
Cdd:COG4618 424 ENI-----------AR-----------------------------------FGDADPEKVVAAAKLAGVHEMILRLPDGY 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 553 DTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIRYANTI 632
Cdd:COG4618 458 DTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRPSLLAAVDKL 536
|
....*
gi 124506379 633 FVLSN 637
Cdd:COG4618 537 LVLRD 541
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
378-620 |
1.97e-34 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 132.30 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIVNDSH-NLKDINLK 451
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 WWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdleamenyyeentndtyenknfslisnsmtsnELLEMKKEYQTikDSD 531
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGL------------------------------------RLHGIKLKEEL--DER 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 532 VVDVSKKVLIHDFVSslpDKydtlvgSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgn 611
Cdd:cd03260 120 VEEALRKAALWDEVK---DR------LHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELK-- 188
|
....*....
gi 124506379 612 eNRITIIIA 620
Cdd:cd03260 189 -KEYTIVIV 196
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1126-1408 |
2.18e-34 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 132.07 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnNSL 1205
Cdd:COG1122 1 IELENLSFSY--PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLL----------------------------NGL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 VLknvnefsNQSGsaedytvfnnngEILLDDINICDYNLRDLRNLFSIVSQEP--MLFNMSIYENIKFG-------REDA 1276
Cdd:COG1122 51 LK-------PTSG------------EVLVDGKDITKKNLRELRRKVGLVFQNPddQLFAPTVEEDVAFGpenlglpREEI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1277 tledVKRVSKfaAIDEF-IESLPNKYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1355
Cdd:COG1122 112 ----RERVEE--ALELVgLEHLADRP-----PH--ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLK 178
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 124506379 1356 DIKdKADKTIITIAHRIASI-KRSDKIVVFNnpdrNGTfVQSHGTHDELLSAQD 1408
Cdd:COG1122 179 RLN-KEGKTVIIVTHDLDLVaELADRVIVLD----DGR-IVADGTPREVFSDYE 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1128-1386 |
6.42e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.94 E-value: 6.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYISRPnvpIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnnslvl 1207
Cdd:COG4619 3 LEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP--------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqsgsaedytvfnNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDAtledvKRVSKF 1287
Cdd:COG4619 53 --------------------TSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNLPFPFQLR-----ERKFDR 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1288 AAIDEFIES--LPNKY-DTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKT 1364
Cdd:COG4619 108 ERALELLERlgLPPDIlDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRA 183
|
250 260
....*....|....*....|...
gi 124506379 1365 IITIAHRIASIKR-SDKIVVFNN 1386
Cdd:COG4619 184 VLWVSHDPEQIERvADRVLTLEA 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1144-1340 |
7.18e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 127.76 E-value: 7.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1144 YKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYdlkndhiilkndmtnfqdyqnnnnnslvlknvnefSNQSGsaedy 1223
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL-----------------------------------SPTEG----- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1224 tvfnnngEILLDDINICDYNLRDLRNLFSIVSQEPMLFN-MSIYENIKFGREDATLEDVKRVSKFAAIDEFIeSLPNKYD 1302
Cdd:pfam00005 41 -------TILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENLRLGLLLKGLSKREKDARAEEALEKL-GLGDLAD 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 124506379 1303 TNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1340
Cdd:pfam00005 113 RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
378-638 |
9.32e-34 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 130.31 E-value: 9.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDINLKWWRS 455
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgeDISGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 456 KIGVVSQDPLLFSN-SIKNNIKYSLYslkdleamenyyeENTNDTYEnknfslisnsmTSNELLEMKKEyqtikdsdvvd 534
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLR-------------EHTRLSEE-----------EIREIVLEKLE----------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 535 vskKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 614
Cdd:cd03261 123 ---AVGLRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGL 188
|
250 260
....*....|....*....|....*
gi 124506379 615 ITIIIAHRLSTIRY-ANTIFVLSNR 638
Cdd:cd03261 189 TSIMVTHDLDTAFAiADRIAVLYDG 213
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1139-1406 |
1.14e-33 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 137.86 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1139 PNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnslvlknVNEFSNQSG 1218
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLI-----------------------------------VGIWPPTSG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1219 SAEdytvfnnngeilLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVSKFAAIDEFIESLP 1298
Cdd:TIGR01842 374 SVR------------LDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLP 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1299 NKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIKRS 1378
Cdd:TIGR01842 442 DGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALK-ARGITVVVITHRPSLLGCV 520
|
250 260
....*....|....*....|....*...
gi 124506379 1379 DKIVVFNnpdrNGTfVQSHGTHDELLSA 1406
Cdd:TIGR01842 521 DKILVLQ----DGR-IARFGERDEVLAK 543
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
378-637 |
1.37e-33 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 127.72 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDvEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSKI 457
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-DGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSNSIKNNIkyslyslkdleamenyyeentndtyenknfslisnsmtsnellemkkeyqtikdsdvvdvsk 537
Cdd:cd03246 79 GYLPQDDELFSGSIAENI-------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 kvlihdfvsslpdkydtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITI 617
Cdd:cd03246 97 -------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKA-AGATRI 150
|
250 260
....*....|....*....|
gi 124506379 618 IIAHRLSTIRYANTIFVLSN 637
Cdd:cd03246 151 VIAHRPETLASADRILVLED 170
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1128-1386 |
1.50e-33 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 129.12 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYiSRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnslvl 1207
Cdd:cd03225 2 LKNLSFSY-PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLL--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqSGSAEDYTvfnnnGEILLDDINICDYNLRDLRNLFSIVSQEP--MLFNMSIYENIKFGREDATL---EDVK 1282
Cdd:cd03225 48 ---------NGLLGPTS-----GEVLVDGKDLTKLSLKELRRKVGLVFQNPddQFFGPTVEEEVAFGLENLGLpeeEIEE 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1283 RVSkfAAIDEF-IESLPNKYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKa 1361
Cdd:cd03225 114 RVE--EALELVgLEGLRDRS-----PF--TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE- 183
|
250 260
....*....|....*....|....*.
gi 124506379 1362 DKTIITIAHRIASIKR-SDKIVVFNN 1386
Cdd:cd03225 184 GKTIIIVTHDLDLLLElADRVIVLED 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
378-637 |
2.77e-33 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 126.92 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYdtrKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND-SHNLKDINLKWWRSK 456
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGeDLTDLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSN-SIKNNIKYSlyslkdleamenyyeentndtyenknfslisnsmtsnellemkkeyqtikdsdvvdv 535
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG--------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 536 skkvlihdfvsslpdkydtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 615
Cdd:cd03229 101 ---------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGIT 153
|
250 260
....*....|....*....|...
gi 124506379 616 TIIIAHRLS-TIRYANTIFVLSN 637
Cdd:cd03229 154 VVLVTHDLDeAARLADRVVVLRD 176
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1128-1386 |
5.37e-33 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 126.18 E-value: 5.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYISRPNvPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLrfydlkndhiilkndmtnfqdyqnnnNNSLVL 1207
Cdd:cd03246 3 VENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIL--------------------------GLLRPT 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 KnvnefsnqsgsaedytvfnnnGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIkfgredatledvkrvskf 1287
Cdd:cd03246 56 S---------------------GRVRLDGADISQWDPNELGDHVGYLPQDDELFSGSIAENI------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1288 aaidefieslpnkydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIIT 1367
Cdd:cd03246 97 ------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIV 151
|
250
....*....|....*....
gi 124506379 1368 IAHRIASIKRSDKIVVFNN 1386
Cdd:cd03246 152 IAHRPETLASADRILVLED 170
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
378-637 |
6.27e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 129.09 E-value: 6.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVEIyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN-----DSHNLKDInlkw 452
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAL-KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDgldtlDEENLWEI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 453 wRSKIGVVSQDP--LLFSNSIKNNIKYSLyslkdleamenyyeentndtyENKNFSLIsnsmtsnellEMKKEyqtikds 530
Cdd:TIGR04520 76 -RKKVGMVFQNPdnQFVGATVEDDVAFGL---------------------ENLGVPRE----------EMRKR------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 531 dVVDVSKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKg 610
Cdd:TIGR04520 117 -VDEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLN- 183
|
250 260
....*....|....*....|....*...
gi 124506379 611 NENRITII-IAHRLSTIRYANTIFVLSN 637
Cdd:TIGR04520 184 KEEGITVIsITHDMEEAVLADRVIVMNK 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1126-1386 |
1.64e-32 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 125.66 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPNVPIY--KNLSFTCDSKKTTAIVGETGSGKSTFMNLLLrfydlkndhiilkndmtnfqdyqnnnnn 1203
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlKDINLEVPKGELVAIVGPVGSGKSSLLSALL---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1204 slvlknvNEFSNQSGSaedytVFNNNGeillddinicdynlrdlrnlFSIVSQEPMLFNMSIYENIKFGRE-DAtlEDVK 1282
Cdd:cd03250 53 -------GELEKLSGS-----VSVPGS--------------------IAYVSQEPWIQNGTIRENILFGKPfDE--ERYE 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1283 RVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKdKA 1361
Cdd:cd03250 99 KVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLL-LN 177
|
250 260
....*....|....*....|....*
gi 124506379 1362 DKTIITIAHRIASIKRSDKIVVFNN 1386
Cdd:cd03250 178 NKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
316-623 |
1.74e-32 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 134.03 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 316 GASVISILL------------GVLISMFMLT--------IILPN----ITEYMKALEATNSLYEIINRKPLVENNDDGET 371
Cdd:TIGR02868 249 GLAVLGALWaggpavadgrlaPVTLAVLVLLplaafeafAALPAaaqqLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 372 LPNIKKIEFKNVRFHYDTrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHnLKDINLK 451
Cdd:TIGR02868 329 GLGKPTLELRDLSAGYPG--APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP-VSSLDQD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 WWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdleamenyyeentndtyenknfsLISNSMTSnellemkkeyqtikDSD 531
Cdd:TIGR02868 406 EVRRRVSVCAQDAHLFDTTVRENL-------------------------------RLARPDAT--------------DEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 532 VVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTInnLKGN 611
Cdd:TIGR02868 441 LWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAAL 518
|
330
....*....|..
gi 124506379 612 ENRITIIIAHRL 623
Cdd:TIGR02868 519 SGRTVVLITHHL 530
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
378-639 |
2.22e-32 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 126.63 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDINLKWWRS 455
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDgqDITGLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 456 KIGVVSQDPLLFSN-SIKNNIKYSLYslkdleamenyyeENTNdtyenknfslisnsMTSNELLEMkkeyqtikdsdVVD 534
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPLR-------------EHTD--------------LSEAEIREL-----------VLE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 535 VSKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 614
Cdd:COG1127 125 KLELVGLPGAADKMP-----------SELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGL 193
|
250 260
....*....|....*....|....*.
gi 124506379 615 ITIIIAHRLSTIRY-ANTIFVLSNRE 639
Cdd:COG1127 194 TSVVVTHDLDSAFAiADRVAVLADGK 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1126-1383 |
6.46e-32 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 124.93 E-value: 6.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPN-VPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnns 1204
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1205 lvlknvnefsnqsgsaedytvfnNNGEILLDDINICDYN---LRDLRNLFSIVSQEPML-FN--MSIYENIKfgredATL 1278
Cdd:cd03257 58 -----------------------TSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDPMSsLNprMTIGEQIA-----EPL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1279 EDVKRVSKFAAIDEFI----------ESLPNKYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1348
Cdd:cd03257 110 RIHGKLSKKEARKEAVllllvgvglpEEVLNRY-----PH--ELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQA 182
|
250 260 270
....*....|....*....|....*....|....*.
gi 124506379 1349 LIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1383
Cdd:cd03257 183 QILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAV 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
378-639 |
6.83e-32 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 124.52 E-value: 6.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKD-VEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDINL-KWW 453
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtDISKLSEKELaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 454 RSKIGVVSQDPLLfsnsiknnikyslysLKDLEAMENyyeentndtyenknfslisnsmtsnelLEMKKEYQTIKDSDVV 533
Cdd:cd03255 81 RRHIGFVFQSFNL---------------LPDLTALEN---------------------------VELPLLLAGVPKKERR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 DVSKKVL--IHdfvssLPDKYDTLVgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGN 611
Cdd:cd03255 119 ERAEELLerVG-----LGDRLNHYP----SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKE 189
|
250 260
....*....|....*....|....*...
gi 124506379 612 ENRITIIIAHRLSTIRYANTIFVLSNRE 639
Cdd:cd03255 190 AGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1128-1371 |
1.03e-31 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 131.71 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYisRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNdhiilkndmtnfqdyqnnnnnslvl 1207
Cdd:TIGR02868 337 LRDLSAGY--PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ------------------------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqsgsaedytvfnnnGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVSKF 1287
Cdd:TIGR02868 390 ----------------------GEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALER 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1288 AAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKadKTIIT 1367
Cdd:TIGR02868 448 VGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVL 525
|
....
gi 124506379 1368 IAHR 1371
Cdd:TIGR02868 526 ITHH 529
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1128-1386 |
1.24e-31 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 122.42 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYISRpNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfyDLKNDHiilkndmtnfqdyqnnnnnslvl 1207
Cdd:cd03247 3 INNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQQ----------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqsgsaedytvfnnnGEILLDDINICDYNlRDLRNLFSIVSQEPMLFNMSIYENIkfgredatledvkrvskf 1287
Cdd:cd03247 57 ----------------------GEITLDGVPVSDLE-KALSSLISVLNQRPYLFDTTLRNNL------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1288 aaidefieslpnkydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIIT 1367
Cdd:cd03247 96 ---------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIW 152
|
250
....*....|....*....
gi 124506379 1368 IAHRIASIKRSDKIVVFNN 1386
Cdd:cd03247 153 ITHHLTGIEHMDKILFLEN 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
379-637 |
1.35e-31 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 121.58 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 379 EFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLKWWRSKIG 458
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-KDIAKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 459 VVSQdpllfsnsiknnikyslyslkdleamenyyeentndtyenknfslisnsmtsnellemkkeyqtikdsdvvdvskk 538
Cdd:cd00267 77 YVPQ---------------------------------------------------------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 539 vlihdfvsslpdkydtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITII 618
Cdd:cd00267 81 ------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA-EEGRTVII 135
|
250 260
....*....|....*....|
gi 124506379 619 IAHRLSTI-RYANTIFVLSN 637
Cdd:cd00267 136 VTHDPELAeLAADRVIVLKD 155
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
378-626 |
1.38e-31 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 124.58 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYdtrKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHnlKDINLKWWRSKI 457
Cdd:COG4555 2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED--VRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSN-SIKNNIKY--SLYSLKDLEAMENYYEentndtyenknfslisnsmtsnellemkkeyqtikdsdvvd 534
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRYfaELYGLFDEELKKRIEE----------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 535 vskkvLIHDFvsSLPDKYDTLVGsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENR 614
Cdd:COG4555 116 -----LIELL--GLEEFLDRRVG----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALK-KEGK 183
|
250
....*....|..
gi 124506379 615 ITIIIAHRLSTI 626
Cdd:COG4555 184 TVLFSSHIMQEV 195
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
792-1081 |
2.78e-31 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 125.28 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 792 IFFSIlVAGGLYPVFALLYARYVSTLFDFANLEYNS-------NKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMK 864
Cdd:cd18577 5 LLAAI-AAGAALPLMTIVFGDLFDAFTDFGSGESSPdeflddvNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 865 RRLFENILYQEMSFFDqdKNTPGVLSAHINRDVHLLKTGLVNNIVIFSHFIMLFLVSMVMSFYFCPIVAAVLTFIYFINM 944
Cdd:cd18577 84 KRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 945 RVFAVRAR-LTKSKEIEKKENMSSGVFAfssddemfkdpsfliQEAFYNMHTVINYGLEDYFCNLIEKAIDYKNKGQKRR 1023
Cdd:cd18577 162 IVGGIMGKlLSKYTKKEQEAYAKAGSIA---------------EEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKK 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 1024 IIVNAALWGFSQSAQLFINSFAYWFGSFLIKRGTILVDDFMKSLFTFIFTGSYAGKLM 1081
Cdd:cd18577 227 GLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIA 284
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1125-1386 |
3.22e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.99 E-value: 3.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1125 KVDIKDVNFRYISRP-----NVPIYKNlsftcdskKTTAIVGETGSGKSTFMNLLLRFydlkNDHIilkndmtnfqdyqn 1199
Cdd:COG1117 11 KIEVRNLNVYYGDKQalkdiNLDIPEN--------KVTALIGPSGCGKSTLLRCLNRM----NDLI-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1200 nnnnslvlknvnefsnqsgsaEDYTVfnnNGEILLDDINI--CDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFG----- 1272
Cdd:COG1117 65 ---------------------PGARV---EGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhg 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1273 -REDATLED-VKRVSKFAAI-DEfiesLPNKYDTNvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1349
Cdd:COG1117 121 iKSKSELDEiVEESLRKAALwDE----VKDRLKKS----ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAK 192
|
250 260 270
....*....|....*....|....*....|....*...
gi 124506379 1350 IEKTIVDIKDkaDKTIITIAHRIASIKR-SDKIVVFNN 1386
Cdd:COG1117 193 IEELILELKK--DYTIVIVTHNMQQAARvSDYTAFFYL 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
378-637 |
5.32e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 122.07 E-value: 5.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRK-DVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDS--HNLKDINL-KWW 453
Cdd:COG1136 5 LELRNLTKSYGTGEgEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdiSSLSERELaRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 454 RSKIGVVSQDPLLFSN-SIKNNIKYSL-YSLKDLEAMENYYEentndtyenknfslisnsmtsnELLEMkkeyqtikdsd 531
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALPLlLAGVSRKERRERAR----------------------ELLER----------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 532 vvdvskkVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGN 611
Cdd:COG1136 132 -------VGLGDRLDHRP-----------SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRE 193
|
250 260
....*....|....*....|....*.
gi 124506379 612 ENRITIIIAHRLSTIRYANTIFVLSN 637
Cdd:COG1136 194 LGTTIVMVTHDPELAARADRVIRLRD 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
378-637 |
5.37e-31 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 122.99 E-value: 5.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTR-KDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLKWWRSK 456
Cdd:COG1124 2 LEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG-RPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLfsnsiknnikySL---YSLKDleamenyyeentndtyenknfsLISNSMTSNELLEMKKEyqtikdsdVV 533
Cdd:COG1124 81 VQMVFQDPYA-----------SLhprHTVDR----------------------ILAEPLRIHGLPDREER--------IA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 DVSKKV-LIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDnkseYLVQKTINNL---- 608
Cdd:COG1124 120 ELLEQVgLPPSFLDRYP-----------HQLSGGQRQRVAIARALILEPELLLLDEPTSALD----VSVQAEILNLlkdl 184
|
250 260 270
....*....|....*....|....*....|
gi 124506379 609 KGNENRITIIIAHRLSTIRY-ANTIFVLSN 637
Cdd:COG1124 185 REERGLTYLFVSHDLAVVAHlCDRVAVMQN 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1126-1387 |
1.32e-30 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 119.21 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydlkndhiiLKNDmtnfqdyqnnnnnsl 1205
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL---------EEPD--------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnnNGEILLDDINICDYN--LRDLRNLFSIVSQEPMLF-NMSIYENIKFGredatledvk 1282
Cdd:cd03229 54 -----------------------SGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFpHLTVLENIALG---------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1283 rvskfaaidefieslpnkydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAD 1362
Cdd:cd03229 101 -----------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLG 151
|
250 260
....*....|....*....|....*.
gi 124506379 1363 KTIITIAHRIASIKR-SDKIVVFNNP 1387
Cdd:cd03229 152 ITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
321-637 |
1.45e-30 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 128.62 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 321 SILLGVLISMFMLTIilPNITEYMKALEATNSLYEIINRKPLvenNDDGETLPNIKK-IEFKNVRF-HYDTRKDveIYKD 398
Cdd:TIGR01842 264 SILVGRALAPIDGAI--GGWKQFSGARQAYKRLNELLANYPS---RDPAMPLPEPEGhLSVENVTIvPPGGKKP--TLRG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 399 LSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYs 478
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL-DGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIAR- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 479 lyslkdleamenyYEENtndtyenknfslisnsmtsnellemkkeyqtIKDSDVVDVSKKVLIHDFVSSLPDKYDTLVGS 558
Cdd:TIGR01842 415 -------------FGEN-------------------------------ADPEKIIEAAKLAGVHELILRLPDGYDTVIGP 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 559 NASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHRLSTIRYANTIFVLSN 637
Cdd:TIGR01842 451 GGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKA-RGITVVVITHRPSLLGCVDKILVLQD 528
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
378-627 |
2.01e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.54 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYdtRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLK---WWR 454
Cdd:COG2884 2 IRFENVSKRY--PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG-QDLSRLKRReipYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 455 SKIGVVSQD-PLLFSNSIKNNIKYSLyslkdleamenyyeentndtyenknfslisnsmtsnELLEMKKEyqTIKdSDVV 533
Cdd:COG2884 79 RRIGVVFQDfRLLPDRTVYENVALPL------------------------------------RVTGKSRK--EIR-RRVR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 DVSKKVlihdfvsSLPDKYDTLVgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDnksEYLVQKTINNLKG-NE 612
Cdd:COG2884 120 EVLDLV-------GLSDKAKALP----HELSGGEQQRVAIARALVNRPELLLADEPTGNLD---PETSWEIMELLEEiNR 185
|
250
....*....|....*.
gi 124506379 613 NRITIIIA-HRLSTIR 627
Cdd:COG2884 186 RGTTVLIAtHDLELVD 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
378-639 |
3.63e-30 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 119.99 E-value: 3.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHY-DTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDINLKWWR 454
Cdd:cd03258 2 IELKNVSKVFgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 455 SKIGVVSQDPLLFSN-SIKNNIKYSLyslkdleamenyyeentndtyenknfslisnsmtsnELLEMKKEYQTikdsdvv 533
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPL------------------------------------EIAGVPKAEIE------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 dvsKKVL-IHDFVSsLPDKYDtlvgSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKS-----EYLvqKTINn 607
Cdd:cd03258 119 ---ERVLeLLELVG-LEDKAD----AYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsilALL--RDIN- 187
|
250 260 270
....*....|....*....|....*....|....
gi 124506379 608 lkgNENRITI-IIAHRLSTIR-YANTIFVLSNRE 639
Cdd:cd03258 188 ---RELGLTIvLITHEMEVVKrICDRVAVMEKGE 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
373-636 |
4.18e-30 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 119.05 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 373 PNIKKIEFKNVRFHYdtRKDV-EIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLK 451
Cdd:cd03369 2 PEHGEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 WWRSKIGVVSQDPLLFSNSIKNNI-KYSLYSLKDLeamenyyeentndtyenknfslisnsmtsnellemkkeYQTIKds 530
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSGTIRSNLdPFDEYSDEEI--------------------------------------YGALR-- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 531 dvvdvskkvlihdfvsslpdkydtlVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKG 610
Cdd:cd03369 119 -------------------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT 173
|
250 260
....*....|....*....|....*.
gi 124506379 611 NENriTIIIAHRLSTIRYANTIFVLS 636
Cdd:cd03369 174 NST--ILTIAHRLRTIIDYDKILVMD 197
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
378-637 |
4.53e-30 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 117.80 E-value: 4.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDINLKwwRSKI 457
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL--SSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSNSIKNNIkyslyslkdleamenyyeentndtyenknfslisnsmtsnellemkkeyqtikdsdvvdvsk 537
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL-------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 kvlihdfvsslpdkydtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITI 617
Cdd:cd03247 96 ----------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLI 151
|
250 260
....*....|....*....|
gi 124506379 618 IIAHRLSTIRYANTIFVLSN 637
Cdd:cd03247 152 WITHHLTGIEHMDKILFLEN 171
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
378-637 |
1.48e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.33 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVEIyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSKI 457
Cdd:PRK13632 8 IKVENVSFSYPNSENNAL-KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-DGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDP--LLFSNSIKNNIKYSLyslkdleamenyyeentndtyENKNFSlisnsmtsnellemKKEYQTIkdsdVVDV 535
Cdd:PRK13632 86 GIIFQNPdnQFIGATVEDDIAFGL---------------------ENKKVP--------------PKKMKDI----IDDL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 536 SKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 615
Cdd:PRK13632 127 AKKVGMEDYLDKEP-----------QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKT 195
|
250 260
....*....|....*....|..
gi 124506379 616 TIIIAHRLSTIRYANTIFVLSN 637
Cdd:PRK13632 196 LISITHDMDEAILADKVIVFSE 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
379-637 |
1.53e-29 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 116.38 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 379 EFKNVRFHYDTRkdvEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLKWWRSKIG 458
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-KDLASLSPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 459 VVSQdpllfsnsiknnikyslyslkdleAMEnyyeentndtyenknfslisnsmtsnellemkkeyqtikdsdVVDVSKk 538
Cdd:cd03214 77 YVPQ------------------------ALE------------------------------------------LLGLAH- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 539 vLIHDFVSSLpdkydtlvgsnasklSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITII 618
Cdd:cd03214 90 -LADRPFNEL---------------SGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVM 153
|
250 260
....*....|....*....|
gi 124506379 619 IAHRLS-TIRYANTIFVLSN 637
Cdd:cd03214 154 VLHDLNlAARYADRVILLKD 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
378-637 |
2.16e-29 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 115.57 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYdtrKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDiNLKWWRSKI 457
Cdd:cd03230 1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG-KDIKK-EPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSNsiknnikyslyslkdleamenyyeentndtyenknfslisnsMTSNELLemkkeyqtikdsdvvdvsk 537
Cdd:cd03230 76 GYLPEEPSLYEN------------------------------------------LTVRENL------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 kvlihdfvsslpdkydtlvgsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITI 617
Cdd:cd03230 95 ------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELK-KEGKTIL 149
|
250 260
....*....|....*....|.
gi 124506379 618 IIAHRLSTI-RYANTIFVLSN 637
Cdd:cd03230 150 LSSHILEEAeRLCDRVAILNN 170
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
377-690 |
3.45e-29 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 124.83 E-value: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 377 KIEFKNVRFHYdtRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSK 456
Cdd:PRK10790 340 RIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL-DGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSNSIKNNIKYSlyslkdleamenyyeentndtyenknfslisnsmtsnellemkkeyQTIKDSDVVDVS 536
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLG----------------------------------------------RDISEEQVWQAL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 537 KKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRIT 616
Cdd:PRK10790 451 ETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVR--EHTTL 528
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 617 IIIAHRLSTIRYANTIFVLSNRErsdnnnnnnnddnnnnnnnnnnkinnegsyIIEQGTHDSLMKnKNGIYHLM 690
Cdd:PRK10790 529 VVIAHRLSTIVEADTILVLHRGQ------------------------------AVEQGTHQQLLA-AQGRYWQM 571
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
398-628 |
5.54e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 119.45 E-value: 5.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 398 DLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDINLKWWRSKIGVVSQDPllfsnsiknni 475
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqDITGLSGRELRPLRRRMQMVFQDP----------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 476 kYSlySLkdleamenyyeeNTndtyenknfslisnSMTSNELLEMKKEYQTIKDSDvvDVSKKV--LIhdfvsslpdkyd 553
Cdd:COG4608 105 -YA--SL------------NP--------------RMTVGDIIAEPLRIHGLASKA--ERRERVaeLL------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 554 TLVGSNAS-------KLSGGQKQRISIARAIMRNPKILILDEATSSLDnKSeylVQKTINNLKG---NENRIT-IIIAHR 622
Cdd:COG4608 142 ELVGLRPEhadryphEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-VS---IQAQVLNLLEdlqDELGLTyLFISHD 217
|
....*.
gi 124506379 623 LSTIRY 628
Cdd:COG4608 218 LSVVRH 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1128-1407 |
1.00e-28 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 116.68 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiILKNDmtnfqdyqnnnnnslvl 1207
Cdd:COG1120 4 AENLSVGY---GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG---------LLKPS----------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqsgsaedytvfnnNGEILLDDINICDYNLRDLRNLFSIVSQEPML-FNMSIYENIKFGR-------EDATLE 1279
Cdd:COG1120 55 ---------------------SGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVRELVALGRyphlglfGRPSAE 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1280 DVKRVSkfAAIDEF-IESLPNKydtnvgPYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIEkTIVDI 1357
Cdd:COG1120 114 DREAVE--EALERTgLEHLADR------PVD-ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDlAHQLEVLE-LLRRL 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 1358 KDKADKTII------TIAHRIAsikrsDKIVVFnnpdRNGTfVQSHGTHDELLSAQ 1407
Cdd:COG1120 184 ARERGRTVVmvlhdlNLAARYA-----DRLVLL----KDGR-IVAQGPPEEVLTPE 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1126-1413 |
1.26e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 121.93 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPN--VPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnn 1203
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP----------------------- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1204 slvlknvnefsnqsgsaedytvfnNNGEILLDDINICDYN---LRDLRNLFSIVSQEPML-FN--MSIYENIKFG---RE 1274
Cdd:COG1123 318 ------------------------TSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYSsLNprMTVGDIIAEPlrlHG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1275 DATLEDVKrvskfAAIDEFIES--LP----NKYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1348
Cdd:COG1123 374 LLSRAERR-----ERVAELLERvgLPpdlaDRY-----PH--ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQA 441
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 1349 LIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFnnpdRNGTFVQsHGTHDELLSAQDGIYKK 1413
Cdd:COG1123 442 QILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVM----YDGRIVE-DGPTEEVFANPQHPYTR 502
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1126-1382 |
3.08e-28 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 114.12 E-value: 3.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRY-ISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnns 1204
Cdd:cd03255 1 IELKNLSKTYgGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNIL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1205 lvlknvnefsnqsGSAEDYTvfnnNGEILLDDINICDYNLRDLRNL----FSIVSQEPMLF-NMSIYENIKFGredATLE 1279
Cdd:cd03255 51 -------------GGLDRPT----SGEVRVDGTDISKLSEKELAAFrrrhIGFVFQSFNLLpDLTALENVELP---LLLA 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1280 DVKRVSKFAAIDEFIES--LPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1357
Cdd:cd03255 111 GVPKKERRERAEELLERvgLGDRLNHYPS----ELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLREL 186
|
250 260
....*....|....*....|....*..
gi 124506379 1358 KDKADKTIITIAH--RIASikRSDKIV 1382
Cdd:cd03255 187 NKEAGTTIVVVTHdpELAE--YADRII 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
378-637 |
4.27e-28 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 113.38 E-value: 4.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDI-NLKWWRSK 456
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG----RDVtGVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEAMenyyeentndtyenknfslISNSMtsNELLEMkkeyqtikdsdvvdv 535
Cdd:cd03259 74 IGMVFQDYALFPHlTVAENIAFGLKLRGVPKAE-------------------IRARV--RELLEL--------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 536 skkVLIHDFVSSLPDkydtlvgsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 615
Cdd:cd03259 118 ---VGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGIT 183
|
250 260
....*....|....*....|...
gi 124506379 616 TIIIAHRLS-TIRYANTIFVLSN 637
Cdd:cd03259 184 TIYVTHDQEeALALADRIAVMNE 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1126-1384 |
4.91e-28 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 113.60 E-value: 4.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPN-VPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnS 1204
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL-----------------------------G 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1205 LVLKnvnefsnqsgsaedYTvfnnNGEILLDDINICDYN---LRDLRN-LFSIVSQEPMLF-NMSIYENIKF-----GRE 1274
Cdd:COG1136 56 GLDR--------------PT----SGEVLIDGQDISSLSereLARLRRrHIGFVFQFFNLLpELTALENVALplllaGVS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1275 DAtlEDVKRVSKFAA---IDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1351
Cdd:COG1136 118 RK--ERRERARELLErvgLGDRLDHRPSQ-----------LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVL 184
|
250 260 270
....*....|....*....|....*....|....*
gi 124506379 1352 KTIVDIKDKADKTIITIAH--RIASikRSDKIVVF 1384
Cdd:COG1136 185 ELLRELNRELGTTIVMVTHdpELAA--RADRVIRL 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1128-1386 |
5.57e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 111.18 E-value: 5.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYISRPNVpiyKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnnslvl 1207
Cdd:cd00267 2 IENLSFRYGGRTAL---DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP--------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqsgsaedytvfnNNGEILLDDINICDYNLRDLRNLFSIVSQepmlfnmsiyenikfgredatledvkrvskf 1287
Cdd:cd00267 52 --------------------TSGEILIDGKDIAKLPLEELRRRIGYVPQ------------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1288 aaidefieslpnkydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIIT 1367
Cdd:cd00267 81 ------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVII 135
|
250 260
....*....|....*....|
gi 124506379 1368 IAHRIASIKR-SDKIVVFNN 1386
Cdd:cd00267 136 VTHDPELAELaADRVIVLKD 155
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
378-638 |
5.63e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 113.34 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKD-VEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDINLKwwRSK 456
Cdd:cd03293 1 LEVRNVSKTYGGGGGaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGP--GPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFS-NSIKNNIKYSL--YSLKDLEAMEnyyeentndtyenknfslisnsmTSNELLEMkkeyqtikdsdvV 533
Cdd:cd03293 75 RGYVFQQDALLPwLTVLDNVALGLelQGVPKAEARE-----------------------RAEELLEL------------V 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 DVSkkvlihDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNEN 613
Cdd:cd03293 120 GLS------GFENAYP-----------HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIW-RET 181
|
250 260
....*....|....*....|....*..
gi 124506379 614 RITII-IAHRLS-TIRYANTIFVLSNR 638
Cdd:cd03293 182 GKTVLlVTHDIDeAVFLADRVVVLSAR 208
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
378-637 |
5.95e-28 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 112.56 E-value: 5.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVEIY--KDLSFTLKEGKTYAFVGESGCGKSTILKLI--ErlYDPTEGDIIVNDShnlkdinlkww 453
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 454 rskIGVVSQDPLLFSNSIKNNIKYSlyslkdleamENYYEEntndtyenknfslisnsmtsnellemkkEYQtikdsDVV 533
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENILFG----------KPFDEE----------------------------RYE-----KVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 DVSkkVLIHDFvSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNK-SEYLVQKTINNLkGNE 612
Cdd:cd03250 102 KAC--ALEPDL-EILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGL-LLN 177
|
250 260
....*....|....*....|....*
gi 124506379 613 NRITIIIAHRLSTIRYANTIFVLSN 637
Cdd:cd03250 178 NKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1124-1419 |
6.45e-28 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 114.24 E-value: 6.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1124 GKVDIKDVNFRYISRPNvPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDlkndhiilkndmtnfqdyqnnnnn 1203
Cdd:cd03288 18 GEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD------------------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1204 slvlknvnefsnqsgsaedytVFNnnGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGRE--DATLEDV 1281
Cdd:cd03288 73 ---------------------IFD--GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKctDDRLWEA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1282 KRVskfAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKA 1361
Cdd:cd03288 130 LEI---AQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFA 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 1362 DKTIITIAHRIASIKRSDKIVVFnnpdRNGTFVQsHGTHDELLSAQDGIYKKYVKLAK 1419
Cdd:cd03288 205 DRTVVTIAHRVSTILDADLVLVL----SRGILVE-CDTPENLLAQEDGVFASLVRTDK 257
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
377-619 |
7.52e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.98 E-value: 7.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 377 KIEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYD--P---TEGDIIVNDsHNL--KDIN 449
Cdd:COG1117 11 KIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDG-EDIydPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 450 LKWWRSKIGVVSQDPLLFSNSIKNNIKYSL--YSLKDLEAMENYYEEntndtyenknfSLisnsmtsnellemkkeyqti 527
Cdd:COG1117 87 VVELRRRVGMVFQKPNPFPKSIYDNVAYGLrlHGIKSKSELDEIVEE-----------SL-------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 528 kdsdvvdvsKKVLIHDFVSslpDKYDtlvgSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINN 607
Cdd:COG1117 136 ---------RKAALWDEVK---DRLK----KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE 199
|
250
....*....|..
gi 124506379 608 LKgneNRITIII 619
Cdd:COG1117 200 LK---KDYTIVI 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
378-635 |
1.91e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 118.47 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPT---EGDIIVNDsHNLKDINLKWWR 454
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDG-RDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 455 SKIGVVSQDPL--LFSNSIKNNIkyslyslkdLEAMENyyeentndtyenknfSLISNSmtsnellEMKKEyqtikdsdV 532
Cdd:COG1123 83 RRIGMVFQDPMtqLNPVTVGDQI---------AEALEN---------------LGLSRA-------EARAR--------V 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 533 VDVSKKVLIHDFVSSLPDkydtlvgsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNE 612
Cdd:COG1123 124 LELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRER 192
|
250 260
....*....|....*....|....
gi 124506379 613 NRITIIIAHRLSTI-RYANTIFVL 635
Cdd:COG1123 193 GTTVLLITHDLGVVaEIADRVVVM 216
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1126-1412 |
2.40e-27 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 112.91 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRpNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnNSL 1205
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLL----------------------------NGL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 VLKnvnefsnQSGsaedytvfnnngEILLDDINICD-YNLRDLRNLFSIVSQEP--MLFNMSIYENIKFGREDATL---E 1279
Cdd:TIGR04520 52 LLP-------TSG------------KVTVDGLDTLDeENLWEIRKKVGMVFQNPdnQFVGATVEDDVAFGLENLGVpreE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1280 DVKRVSKFAA---IDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1356
Cdd:TIGR04520 113 MRKRVDEALKlvgMEDFRDREPHL-----------LSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRK 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 1357 IKDKADKTIITIAHRIASIKRSDKIVVFNnpdrNGTfVQSHGTHDELLSAQDGIYK 1412
Cdd:TIGR04520 182 LNKEEGITVISITHDMEEAVLADRVIVMN----KGK-IVAEGTPREIFSQVELLKE 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1126-1414 |
2.64e-27 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 111.82 E-value: 2.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPnvpIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiILKNDmtnfqdyqnnnnnsl 1205
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG---------LLRPD--------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnnNGEILLDDINICDYN---LRDLRNLFSIVSQEPMLFN-MSIYENIKFG-REDATLED 1280
Cdd:cd03261 54 -----------------------SGEVLIDGEDISGLSeaeLYRLRRRMGMLFQSGALFDsLTVFENVAFPlREHTRLSE 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1281 vKRVSKFAAidEFIE--SLPNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1358
Cdd:cd03261 111 -EEIREIVL--EKLEavGLRGAEDL----YPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLK 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1359 DKADKTIITIAHRIASIKR-SDKIVVFNnpdrNGTFVqSHGTHDELLSAQDGIYKKY 1414
Cdd:cd03261 184 KELGLTSIMVTHDLDTAFAiADRIAVLY----DGKIV-AEGTPEELRASDDPLVRQF 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1126-1409 |
2.81e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 118.08 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPnVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDlKNDHIilkndmtnfqdyqnnnnnsl 1205
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLP-HGGRI-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnnNGEILLDDINICDYNLRDLRNLFSIVSQEPM--LFNMSIYENIKFGRE------DAT 1277
Cdd:COG1123 63 -----------------------SGEVLLDGRDLLELSEALRGRRIGMVFQDPMtqLNPVTVGDQIAEALEnlglsrAEA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1278 LEDVKRVSKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1357
Cdd:COG1123 120 RARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLREL 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 124506379 1358 KDKADKTIITIAHRIASIKR-SDKIVVFnnpdRNGTFVqSHGTHDELLSAQDG 1409
Cdd:COG1123 189 QRERGTTVLLITHDLGVVAEiADRVVVM----DDGRIV-EDGPPEEILAAPQA 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1126-1395 |
3.28e-27 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 110.69 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydLKNDHiilkndmtnfqdyqnnnnnsl 1205
Cdd:cd03259 1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL--ERPDS--------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnnnGEILLDDINICDYNLRDlRNLfSIVSQEPMLF-NMSIYENIKFG------REDATL 1278
Cdd:cd03259 55 ------------------------GEILIDGRDVTGVPPER-RNI-GMVFQDYALFpHLTVAENIAFGlklrgvPKAEIR 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1279 EDVKRVSKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1358
Cdd:cd03259 109 ARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQ 177
|
250 260 270
....*....|....*....|....*....|....*...
gi 124506379 1359 DKADKTIITIAHRIASIKR-SDKIVVFNnpdrNGTFVQ 1395
Cdd:cd03259 178 RELGITTIYVTHDQEEALAlADRIAVMN----EGRIVQ 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
378-637 |
3.29e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 112.90 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSKI 457
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII-DGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDP--LLFSNSIKNNIKYSLyslkdleamenyyeentndtyENKNFSLIsnsmtsnellEMKKEyqtikdsdVVDV 535
Cdd:PRK13650 84 GMVFQNPdnQFVGATVEDDVAFGL---------------------ENKGIPHE----------EMKER--------VNEA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 536 SKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRI 615
Cdd:PRK13650 125 LELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIR-DDYQM 192
|
250 260
....*....|....*....|...
gi 124506379 616 TII-IAHRLSTIRYANTIFVLSN 637
Cdd:PRK13650 193 TVIsITHDLDEVALSDRVLVMKN 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
378-637 |
3.38e-27 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 111.89 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDS--HNLKDINLKWWRS 455
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdiNKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 456 KIGVVSQDPllfsnsikNNIKyslyslkDLEAMENYyeentndtyenkNFSLISNSMTSNELLEMKKEYQTIKDSDVVDv 535
Cdd:cd03256 79 QIGMIFQQF--------NLIE-------RLSVLENV------------LSGRLGRRSTWRSLFGLFPKEEKQRALAALE- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 536 skKVLIHDFVSSlpdkydtlvgsNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 615
Cdd:cd03256 131 --RVGLLDKAYQ-----------RADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGIT 197
|
250 260
....*....|....*....|...
gi 124506379 616 TIIIAHRLSTIR-YANTIFVLSN 637
Cdd:cd03256 198 VIVSLHQVDLAReYADRIVGLKD 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1128-1419 |
3.40e-27 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 111.87 E-value: 3.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydLKNDHiilkndmtnfqdyqnnnnnslvl 1207
Cdd:COG4555 4 VENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL--LKPDS----------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqsgsaedytvfnnnGEILLDDINICDYNLRDLRNLFsIVSQEPMLF-NMSIYENIKFgreDATLEDVKRVSK 1286
Cdd:COG4555 56 ----------------------GSILIDGEDVRKEPREARRQIG-VLPDERGLYdRLTVRENIRY---FAELYGLFDEEL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1287 FAAIDEFIES--LPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKT 1364
Cdd:COG4555 110 KKRIEELIELlgLEEFLDRRVG----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKT 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 1365 IITIAHRIASIKR-SDKIVVFnnpdRNGTfVQSHGTHDELLS--AQDGIYKKYVKLAK 1419
Cdd:COG4555 185 VLFSSHIMQEVEAlCDRVVIL----HKGK-VVAQGSLDELREeiGEENLEDAFVALIG 237
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
378-637 |
3.51e-27 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 112.06 E-value: 3.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRkdvEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLKWWRSKI 457
Cdd:COG1120 2 LEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG-RDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPllfsnsiknnikyslyslkdleamenyyeentndtyenknfsLISNSMTSNELLEM-----KKEYQTIKDSD- 531
Cdd:COG1120 78 AYVPQEP------------------------------------------PAPFGLTVRELVALgryphLGLFGRPSAEDr 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 532 --VVDVSKKVLIHDFVsslpdkyDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLK 609
Cdd:COG1120 116 eaVEEALERTGLEHLA-------DRPVDE----LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLA 184
|
250 260
....*....|....*....|....*....
gi 124506379 610 GNENRITIIIAHRLS-TIRYANTIFVLSN 637
Cdd:COG1120 185 RERGRTVVMVLHDLNlAARYADRLVLLKD 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1126-1408 |
4.23e-27 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 111.22 E-value: 4.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPnvpIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydLKNDHiilkndmtnfqdyqnnnnnsl 1205
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL--LRPDS--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnnnGEILLDDINICDYN---LRDLRNLFSIVSQEPMLF-NMSIYENIKFG-RE-----D 1275
Cdd:COG1127 60 ------------------------GEILVDGQDITGLSekeLYELRRRIGMLFQGGALFdSLTVFENVAFPlREhtdlsE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1276 ATLED-VKRVSKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1354
Cdd:COG1127 116 AEIRElVLEKLELVGLPGAADKMPS-----------ELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELI 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 1355 VDIKDKADKTIITIAHRIASIKR-SDKIVVFNnpdrNGTfVQSHGTHDELLSAQD 1408
Cdd:COG1127 185 RELRDELGLTSVVVTHDLDSAFAiADRVAVLA----DGK-IIAEGTPEELLASDD 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
378-594 |
6.16e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 113.63 E-value: 6.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRK-DVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDINLKWWR 454
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 455 SKIGVVSQDP-LLFSNSIKNNIKYSLyslkdleamenyyeentndtyenknfslisnsmtsnELLEMKKEyqtikdsdvv 533
Cdd:COG1135 82 RKIGMIFQHFnLLSSRTVAENVALPL------------------------------------EIAGVPKA---------- 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 534 DVSKKV--LIhDFVSsLPDKydtlvgSNA--SKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:COG1135 116 EIRKRVaeLL-ELVG-LSDK------ADAypSQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
375-637 |
6.82e-27 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 109.65 E-value: 6.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 375 IKKIEFKnvrfhydTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDINLKWWR 454
Cdd:cd03226 2 IENISFS-------YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG----KPIKAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 455 SKIGVVSQDP--LLFSNSIKNNIkysLYSLKDLEAmenyyeentndtyenknfslisnsmtsnellemkkeyqtiKDSDV 532
Cdd:cd03226 71 KSIGYVMQDVdyQLFTDSVREEL---LLGLKELDA----------------------------------------GNEQA 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 533 VDVSKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGnE 612
Cdd:cd03226 108 ETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAA-Q 175
|
250 260
....*....|....*....|....*.
gi 124506379 613 NRITIIIAHRLSTI-RYANTIFVLSN 637
Cdd:cd03226 176 GKAVIVITHDYEFLaKVCDRVLLLAN 201
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
378-635 |
8.35e-27 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 112.84 E-value: 8.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRK-DVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDP---TEGDIIVN--DSHNLKDINLK 451
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDgeDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 WWRSK-IGVVSQDPLlfsNS------IKNNIKyslyslkdlEAMEnyyeentndtyenknfslISNSMTSNELLEMkkey 524
Cdd:COG0444 82 KIRGReIQMIFQDPM---TSlnpvmtVGDQIA---------EPLR------------------IHGGLSKAEARER---- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 525 qtikdsdVVDVSKKVLIHDfvsslPDKYdtlvgsnASK----LSGGQKQRISIARAIMRNPKILILDEATSSLDnkseYL 600
Cdd:COG0444 128 -------AIELLERVGLPD-----PERR-------LDRypheLSGGMRQRVMIARALALEPKLLIADEPTTALD----VT 184
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 124506379 601 VQKTI----NNLKgNENRITII-IAHRLSTIRY-ANTIFVL 635
Cdd:COG0444 185 IQAQIlnllKDLQ-RELGLAILfITHDLGVVAEiADRVAVM 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
377-638 |
1.23e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 110.56 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 377 KIEFKNVRFHYDTRK-DVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDINLKwwRS 455
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGP--GP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 456 KIGVVSQDPLLFS-NSIKNNIKYSLySLKDLEAMEnyYEEntndtyenknfslisnsmTSNELLEMkkeyqtikdsdvVD 534
Cdd:COG1116 81 DRGVVFQEPALLPwLTVLDNVALGL-ELRGVPKAE--RRE------------------RARELLEL------------VG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 535 VSkkvlihDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 614
Cdd:COG1116 128 LA------GFEDAYP-----------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGK 190
|
250 260 270
....*....|....*....|....*....|
gi 124506379 615 ITIIIAH------RLstiryANTIFVLSNR 638
Cdd:COG1116 191 TVLFVTHdvdeavFL-----ADRVVVLSAR 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
378-640 |
1.26e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.18 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRkdvEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDinlkwwRSKI 457
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA------RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQdpllfsnsiKNNIkyslyslkdleamenyyeentndtyeNKNFSlisnsMTSNELLEM-------------KKEY 524
Cdd:COG1121 78 GYVPQ---------RAEV--------------------------DWDFP-----ITVRDVVLMgrygrrglfrrpsRADR 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 525 QTIKDS-DVVDVSkkvlihdfvsslpDKYDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQK 603
Cdd:COG1121 118 EAVDEAlERVGLE-------------DLADRPIGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYE 180
|
250 260 270
....*....|....*....|....*....|....*....
gi 124506379 604 TINNLkgNENRITIIIA-HRLSTIR-YANTIFVLsNRER 640
Cdd:COG1121 181 LLREL--RREGKTILVVtHDLGAVReYFDRVLLL-NRGL 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1126-1386 |
1.48e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.85 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPNvPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnSL 1205
Cdd:PRK13632 8 IKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKIL-----------------------------TG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 VLKNvnefsnqsgsaedytvfnNNGEILLDDINICDYNLRDLRNLFSIVSQEP--MLFNMSIYENIKFGREDATL--EDV 1281
Cdd:PRK13632 58 LLKP------------------QSGEIKIDGITISKENLKEIRKKIGIIFQNPdnQFIGATVEDDIAFGLENKKVppKKM 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1282 KRVSKFAA----IDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1357
Cdd:PRK13632 120 KDIIDDLAkkvgMEDYLDKEP-----------QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDL 188
|
250 260
....*....|....*....|....*....
gi 124506379 1358 KDKADKTIITIAHRIASIKRSDKIVVFNN 1386
Cdd:PRK13632 189 RKTRKKTLISITHDMDEAILADKVIVFSE 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
378-594 |
1.54e-26 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 108.77 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRkdvEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND---SHNLKDINLkwWR 454
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlklTDDKKNINE--LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 455 SKIGVVSQDPLLFSN-SIKNNIKYSLYSLKDL---EAMEnyyeentndtyenknfslisnsmTSNELLEmkkeyqtikds 530
Cdd:cd03262 76 QKVGMVFQQFNLFPHlTVLENITLAPIKVKGMskaEAEE-----------------------RALELLE----------- 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 531 dvvdvskKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:cd03262 122 -------KVGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1127-1386 |
1.84e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 107.52 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1127 DIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiILKNDmtnfqdyqnnnnnslv 1206
Cdd:cd03214 1 EVENLSVGY---GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAG---------LLKPS---------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1207 lknvnefsnqsgsaedytvfnnNGEILLDDINICDYNLRDLRNLFSIVSQepmlfnmsiyenikfgredatledvkrvsk 1286
Cdd:cd03214 53 ----------------------SGEILLDGKDLASLSPKELARKIAYVPQ------------------------------ 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1287 faAIDEF-IESLPNKYDTnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTI 1365
Cdd:cd03214 81 --ALELLgLAHLADRPFN-------ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTV 151
|
250 260
....*....|....*....|..
gi 124506379 1366 ITIAHRIASIKR-SDKIVVFNN 1386
Cdd:cd03214 152 VMVLHDLNLAARyADRVILLKD 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
378-594 |
1.92e-26 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 109.31 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSH-NLKDINLKWWRSK 456
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDlTDSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDL---EAMEnyyeentndtyenknfslisnsmTSNELLEMkkeyqtikdsdv 532
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENVTLAPIKVKKMskaEAEE-----------------------RAMELLER------------ 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 533 VDVSKKVlihdfvsslpDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:COG1126 124 VGLADKA----------DAY-------PAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1128-1386 |
2.85e-26 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 108.00 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydLKNDHiilkndmtnfqdyqnnnnnslvl 1207
Cdd:cd03235 2 VEDLTVSY---GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGL--LKPTS----------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqsgsaedytvfnnnGEILLDDinicdYNLRDLRNLFSIVSQEPML---FNMSIYENIKFGReDATLEDVKRV 1284
Cdd:cd03235 54 ----------------------GSIRVFG-----KPLEKERKRIGYVPQRRSIdrdFPISVRDVVLMGL-YGHKGLFRRL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1285 SK--FAAIDEFIES--LPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1360
Cdd:cd03235 106 SKadKAKVDEALERvgLSELADRQIG----ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE 181
|
250 260
....*....|....*....|....*..
gi 124506379 1361 aDKTIITIAHRI-ASIKRSDKIVVFNN 1386
Cdd:cd03235 182 -GMTILVVTHDLgLVLEYFDRVLLLNR 207
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1126-1406 |
3.12e-26 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 109.12 E-value: 3.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRY-ISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRfydlkndhIILkndmtnfqdyqnnnnns 1204
Cdd:COG1124 2 LEVRNLSVSYgQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKST----LLR--------ALA----------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1205 lvlknvnefsnqsGSAEDYTvfnnnGEILLDDINICDYNLRDLRNLFSIVSQEPML-FN--MSIyenikfgreDATLEDV 1281
Cdd:COG1124 53 -------------GLERPWS-----GEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAsLHprHTV---------DRILAEP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1282 KRVSKFAAIDEFIESLPNkyDTNVGP-----YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1356
Cdd:COG1124 106 LRIHGLPDREERIAELLE--QVGLPPsfldrYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKD 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 124506379 1357 IKDKADKTIITIAHRIASIKR-SDKIVVFnnpdRNGTFVqSHGTHDELLSA 1406
Cdd:COG1124 184 LREERGLTYLFVSHDLAVVAHlCDRVAVM----QNGRIV-EELTVADLLAG 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
379-638 |
4.52e-26 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 107.62 E-value: 4.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 379 EFKNVRFHYDTRkdvEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDinlkwwRSKIG 458
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 459 VVSQdpllfsnsiKNNIKYSL-YSLKDLEAMENYYEENTNDTYENKNFSLIsnsmtsNELLEMkkeyqtikdsdvVDVSK 537
Cdd:cd03235 72 YVPQ---------RRSIDRDFpISVRDVVLMGLYGHKGLFRRLSKADKAKV------DEALER------------VGLSE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 kvLIHdfvsslpdkydtlvgSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITI 617
Cdd:cd03235 125 --LAD---------------RQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTIL 186
|
250 260
....*....|....*....|..
gi 124506379 618 IIAHRLSTI-RYANTIFVLSNR 638
Cdd:cd03235 187 VVTHDLGLVlEYFDRVLLLNRT 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1126-1406 |
9.13e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 107.46 E-value: 9.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydLKNDHiilkndmtnfqdyqnnnnnsl 1205
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL--LRPTS--------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnnnGEILLDDINICDyNLRDLRNLFSIVSQEPMLF-NMSIYENIKFGredATLEDVKRV 1284
Cdd:COG1131 55 ------------------------GEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYpDLTVRENLRFF---ARLYGLPRK 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1285 SKFAAIDEFIE--SLPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaD 1362
Cdd:COG1131 107 EARERIDELLElfGLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-G 181
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 124506379 1363 KTIITIAHRIASIKR-SDKIVVFNnpdrNGTFVQsHGTHDELLSA 1406
Cdd:COG1131 182 KTVLLSTHYLEEAERlCDRVAIID----KGRIVA-DGTPDELKAR 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
378-596 |
1.19e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 110.19 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDI-NLKWWRSK 456
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVtGLPPEKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSN-SIKNNIKYSLySLKDLEAMEnyyeentndtyenknfslISNSMtsNELLEMkkeyqtikdsdvVDv 535
Cdd:COG3842 79 VGMVFQDYALFPHlTVAENVAFGL-RMRGVPKAE------------------IRARV--AELLEL------------VG- 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124506379 536 skkvlihdfVSSLPDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNK 596
Cdd:COG3842 125 ---------LEGLADRY-------PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAK 169
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1126-1397 |
1.86e-25 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 106.02 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISR-PNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydlkndhiilkndmtnfqdyqnnnnns 1204
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGL--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1205 lvlknvnefsnqsgsaEDYTvfnnNGEILLDDINICDYNlRDLrnlfSIVSQEPMLFN-MSIYENIKFGREdatLEDVKR 1283
Cdd:cd03293 54 ----------------ERPT----SGEVLVDGEPVTGPG-PDR----GYVFQQDALLPwLTVLDNVALGLE---LQGVPK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1284 VSKFAAIDEFIESLP-----NKYdtnvgPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1358
Cdd:cd03293 106 AEARERAEELLELVGlsgfeNAY-----P--HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIW 178
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 124506379 1359 DKADKTIITIAHRIA-SIKRSDKIVVFNNpdRNGTFVQSH 1397
Cdd:cd03293 179 RETGKTVLLVTHDIDeAVFLADRVVVLSA--RPGRIVAEV 216
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
378-619 |
2.05e-25 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 106.68 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDINLKWWRS 455
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDgqDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 456 KIGVVSQDPLLFSNS--IKN----NIKY--------SLYSLKDLE-AMEnyyeentndtyenknfslisnsmtsneLLEM 520
Cdd:COG3638 81 RIGMIFQQFNLVPRLsvLTNvlagRLGRtstwrsllGLFPPEDRErALE---------------------------ALER 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 521 kkeyqtikdsdvVDVSKKVLIHdfvsslpdkydtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKS--- 597
Cdd:COG3638 134 ------------VGLADKAYQR-----------------ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTarq 184
|
250 260
....*....|....*....|....
gi 124506379 598 --EYLvqKTINnlkgNENRITIII 619
Cdd:COG3638 185 vmDLL--RRIA----REDGITVVV 202
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
378-596 |
2.40e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 109.39 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDIN-LKWWRSK 456
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG----RDVTdLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSN-SIKNNIKYSlyslkdleamenyyeentndtyenknfslisnsmtsnelLEMKKEYQTIKDSDVVDV 535
Cdd:COG3839 77 IAMVFQSYALYPHmTVYENIAFP---------------------------------------LKLRKVPKAEIDRRVREA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124506379 536 SKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNK 596
Cdd:COG3839 118 AELLGLEDLLDRKP-----------KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
376-639 |
4.93e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 106.64 E-value: 4.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 376 KKIEFKNVRFHYDTRKDVEIyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN----DSHNLKDInlk 451
Cdd:PRK13635 4 EIIRVEHISFRYPDAATYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlSEETVWDV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 wwRSKIGVVSQDPllfsnsiknnikyslyslkdleamENYYEENTndTYENKNFSLISNSMTSNELLEMkkeyqtikdsd 531
Cdd:PRK13635 80 --RRQVGMVFQNP------------------------DNQFVGAT--VQDDVAFGLENIGVPREEMVER----------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 532 VVDVSKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgN 611
Cdd:PRK13635 121 VDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLK-E 188
|
250 260
....*....|....*....|....*....
gi 124506379 612 ENRITII-IAHRLSTIRYANTIFVLSNRE 639
Cdd:PRK13635 189 QKGITVLsITHDLDEAAQADRVIVMNKGE 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1126-1407 |
6.24e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.17 E-value: 6.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:COG1121 7 IELENLTVSY---GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnQSGSaedytvfnnngeillddINICDYNLRDLRNLFSIVSQEPML---FNMSIYENIKFGReDATLEDVK 1282
Cdd:COG1121 59 ----------TSGT-----------------VRLFGKPPRRARRRIGYVPQRAEVdwdFPITVRDVVLMGR-YGRRGLFR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1283 RVSK--FAAIDEFIESlpnkydtnVG-------PYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1353
Cdd:COG1121 111 RPSRadREAVDEALER--------VGledladrPIG-ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEL 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 1354 IVDIKdKADKTIITIAHRIASIKR-SDKIVVFNNPdrngtfVQSHGTHDELLSAQ 1407
Cdd:COG1121 182 LRELR-REGKTILVVTHDLGAVREyFDRVLLLNRG------LVAHGPPEEVLTPE 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
378-620 |
1.91e-24 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 102.87 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDINLKWWRS 455
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqDVSDLRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 456 KIGVVSQDPLLFSNSiknnikyslyslkdleamenyyeentnDTYENKNFSLisnsmtsnELLEMKKEyqtikdsdvvDV 535
Cdd:cd03292 79 KIGVVFQDFRLLPDR---------------------------NVYENVAFAL--------EVTGVPPR----------EI 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 536 SKKVLIHDFVSSLPDKYDTLvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRI 615
Cdd:cd03292 114 RKRVPAALELVGLSHKHRAL----PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLK--KINKAGT 187
|
....*
gi 124506379 616 TIIIA 620
Cdd:cd03292 188 TVVVA 192
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
378-621 |
2.26e-24 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 102.72 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVeiyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDIN-LKWWRSK 456
Cdd:cd03301 1 VELENVTKRFGNVTAL---DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG----RDVTdLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDpllfsnsiknnikYSLYSLKDLeamenyyeentndtYENKNFSlisnsmtsnelLEMKKEYQTIKDSDVVDVS 536
Cdd:cd03301 74 IAMVFQN-------------YALYPHMTV--------------YDNIAFG-----------LKLRKVPKDEIDERVREVA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 537 KKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 616
Cdd:cd03301 116 ELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTT 184
|
....*
gi 124506379 617 IIIAH 621
Cdd:cd03301 185 IYVTH 189
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
394-1386 |
2.52e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 111.41 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 394 EIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIivndshnlkdinlkWWRSKIGVVSQDPLLFSNSIKN 473
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAERSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 474 NIKYslyslkdleamenYYEENTNDTyenknfslisnsmtsnellemkkeyqtikdSDVVDVSKkvLIHDfVSSLPDKYD 553
Cdd:PTZ00243 740 NILF-------------FDEEDAARL------------------------------ADAVRVSQ--LEAD-LAQLGGGLE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 554 TLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLD-NKSEYLVQKTI-NNLKGnenRITIIIAHRLSTIRYANT 631
Cdd:PTZ00243 774 TEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDaHVGERVVEECFlGALAG---KTRVLATHQVHVVPRADY 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 632 IFVLSnRERsdnnnnnnnddnnnnnnnnnnkINNEGSYI------IEQGTHDSLMKNKNGiyhlminnqkissnkssnng 705
Cdd:PTZ00243 851 VVALG-DGR----------------------VEFSGSSAdfmrtsLYATLAAELKENKDS-------------------- 887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 706 ndngsdnkssayKDSDTGNDADNMNSL---SIHENENISNNRNckNTAENEKEEKVPFFKRMFRRKKKAPNNLRI-IYKE 781
Cdd:PTZ00243 888 ------------KEGDADAEVAEVDAApggAVDHEPPVAKQEG--NAEGGDGAALDAAAGRLMTREEKASGSVPWsTYVA 953
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 782 IFSYkkdvtiiffsilvAGGLYPVFALLYARYVSTLFDFAN-----------LEYNSNKYSIYILLIAIAMFISETLKNY 850
Cdd:PTZ00243 954 YLRF-------------CGGLHAAGFVLATFAVTELVTVSSgvwlsmwstrsFKLSAATYLYVYLGIVLLGTFSVPLRFF 1020
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 851 YNNKIGEKVEKTMKRRLFENILYQEMSFFDQdknTP-GVLSAHINRDVHLLKTGLVNNIVIFSHFIMLFLVSMVMSFYFC 929
Cdd:PTZ00243 1021 LSYEAMRRGSRNMHRDLLRSVSRGTMSFFDT---TPlGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQ 1097
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 930 PIVAAVLT---FIYFINMRVFAVRARltkskEIEKKENMSsgvfafssddemfKDPSF-LIQEAFYNMHTVINYGledyf 1005
Cdd:PTZ00243 1098 PFVLVALVpcgYLYYRLMQFYNSANR-----EIRRIKSVA-------------KSPVFtLLEEALQGSATITAYG----- 1154
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1006 cnlieKAIDYKNKGQKRRIIVNAALwgfsqsaqLFINSFAYWFGSFLIKRGTILVddfmkslFTFIFTGSYAGKLMSlkg 1085
Cdd:PTZ00243 1155 -----KAHLVMQEALRRLDVVYSCS--------YLENVANRWLGVRVEFLSNIVV-------TVIALIGVIGTMLRA--- 1211
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1086 DSENAKL------------------------------SFEK--YY---------PLM-------IRKSNIDVRDDGGIRI 1117
Cdd:PTZ00243 1212 TSQEIGLvslsltmamqttatlnwlvrqvatveadmnSVERllYYtdevphedmPELdeevdalERRTGMAADVTGTVVI 1291
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1118 N---------KNLIKGKVDIKDVNFRYisRPNVP-IYKNLSFTCDSKKTTAIVGETGSGKSTfmnLLLRFYDLkndhiil 1187
Cdd:PTZ00243 1292 EpasptsaapHPVQAGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKST---LLLTFMRM------- 1359
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1188 kndmtnfqdyqnnnnnslvlknvnefsnqsgsaedytVFNNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYE 1267
Cdd:PTZ00243 1360 -------------------------------------VEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQ 1402
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1268 NIKFGREdATLEDVKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALL-REPKILLLDEATSSLDSNS 1346
Cdd:PTZ00243 1403 NVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPAL 1481
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|
gi 124506379 1347 EKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFNN 1386
Cdd:PTZ00243 1482 DRQIQATV--MSAFSAYTVITIAHRLHTVAQYDKIIVMDH 1519
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
398-635 |
2.73e-24 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 102.37 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 398 DLSFTLKEGKTyAFVGESGCGKSTILKLIERLYDPTEGDIIVNDS---HNLKDINLKWWRSKIGVVSQDPLLFSN-SIKN 473
Cdd:cd03297 16 KIDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKKINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 474 NIkysLYSLKDLEAMENYYEENtndtyenknfslisnsmtsnELLemkkeyqtikdsDVVDVSKkvlihdfvsslpdkyd 553
Cdd:cd03297 95 NL---AFGLKRKRNREDRISVD--------------------ELL------------DLLGLDH---------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 554 tLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY-ANTI 632
Cdd:cd03297 124 -LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRI 202
|
...
gi 124506379 633 FVL 635
Cdd:cd03297 203 VVM 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1126-1403 |
2.91e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 105.95 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLR----FYDLkndhiilkndmtnfqdyqnnn 1201
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTT----LLRmiagFETP--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1202 nnslvlknvnefsnqsgsaedytvfnNNGEILLDDinicdynlRDLRNL------FSIVSQEPMLF-NMSIYENIKFGre 1274
Cdd:COG3842 58 --------------------------DSGRILLDG--------RDVTGLppekrnVGMVFQDYALFpHLTVAENVAFG-- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1275 datLEdVKRVSKfAAIDE---------FIESLPNKYdtnvgPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSn 1345
Cdd:COG3842 102 ---LR-MRGVPK-AEIRArvaellelvGLEGLADRY-----P--HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDA- 168
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1346 seKLIEKTIVDIKD---KADKTIITIAH------RIasikrSDKIVVFNnpdrNGTFVQsHGTHDEL 1403
Cdd:COG3842 169 --KLREEMREELRRlqrELGITFIYVTHdqeealAL-----ADRIAVMN----DGRIEQ-VGTPEEI 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1125-1389 |
7.10e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 102.48 E-value: 7.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1125 KVDIKDVNFRYISRPN-VPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnn 1203
Cdd:COG1116 7 ALELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLI----------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1204 slvlknvnefsnqSGSAEDYTvfnnnGEILLDDINICDYNLRdlrnlFSIVSQEPMLFN-MSIYENIKFGREDATL---E 1279
Cdd:COG1116 58 -------------AGLEKPTS-----GEVLVDGKPVTGPGPD-----RGVVFQEPALLPwLTVLDNVALGLELRGVpkaE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1280 DVKRVSKFAAI---DEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1356
Cdd:COG1116 115 RRERARELLELvglAGFEDAYP-----------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLR 183
|
250 260 270
....*....|....*....|....*....|....*
gi 124506379 1357 IKDKADKTIITIAHRIA-SIKRSDKIVVF-NNPDR 1389
Cdd:COG1116 184 LWQETGKTVLFVTHDVDeAVFLADRVVVLsARPGR 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
378-635 |
9.38e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.52 E-value: 9.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVEIyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND----SHNLKDInlkww 453
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaitDDNFEKL----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 454 RSKIGVVSQDPL-LFSNSIknnIKYSLyslkdleamenyyeentndtyenkNFSLISNSMTSNELLEMKKeyQTIKDSDV 532
Cdd:PRK13648 82 RKHIGIVFQNPDnQFVGSI---VKYDV------------------------AFGLENHAVPYDEMHRRVS--EALKQVDM 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 533 VDVSKkvlihdfvsslpdkydtlvgSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNE 612
Cdd:PRK13648 133 LERAD--------------------YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEH 192
|
250 260
....*....|....*....|....
gi 124506379 613 NrITII-IAHRLSTIRYANTIFVL 635
Cdd:PRK13648 193 N-ITIIsITHDLSEAMEADHVIVM 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1145-1388 |
1.36e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.78 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIIlkndmtnfqdyqnnnnnslvlknvnefsnqsgsaedyt 1224
Cdd:PRK14239 22 NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTI-------------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1225 vfnnNGEILLDDINIcdYNLR----DLRNLFSIVSQEPMLFNMSIYENIKFG------REDATL-EDVKRVSKFAAI-DE 1292
Cdd:PRK14239 64 ----TGSIVYNGHNI--YSPRtdtvDLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLdEAVEKSLKGASIwDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1293 FIESLpnkYDTNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRI 1372
Cdd:PRK14239 138 VKDRL---HDSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSM 207
|
250
....*....|....*..
gi 124506379 1373 ASIKR-SDKIVVFNNPD 1388
Cdd:PRK14239 208 QQASRiSDRTGFFLDGD 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
378-639 |
1.57e-23 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 101.22 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHY-DTRKDVeiyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDShNLKDINLKWWRSK 456
Cdd:cd03295 1 IEFENVTKRYgGGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-DIREQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSN-SIKNNIKYSLYSLKdleamenyYEENTNDTyenknfslisnsmTSNELLEMkkeyqtikdsdvVDV 535
Cdd:cd03295 77 IGYVIQQIGLFPHmTVEENIALVPKLLK--------WPKEKIRE-------------RADELLAL------------VGL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 536 SKKvlihdfvsSLPDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 615
Cdd:cd03295 124 DPA--------EFADRY-------PHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKT 188
|
250 260
....*....|....*....|....*
gi 124506379 616 TIIIAHRL-STIRYANTIFVLSNRE 639
Cdd:cd03295 189 IVFVTHDIdEAFRLADRIAIMKNGE 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1126-1383 |
1.71e-23 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 100.73 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPN-VPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRFYDLkndhiilkndmtnfqdyqnnnnns 1204
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKST----LIRCING------------------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1205 lvlknvnefsnqsgsAEDYTvfnnNGEILLDDINICDYNLRDLRNL---FSIVSQEPMLFN-MSIYENIKFGREDATLED 1280
Cdd:cd03258 54 ---------------LERPT----SGSVLVDGTDLTLLSGKELRKArrrIGMIFQHFNLLSsRTVFENVALPLEIAGVPK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1281 VKRVSKfaaIDEFIE--SLPNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1358
Cdd:cd03258 115 AEIEER---VLELLElvGLEDKADA----YPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDIN 187
|
250 260
....*....|....*....|....*.
gi 124506379 1359 DKADKTIITIAHRIASIKR-SDKIVV 1383
Cdd:cd03258 188 RELGLTIVLITHEMEVVKRiCDRVAV 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1126-1404 |
2.65e-23 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 100.45 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPnvPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydlkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRL---------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytVFNNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLF-NMSIYENIKFgreDATLEDVKRV 1284
Cdd:cd03295 51 -------------------IEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFpHMTVEENIAL---VPKLLKWPKE 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1285 SKFAAIDEFIESL---PNKYdtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1361
Cdd:cd03295 109 KIRERADELLALVgldPAEF---ADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL 185
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 124506379 1362 DKTIITIAHRI-ASIKRSDKIVVFNnpdrNGTFVQsHGTHDELL 1404
Cdd:cd03295 186 GKTIVFVTHDIdEAFRLADRIAIMK----NGEIVQ-VGTPDEIL 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
378-596 |
3.17e-23 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 100.00 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDI-NLKWWRSK 456
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG----KDItNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSNSiknnikyslyslkdleamenyyeentnDTYENKNFSlisnsmtsnelLEMKKEYQTIKDSDVVDVS 536
Cdd:cd03300 74 VNTVFQNYALFPHL---------------------------TVFENIAFG-----------LRLKKLPKAEIKERVAEAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 537 KKVLIHDFVSSLPDkydtlvgsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLDNK 596
Cdd:cd03300 116 DLVQLEGYANRKPS-----------QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1126-1383 |
3.98e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 102.05 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRY-ISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDlkndhiilKNDMTNfqdyqnnnnns 1204
Cdd:COG0444 2 LEVRNLKVYFpTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLP--------PPGITS----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1205 lvlknvnefsnqsgsaedytvfnnnGEILLDDINICDYNLRDLRNL----FSIVSQEPML-FN--MSIYENIkfgREdaT 1277
Cdd:COG0444 63 -------------------------GEILFDGEDLLKLSEKELRKIrgreIQMIFQDPMTsLNpvMTVGDQI---AE--P 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1278 LEDVKRVSKFAAIDEFIESLpnkydTNVG-PYGKS--------LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1348
Cdd:COG0444 113 LRIHGGLSKAEARERAIELL-----ERVGlPDPERrldrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQA 187
|
250 260 270
....*....|....*....|....*....|....*.
gi 124506379 1349 LIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1383
Cdd:COG0444 188 QILNLLKDLQRELGLAILFITHDLGVVAEiADRVAV 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1145-1401 |
5.07e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.72 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnslvlknvnefsnqSGSAEDYT 1224
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKIL------------------------------------------SGVYQPDS 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1225 vfnnnGEILLDDINICDYNLRDLRNL-FSIVSQEPMLF-NMSIYENIKFGREDAT--LEDVKRVSKFAAidEFIESL--- 1297
Cdd:COG1129 59 -----GEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVpNLSVAENIFLGREPRRggLIDWRAMRRRAR--ELLARLgld 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1298 --PnkyDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEkTIVDIKDKaDKTIITIAHRIAS 1374
Cdd:COG1129 132 idP---DTPVG----DLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLFR-IIRRLKAQ-GVAIIYISHRLDE 202
|
250 260
....*....|....*....|....*...
gi 124506379 1375 IKR-SDKIVVFnnpdRNGTFVQSHGTHD 1401
Cdd:COG1129 203 VFEiADRVTVL----RDGRLVGTGPVAE 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1126-1386 |
9.32e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 9.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPnVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlknDHIILKNDmtnfqdyqnnnnnsl 1205
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLI--------NGLLLPDD--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfNNNGEILLDDINICDYNLRDLRNLFSIVSQEP--MLFNMSIYENIKFGRED------AT 1277
Cdd:PRK13640 62 ---------------------NPNSKITVDGITLTAKTVWDIREKVGIVFQNPdnQFVGATVGDDVAFGLENravprpEM 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1278 LEDVKRVSKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1357
Cdd:PRK13640 121 IKIVRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKL 189
|
250 260
....*....|....*....|....*....
gi 124506379 1358 KDKADKTIITIAHRIASIKRSDKIVVFNN 1386
Cdd:PRK13640 190 KKKNNLTVISITHDIDEANMADQVLVLDD 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1126-1386 |
1.04e-22 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 96.70 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiILKNDmtnfqdyqnnnnnsl 1205
Cdd:cd03230 1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG---------LLKPD--------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnnNGEILLDDINICDyNLRDLRNLFSIVSQEPMLF-NMSIYENIKfgredatledvkrv 1284
Cdd:cd03230 54 -----------------------SGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYeNLTVRENLK-------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1285 skfaaidefieslpnkydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKT 1364
Cdd:cd03230 96 ---------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKT 147
|
250 260
....*....|....*....|...
gi 124506379 1365 IITIAHRIASI-KRSDKIVVFNN 1386
Cdd:cd03230 148 ILLSSHILEEAeRLCDRVAILNN 170
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1145-1405 |
1.50e-22 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 98.18 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYdlkndhiilKNDmtnfqdyqnnnnnslvlknvnefsnqsgsaedyt 1224
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFI---------KPD---------------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1225 vfnnNGEILLDDINICdyNLRDLRNLFSIVSQEPMLF-NMSIYENIKFG---REDATLEDVKRV---SKFAAIDEFIESL 1297
Cdd:cd03299 53 ----SGKILLNGKDIT--NLPPEKRDISYVPQNYALFpHMTVYKNIAYGlkkRKVDKKEIERKVleiAEMLGIDHLLNRK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1298 PnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-EKLIEKtIVDIKDKADKTIITIAHRIASIK 1376
Cdd:cd03299 127 P-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkEKLREE-LKKIRKEFGVTVLHVTHDFEEAW 194
|
250 260 270
....*....|....*....|....*....|
gi 124506379 1377 R-SDKIVVFnnpdRNGTFVQShGTHDELLS 1405
Cdd:cd03299 195 AlADKVAIM----LNGKLIQV-GKPEEVFK 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1145-1415 |
1.78e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.57 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKK-------------TTAIVGETGSGKSTFMNLLLRFYDLKNDhiilkndmtnfqdyqnnnnnsLVLKNVN 1211
Cdd:PRK14258 11 NNLSFYYDTQKilegvsmeiyqskVTAIIGPSGCGKSTFLKCLNRMNELESE---------------------VRVEGRV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1212 EFSNQSgsaedytVFNNNgeillddinicdYNLRDLRNLFSIVSQEPMLFNMSIYENIKFG------REDATLEDVKRVS 1285
Cdd:PRK14258 70 EFFNQN-------IYERR------------VNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1286 KFAAidEFIESLPNKYDTNvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTI 1365
Cdd:PRK14258 131 LKDA--DLWDEIKHKIHKS----ALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTM 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 124506379 1366 ITIAHRIASIKRSDKIVVF--NNPDRNGTFVQSHGTHDELLSAQDGIYKKYV 1415
Cdd:PRK14258 205 VIVSHNLHQVSRLSDFTAFfkGNENRIGQLVEFGLTKKIFNSPHDSRTREYV 256
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
378-594 |
1.98e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 100.26 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDT-RKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDINLKWWR 454
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDgqDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 455 SKIGVVSQD-PLLFSNSIKNNIKYSL----YSLKDLEAmenyyeentndtyenknfslisnsmTSNELLEMkkeyqtikd 529
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVALPLelagTPKAEIKA-------------------------RVTELLEL--------- 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 530 sdvVDVSKKVlihdfvsslpDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK11153 128 ---VGLSDKA----------DRY-------PAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1125-1386 |
3.34e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.16 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1125 KVDIKDVNFRY--ISRPNVpiyKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnn 1202
Cdd:PRK13635 5 IIRVEHISFRYpdAATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLL---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1203 NSLVLKNvnefsnqsgsaedytvfnnNGEILLDDINICDYNLRDLRNLFSIVSQEP--MLFNMSIYENIKFGREDATL-- 1278
Cdd:PRK13635 54 NGLLLPE-------------------AGTITVGGMVLSEETVWDVRRQVGMVFQNPdnQFVGATVQDDVAFGLENIGVpr 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1279 -EDVKRVSkfAAID-----EFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1352
Cdd:PRK13635 115 eEMVERVD--QALRqvgmeDFLNREPH-----------RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLE 181
|
250 260 270
....*....|....*....|....*....|....
gi 124506379 1353 TIVDIKDKADKTIITIAHRIASIKRSDKIVVFNN 1386
Cdd:PRK13635 182 TVRQLKEQKGITVLSITHDLDEAAQADRVIVMNK 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1126-1404 |
5.44e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 99.07 E-value: 5.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRfydlkndhII--Lkndmtnfqdyqnnnnn 1203
Cdd:COG1118 3 IEVRNISKRF---GSFTLLDDVSLEIASGELVALLGPSGSGKTT----LLR--------IIagL---------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1204 slvlknvnEFSNQsgsaedytvfnnnGEILLDDinicdynlrdlRNLFSIVS----------QEPMLF-NMSIYENIKFG 1272
Cdd:COG1118 52 --------ETPDS-------------GRIVLNG-----------RDLFTNLPprerrvgfvfQHYALFpHMTVAENIAFG 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1273 redatLEdVKRVSKfAAIDE---------FIESLPNKYDTNvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLD 1343
Cdd:COG1118 100 -----LR-VRPPSK-AEIRArveellelvQLEGLADRYPSQ-------LSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1344 SNSEKLIEKTIVDIKDKADKTIITIAH------RIAsikrsDKIVVFNnpdrNGTFVQShGTHDELL 1404
Cdd:COG1118 166 AKVRKELRRWLRRLHDELGGTTVFVTHdqeealELA-----DRVVVMN----QGRIEQV-GTPDEVY 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1126-1386 |
6.53e-22 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 95.40 E-value: 6.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRfydlkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:cd03301 1 VELENVTKRF---GNVTALDDLNLDIADGEFVVLLGPSGCGKTT----TLR----------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 VLKNVNEFSNqsgsaedytvfnnnGEILLDDINICDYNLRDlRNLfSIVSQEPMLF-NMSIYENIKFG------REDATL 1278
Cdd:cd03301 45 MIAGLEEPTS--------------GRIYIGGRDVTDLPPKD-RDI-AMVFQNYALYpHMTVYDNIAFGlklrkvPKDEID 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1279 EDVKRVSKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKT---IV 1355
Cdd:cd03301 109 ERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA---KLRVQMraeLK 174
|
250 260 270
....*....|....*....|....*....|..
gi 124506379 1356 DIKDKADKTIITIAH-RIASIKRSDKIVVFNN 1386
Cdd:cd03301 175 RLQQRLGTTTIYVTHdQVEAMTMADRIAVMND 206
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1128-1386 |
1.06e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.04 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYISRPNVPIYK----NLSFTCDSKKTTAIVGETGSGKSTFMNlllrfydlkndHIilkndmtnfqdyqnnnnN 1203
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQ-----------HL-----------------N 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1204 SLvLKNvnefsnqsgsaedytvfnNNGEILLDDINICD--YNLRDLRNLFSIVSQEP--MLFNMSIYENIKFGREDATLE 1279
Cdd:PRK13637 55 GL-LKP------------------TSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPeyQLFEETIEKDIAFGPINLGLS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1280 D------VKRVSKFAAIDefIESLPNKydtnvGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1353
Cdd:PRK13637 116 EeeienrVKRAMNIVGLD--YEDYKDK-----SPF--ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNK 186
|
250 260 270
....*....|....*....|....*....|....
gi 124506379 1354 IVDIKDKADKTIITIAHRIASI-KRSDKIVVFNN 1386
Cdd:PRK13637 187 IKELHKEYNMTIILVSHSMEDVaKLADRIIVMNK 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1126-1343 |
1.69e-21 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 95.06 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTF---MNLLlrfydlkndhiilkndmtnfqdyqnnnn 1202
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLL---------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1203 nslvlknvnefsnqsgsaEDYTvfnnNGEILLDDINICD--YNLRDLRNLFSIVSQEPMLF-NMSIYENIKFGredatLE 1279
Cdd:COG1126 51 ------------------EEPD----SGTITVDGEDLTDskKDINKLRRKVGMVFQQFNLFpHLTVLENVTLA-----PI 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 1280 DVKRVSKFAAIDEFIESL-----PNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1343
Cdd:COG1126 104 KVKKMSKAEAEERAMELLervglADKADA----YPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
375-640 |
1.79e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.87 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 375 IKKIEFKNVRFHYDTRKDVEiykDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDpTEGDIIV-------NDSHNLKD 447
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILE---GVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVegrveffNQNIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 448 INLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLEAMEnyyeenTNDTYENknfslisnsmtsnellemkkeyqTI 527
Cdd:PRK14258 81 VNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLE------IDDIVES-----------------------AL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 528 KDSDVVDVSKKVlIHdfvsslpdkydtlvgSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINN 607
Cdd:PRK14258 132 KDADLWDEIKHK-IH---------------KSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQS 195
|
250 260 270
....*....|....*....|....*....|....*
gi 124506379 608 LKGNENRITIIIAHRLSTI-RYAN-TIFVLSNRER 640
Cdd:PRK14258 196 LRLRSELTMVIVSHNLHQVsRLSDfTAFFKGNENR 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
378-636 |
2.04e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.40 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSKI 457
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF-EGEDISTLKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSNSIKNNIKYSlyslkdleamenyyeentndtyenknfslisnsmtsnellemkkeYQTIKDSdvvdVSK 537
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFP---------------------------------------------WQIRNQQ----PDP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 KVLIHDFVS-SLPdkyDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 616
Cdd:PRK10247 115 AIFLDDLERfALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAV 191
|
250 260
....*....|....*....|
gi 124506379 617 IIIAHRLSTIRYANTIFVLS 636
Cdd:PRK10247 192 LWVTHDKDEINHADKVITLQ 211
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
58-350 |
2.35e-21 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 96.09 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 58 FISFVCAVLSGGTLPFFIS-VFGVILKNMNLgDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYLRSVF 136
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGrLIDTIIKGGDL-DVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 137 YQDGQFHD-NNPG---SKLRSDLdfylEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVCGVIC 212
Cdd:cd18557 81 RQEIAFFDkHKTGeltSRLSSDT----SVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 213 NKKVKLNKKTSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNKFN--LSETFysKYILKANFVEALHIGLINGLILVSY 290
Cdd:cd18557 157 GRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSeaLDRSY--RLARKKALANALFQGITSLLIYLSL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 291 AFGFWYGTRIIINSatnqypnndfngasviSILLGVLIS----MFMLTI----ILPNITEYMKALEAT 350
Cdd:cd18557 235 LLVLWYGGYLVLSG----------------QLTVGELTSfilyTIMVASsvggLSSLLADIMKALGAS 286
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
378-594 |
2.46e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 95.29 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRK------DVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLK 451
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING-HKLEYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 WwRSK-IGVVSQDPllfSNSIknNIKYSLYSLkdLEAMenyYEENTNdtyenknfslisnsMTSNEllEMKKEYQTIKds 530
Cdd:COG4167 84 Y-RCKhIRMIFQDP---NTSL--NPRLNIGQI--LEEP---LRLNTD--------------LTAEE--REERIFATLR-- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 531 dvvdvskkvlihdFVSSLPDKYDTlvgsNASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:COG4167 135 -------------LVGLLPEHANF----YPHMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
378-637 |
3.41e-21 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 99.37 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRK--------DVEIYKDLSFTLKEGKTYAFVGESGCGKST----ILKLIerlydPTEGDIIVNDS--H 443
Cdd:COG4172 276 LEARDLKVWFPIKRglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQdlD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 444 NLKDINLKWWRSKIGVVSQDPllfsnsiknnikYSlySLkdleamenyyeentndtyeNKNFS---LISNSMTSNELLEM 520
Cdd:COG4172 351 GLSRRALRPLRRRMQVVFQDP------------FG--SL-------------------SPRMTvgqIIAEGLRVHGPGLS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 521 KKEyqtiKDSDVVDVSKKV-L--------IHDFvsslpdkydtlvgsnasklSGGQKQRISIARAIMRNPKILILDEATS 591
Cdd:COG4172 398 AAE----RRARVAEALEEVgLdpaarhryPHEF-------------------SGGQRQRIAIARALILEPKLLVLDEPTS 454
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 124506379 592 SLDnKSeylVQKTINNLKGN---ENRIT-IIIAHRLSTIRY-ANTIFVLSN 637
Cdd:COG4172 455 ALD-VS---VQAQILDLLRDlqrEHGLAyLFISHDLAVVRAlAHRVMVMKD 501
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1124-1394 |
4.27e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 96.68 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1124 GKVDIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRfydlkndhIIlkndmtnfqdyqnnnnn 1203
Cdd:COG3839 2 ASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLR--------MI----------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1204 slvlknvnefsnqsgsA--EDYTvfnnNGEILLDDINICDYNLRDlRNLfSIVSQEPMLF-NMSIYENIKFG----REDA 1276
Cdd:COG3839 50 ----------------AglEDPT----SGEILIGGRDVTDLPPKD-RNI-AMVFQSYALYpHMTVYENIAFPlklrKVPK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1277 TlEDVKRVSKFAA---IDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKT 1353
Cdd:COG3839 108 A-EIDRRVREAAEllgLEDLLDRKP-----------KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA---KLRVEM 172
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124506379 1354 IVDIKD---KADKTII----------TIAHRIASIKRSdKIV-------VFNNPdRNgTFV 1394
Cdd:COG3839 173 RAEIKRlhrRLGTTTIyvthdqveamTLADRIAVMNDG-RIQqvgtpeeLYDRP-AN-LFV 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
378-635 |
5.72e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.87 E-value: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHY-DTRKDVeiYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGD--IIVNDSHNLKDINLKWWR 454
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPA--LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnsKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 455 SKIGVVSQDP--LLFSNSIKNNIKYSLyslkdleamenyyeentndtyENKNFSlisnsmtsnellemKKEYQTIkdsdV 532
Cdd:PRK13640 84 EKVGIVFQNPdnQFVGATVGDDVAFGL---------------------ENRAVP--------------RPEMIKI----V 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 533 VDVSKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNE 612
Cdd:PRK13640 125 RDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLK-KK 192
|
250 260
....*....|....*....|....
gi 124506379 613 NRITII-IAHRLSTIRYANTIFVL 635
Cdd:PRK13640 193 NNLTVIsITHDIDEANMADQVLVL 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
397-637 |
7.06e-21 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 93.17 E-value: 7.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDI-NLKWWRSKIGVVSQDPLLFSN-SIKNN 474
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDItNLPPEKRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 475 IKYSLYSLKdleamenyyeentndtyenknfslisnsmtsnellEMKKEyqtiKDSDVVDVSKKVLIhdfvsslpdkyDT 554
Cdd:cd03299 92 IAYGLKKRK-----------------------------------VDKKE----IERKVLEIAEMLGI-----------DH 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 555 LVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEylvQKTINNLK--GNENRITII-IAHRLSTIRY-AN 630
Cdd:cd03299 122 LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK---EKLREELKkiRKEFGVTVLhVTHDFEEAWAlAD 198
|
....*..
gi 124506379 631 TIFVLSN 637
Cdd:cd03299 199 KVAIMLN 205
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
377-636 |
9.81e-21 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 93.43 E-value: 9.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 377 KIEFKNVRFHYDTRKDvEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSK 456
Cdd:cd03288 19 EIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI-DGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSNSIKNNIkyslyslkDLEAmenyyeENTNDTYEnknfslisnsmtsnELLEMKKeyqtikdsdvvdvs 536
Cdd:cd03288 97 LSIILQDPILFSGSIRFNL--------DPEC------KCTDDRLW--------------EALEIAQ-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 537 kkvlIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRIT 616
Cdd:cd03288 135 ----LKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTV 208
|
250 260
....*....|....*....|
gi 124506379 617 IIIAHRLSTIRYANTIFVLS 636
Cdd:cd03288 209 VTIAHRVSTILDADLVLVLS 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
378-620 |
1.02e-20 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 92.18 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVEIyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDiNLKWWRSKI 457
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING-YSIRT-DRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSNsiknnikyslyslkdleamenyyeentndtyenknfslisnsMTSNELLE----MKKEYQTIKDSDVV 533
Cdd:cd03263 78 GYCPQFDALFDE------------------------------------------LTVREHLRfyarLKGLPKSEIKEEVE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 DVSKKVlihdfvsSLPDKYDTLvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnEN 613
Cdd:cd03263 116 LLLRVL-------GLTDKANKR----ARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR--KG 182
|
....*..
gi 124506379 614 RiTIIIA 620
Cdd:cd03263 183 R-SIILT 188
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
57-303 |
1.38e-20 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 93.64 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 57 LFISFVCAVLSGGTLPFFISVFGVILKNMNLGDD---INPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYLR 133
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDleaLLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 134 SVFYQDGQFHDNNPGSKLRSDLDFYLEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVCGVICN 213
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 214 KKVKLNKKTSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNKFN-LSETFYsKYILKANFVEALHIGLINGLILVSYAF 292
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRkANERLR-RLSMKIARARALSSPLMELLGAIAIAL 239
|
250
....*....|.
gi 124506379 293 GFWYGTRIIIN 303
Cdd:cd18552 240 VLWYGGYQVIS 250
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
377-635 |
1.53e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 93.69 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 377 KIEFKNVRFHYD--TRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND---SHNLKDINLK 451
Cdd:PRK13646 2 TIRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 WWRSKIGVVSQDP--LLFSNSIKNNIKYSlyslkdleamenyyeentndtyeNKNFslisnsmtsNELLEMKKEYQtikd 529
Cdd:PRK13646 82 PVRKRIGMVFQFPesQLFEDTVEREIIFG-----------------------PKNF---------KMNLDEVKNYA---- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 530 sdvvdvskkvliHDFVSSLPDKYDTLVGSnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLK 609
Cdd:PRK13646 126 ------------HRLLMDLGFSRDVMSQS-PFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQ 192
|
250 260
....*....|....*....|....*..
gi 124506379 610 GNENRITIIIAHRLSTI-RYANTIFVL 635
Cdd:PRK13646 193 TDENKTIILVSHDMNEVaRYADEVIVM 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1126-1405 |
1.54e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 93.26 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnNSL 1205
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLI----------------------------DGL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 VlknvnefsnqsgSAEdytvfnnNGEILLDDINICDYNLRDLRNLFSIVSQEP--MLFNMSIYENIKFGREDATL---ED 1280
Cdd:PRK13650 57 L------------EAE-------SGQIIIDGDLLTEENVWDIRHKIGMVFQNPdnQFVGATVEDDVAFGLENKGIpheEM 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1281 VKRVSK---FAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1357
Cdd:PRK13650 118 KERVNEaleLVGMQDFKEREPAR-----------LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGI 186
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 124506379 1358 KDKADKTIITIAHRIASIKRSDKIVVFNNPDrngtfVQSHGTHDELLS 1405
Cdd:PRK13650 187 RDDYQMTVISITHDLDEVALSDRVLVMKNGQ-----VESTSTPRELFS 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
370-594 |
2.02e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 92.93 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 370 ETLpnikkIEFKNVR--FHYDT----RKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsH 443
Cdd:PRK15112 2 ETL-----LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD-H 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 444 NLKDINLKWWRSKIGVVSQDPllfSNSIknNIKYSLYSLKDleamenyyeentndtyenknFSLISNSMTSNELLEmKKE 523
Cdd:PRK15112 76 PLHFGDYSYRSQRIRMIFQDP---STSL--NPRQRISQILD--------------------FPLRLNTDLEPEQRE-KQI 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124506379 524 YQTIKDsdvvdvskkvlihdfVSSLPDKydtlVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK15112 130 IETLRQ---------------VGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1118-1410 |
2.51e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.51 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1118 NKNLIKgkvdIKDVNFRYISRPNVPIyKNLSFTCDSKKTTAIVGETGSGKSTFMNLllrfydlkndhiilkndMTNFQDY 1197
Cdd:PRK13648 4 KNSIIV----FKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKL-----------------MIGIEKV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1198 QNnnnnslvlknvnefsnqsgsaedytvfnnnGEILLDDINICDYNLRDLRNLFSIVSQEP-MLFNMSIYE-NIKFGRE- 1274
Cdd:PRK13648 62 KS------------------------------GEIFYNNQAITDDNFEKLRKHIGIVFQNPdNQFVGSIVKyDVAFGLEn 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1275 -----DATLEDVKRVSKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1349
Cdd:PRK13648 112 havpyDEMHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124506379 1350 IEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNnpdrNGTfVQSHGTHDELLSAQDGI 1410
Cdd:PRK13648 181 LLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMN----KGT-VYKEGTPTEIFDHAEEL 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1126-1382 |
2.98e-20 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 90.67 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPnvpIYKNLSFTCDSKKTTAIVGETGSGKSTF---MNLLlrfydlkndhiilkndmtnfqdyqnnnn 1202
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLL---------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1203 nslvlknvnefsnqsgsaEDYTvfnnNGEILLDDINICD--YNLRDLRNLFSIVSQEPMLF-NMSIYENIKFGredatLE 1279
Cdd:cd03262 50 ------------------EEPD----SGTIIIDGLKLTDdkKNINELRQKVGMVFQQFNLFpHLTVLENITLA-----PI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1280 DVKRVSKFAAIDEFIE-----SLPNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1354
Cdd:cd03262 103 KVKGMSKAEAEERALEllekvGLADKADA----YPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVM 178
|
250 260
....*....|....*....|....*....
gi 124506379 1355 VDIKdKADKTIITIAHRIASIKR-SDKIV 1382
Cdd:cd03262 179 KDLA-EEGMTMVVVTHEMGFAREvADRVI 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
380-602 |
3.42e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 380 FKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNdshnlKDInlkwwrsKIGV 459
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-----KGL-------RIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 460 VSQDPLLFSN-SIKNNIKYSLYSLKDLEA-MENYYEENTNDTYENKNFSLISnsmtsnELLEMKKEYQTikDSDVvdvsK 537
Cdd:COG0488 66 LPQEPPLDDDlTVLDTVLDGDAELRALEAeLEELEAKLAEPDEDLERLAELQ------EEFEALGGWEA--EARA----E 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124506379 538 KVLihdfvSSL---PDKYDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKS-----EYLVQ 602
Cdd:COG0488 134 EIL-----SGLgfpEEDLDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKN 197
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
378-596 |
3.60e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.67 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKD--INLKWWRS 455
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG----RDlfTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 456 KIGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEAmenyyeentndtyENKnfslisnsMTSNELLEMkkeyqtikdsdvVD 534
Cdd:COG1118 76 RVGFVFQHYALFPHmTVAENIAFGLRVRPPSKA-------------EIR--------ARVEELLEL------------VQ 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 535 vskkvlihdfVSSLPDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNK 596
Cdd:COG1118 123 ----------LEGLADRY-------PSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
397-635 |
4.83e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.47 E-value: 4.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN----DSHNLKDInlkwWRSKIGVVSQDPLLFSNsik 472
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgepvRFRSPRDA----QAAGIAIIHQELNLVPN--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 473 nnikyslyslkdLEAMENYYEENtndtyENKNFSLISNSmtsnellEMKKEYQTIKDSDVVDVSkkvlihdfvsslPDky 552
Cdd:COG1129 94 ------------LSVAENIFLGR-----EPRRGGLIDWR-------AMRRRARELLARLGLDID------------PD-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 553 dTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNK-SEYLVqKTINNLKgnENRITII-IAHRLSTIRY-A 629
Cdd:COG1129 136 -TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLF-RIIRRLK--AQGVAIIyISHRLDEVFEiA 207
|
....*.
gi 124506379 630 NTIFVL 635
Cdd:COG1129 208 DRVTVL 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1228-1385 |
1.11e-19 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 89.60 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1228 NNGEILLDDINIcdYNLRDLRNLFSIVSQEPMLF-NMSIYENIKFG------REDATLEDVKRVSKFAAIDEFIESLPNK 1300
Cdd:cd03300 53 TSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPSQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1301 ydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK---TIITIAH-RIASIK 1376
Cdd:cd03300 131 -----------LSGGQQQRVAIARALVNEPKVLLLDEPLGALDL---KLRKDMQLELKRLQKElgiTFVFVTHdQEEALT 196
|
....*....
gi 124506379 1377 RSDKIVVFN 1385
Cdd:cd03300 197 MSDRIAVMN 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
378-637 |
1.13e-19 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 87.48 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN----DSHNLKDInlkwW 453
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDgkevSFASPRDA----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 454 RSKIGVVSQdpllfsnsiknnikyslyslkdleamenyyeentndtyenknfslisnsmtsnellemkkeyqtikdsdvv 533
Cdd:cd03216 74 RAGIAMVYQ----------------------------------------------------------------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 dvskkvlihdfvsslpdkydtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnEN 613
Cdd:cd03216 83 -----------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLR--AQ 131
|
250 260
....*....|....*....|....*.
gi 124506379 614 RITII-IAHRLSTI-RYANTIFVLSN 637
Cdd:cd03216 132 GVAVIfISHRLDEVfEIADRVTVLRD 157
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1126-1370 |
1.21e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 89.34 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfyDLKNDHiilkndmtnfqdyqnnnnnsl 1205
Cdd:COG2884 2 IRFENVSKRY--PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG--EERPTS--------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnnnGEILLDDINICDYNLRDLRNL---FSIVSQE-PMLFNMSIYENIKF-----GREDA 1276
Cdd:COG2884 57 ------------------------GQVLVNGQDLSRLKRREIPYLrrrIGVVFQDfRLLPDRTVYENVALplrvtGKSRK 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1277 TLEdvKRVSkfAAIDEFieSLPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIE---- 1351
Cdd:COG2884 113 EIR--RRVR--EVLDLV--GLSDKAKALPH----ELSGGEQQRVAIARALVNRPELLLADEPTGNLDpETSWEIMEllee 182
|
250 260 270
....*....|....*....|....*....|
gi 124506379 1352 -----KTIV------DIKDKADKTIITIAH 1370
Cdd:COG2884 183 inrrgTTVLiathdlELVDRMPKRVLELED 212
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
63-356 |
1.78e-19 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 91.18 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 63 CAVLSGGTLPFFISVFGVIL-------------KNMNLGDDINP----------IILSLVSIGLVQFILSMISSYCMDVI 119
Cdd:cd18558 7 CAIIHGGLLPAFMVIFGDMTdsftnggmtnitgNSSGLNSSAGPfekleeemtlYAYYYLIIGAIVLITAYIQGSFWGLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 120 TSKILKTLKLEYLRSVFYQDGQFHDNNPGSKLRSDLDFYLEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCIT 199
Cdd:cd18558 87 AGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 200 CVFPLIYVCGVICNKKVKLNKKTSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNKFNLSETFYSKYILKANFVEALHI 279
Cdd:cd18558 167 AISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISM 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 280 GLINGLILVSYAFGFWYGTRIIInsatnqypNNDFNGASVISILLGVLISMFMLTIILPNITEYMKaleATNSLYEI 356
Cdd:cd18558 247 GAAFLLIYASYALAFWYGTYLVT--------QQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFAN---ARGAAYHI 312
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
397-619 |
2.23e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.46 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYD--PT---EGDIIVNDsHNL--KDINLKWWRSKIGVVSQDPLLFSN 469
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHG-KNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 470 SIKNNIKYSlyslkdleAMENYYEENTndtyenknfslisnsmtsNELLEmkkeyQTIKDSDVVDVSKkvlihdfvsslp 549
Cdd:PRK14243 106 SIYDNIAYG--------ARINGYKGDM------------------DELVE-----RSLRQAALWDEVK------------ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 550 DKYDTlvgsNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgneNRITIII 619
Cdd:PRK14243 143 DKLKQ----SGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK---EQYTIII 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1230-1404 |
2.91e-19 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 89.24 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDDINICDYNLRDLRNL----FSIVSQEPMLF-NMSIYENIKFG----------REDATLEDVKRVskfaAIDEFI 1294
Cdd:cd03294 79 GKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTVLENVAFGlevqgvpraeREERAAEALELV----GLEGWE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1295 ESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA- 1373
Cdd:cd03294 155 HKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDe 223
|
170 180 190
....*....|....*....|....*....|.
gi 124506379 1374 SIKRSDKIVVFnnpdRNGTFVQShGTHDELL 1404
Cdd:cd03294 224 ALRLGDRIAIM----KDGRLVQV-GTPEEIL 249
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
397-635 |
3.03e-19 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 89.24 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDINLKWWRSK-IGVVSQDPLLFSN-SIK 472
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqDIAAMSRKELRELRRKkISMVFQSFALLPHrTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 473 NNIKYSLyslkdleamenyyeentndtyenknfslisnsmtsnELLEMKKEyqtIKDSDVVDVSKKVLIHDFVSSLPDKy 552
Cdd:cd03294 121 ENVAFGL------------------------------------EVQGVPRA---EREERAAEALELVGLEGWEHKYPDE- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 553 dtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANT 631
Cdd:cd03294 161 ----------LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDeALRLGDR 230
|
....
gi 124506379 632 IFVL 635
Cdd:cd03294 231 IAIM 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1124-1375 |
5.07e-19 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 88.76 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1124 GKVDIKDVNFRYISRPNVpIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiilkndmtnfqdyqnnnnn 1203
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLR--------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1204 slvlknvnefsnqsgsaedytVFNNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIK-FGREDAtlEDVK 1282
Cdd:cd03289 53 ---------------------LLNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLDpYGKWSD--EEIW 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1283 RVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKAD 1362
Cdd:cd03289 110 KVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFAD 187
|
250
....*....|...
gi 124506379 1363 KTIITIAHRIASI 1375
Cdd:cd03289 188 CTVILSEHRIEAM 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1128-1408 |
5.08e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.50 E-value: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYISRPnvpiyKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNdhiilkndmtnfqdyqnnnnnslvl 1207
Cdd:COG3840 4 LDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDS------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqsgsaedytvfnnnGEILLDDINICDYN--LRdlrnLFSIVSQEPMLFN-MSIYENIKFGREDA---TLEDV 1281
Cdd:COG3840 54 ----------------------GRILWNGQDLTALPpaER----PVSMLFQENNLFPhLTVAQNIGLGLRPGlklTAEQR 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1282 KRVSKFAA---IDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN--SEKLIEktIVD 1356
Cdd:COG3840 108 AQVEQALErvgLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAlrQEMLDL--VDE 174
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 124506379 1357 IKDKADKTIITIAHRIASIKR-SDKIVVFNnpdrNGTfVQSHGTHDELLSAQD 1408
Cdd:COG3840 175 LCRERGLTVLMVTHDPEDAARiADRVLLVA----DGR-IAADGPTAALLDGEP 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
397-635 |
5.54e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.95 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSH-NLKDINLKWWRSKIGVVSQDP--LLFSNSIKN 473
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDiTDKKVKLSDIRKKVGLVFQYPeyQLFEETIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 474 NIKYSLYSLKDLEamenyyEENTNDTYENKNFslisnsmtsnelleMKKEYQTIKDSDVVDvskkvlihdfvsslpdkyd 553
Cdd:PRK13637 104 DIAFGPINLGLSE------EEIENRVKRAMNI--------------VGLDYEDYKDKSPFE------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 554 tlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTI 632
Cdd:PRK13637 145 ---------LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRI 215
|
...
gi 124506379 633 FVL 635
Cdd:PRK13637 216 IVM 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
378-626 |
5.58e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 88.22 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEG-DIIVNDsHNLKDINLKWWRSK 456
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFG-ERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQdpllfsnsiknnikyslyslkdleAMENYYEENTN--DTyenknfsLISNSMTSNELlemkkeYQTIKDSDVvd 534
Cdd:COG1119 80 IGLVSP------------------------ALQLRFPRDETvlDV-------VLSGFFDSIGL------YREPTDEQR-- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 535 vsKKV--LIHDF-VSSLPDK-YDTLvgsnasklSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKG 610
Cdd:COG1119 121 --ERAreLLELLgLAHLADRpFGTL--------SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAA 190
|
250
....*....|....*.
gi 124506379 611 NENRITIIIAHRLSTI 626
Cdd:COG1119 191 EGAPTLVLVTHHVEEI 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1146-1384 |
5.75e-19 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 86.97 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1146 NLSFTCDSKkTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILkndmtnfqdyqnnnnnslvlknvnefsnqsgsaedytv 1225
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-------------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1226 fnnNGEILLD-DINIcdyNLRDLRNLFSIVSQEPMLF-NMSIYENIKFG-REDATLEDVKRVSKFaaIDEF-IESLPNKY 1301
Cdd:cd03297 57 ---NGTVLFDsRKKI---NLPPQQRKIGLVFQQYALFpHLNVRENLAFGlKRKRNREDRISVDEL--LDLLgLDHLLNRY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1302 dtnvgPYGksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDK 1380
Cdd:cd03297 129 -----PAQ--LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADR 201
|
....
gi 124506379 1381 IVVF 1384
Cdd:cd03297 202 IVVM 205
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
792-1083 |
6.09e-19 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 88.77 E-value: 6.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 792 IFFSIL--VAGGLYPVFALLYARYVSTLFDFANLeynsNKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFE 869
Cdd:cd18557 2 LLFLLIssAAQLLLPYLIGRLIDTIIKGGDLDVL----NELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 870 NILYQEMSFFdqDKNTPGVLSAHINRDVHLLKTGLVNNIVIFSHFIMLFLVSMVMSFYFCP---IVAAVLTFIYFINMRV 946
Cdd:cd18557 78 SLLRQEIAFF--DKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWkltLVLLLVIPLLLIASKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 947 FAVRARlTKSKEIEKKenmssgvFAFSSDdemfkdpsfLIQEAFYNMHTVINYGLEDYFCNLIEKAID-YKNKGQKRriI 1025
Cdd:cd18557 156 YGRYIR-KLSKEVQDA-------LAKAGQ---------VAEESLSNIRTVRSFSAEEKEIRRYSEALDrSYRLARKK--A 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1026 VNAALWGFSQSAQLFINSFA-YWFGSFLIKRGTILVDDfmksLFTFI-FTGSYAGKLMSL 1083
Cdd:cd18557 217 LANALFQGITSLLIYLSLLLvLWYGGYLVLSGQLTVGE----LTSFIlYTIMVASSVGGL 272
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
56-303 |
8.47e-19 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 88.38 E-value: 8.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 56 LLFISFVCAVLSGGTLPFFISV---FGVILKNMNLgddINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYL 132
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLlidDVIPAGDLSL---LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 133 RSVFYQDGQFHDNNP-G---SKLRSDLDfyleQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVC 208
Cdd:cd07346 80 RHLQRLSLSFFDRNRtGdlmSRLTSDVD----AVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 209 GVICNKKVKLNKKTSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNKFNLSETFYSKYILKANFVEALHIGLINGLILV 288
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250
....*....|....*
gi 124506379 289 SYAFGFWYGTRIIIN 303
Cdd:cd07346 236 GTALVLLYGGYLVLQ 250
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1127-1370 |
1.02e-18 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 86.16 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1127 DIKDVNFRYisRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnslv 1206
Cdd:cd03226 1 RIENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKIL-------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1207 lknvnefsnqSGSAEDYtvfnnNGEILLDDINICdynLRDLRNLFSIVSQEP--MLFNMSIYENIKFGREDA--TLEDVK 1282
Cdd:cd03226 47 ----------AGLIKES-----SGSILLNGKPIK---AKERRKSIGYVMQDVdyQLFTDSVREELLLGLKELdaGNEQAE 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1283 RVSKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKAD 1362
Cdd:cd03226 109 TVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELA-AQG 176
|
....*...
gi 124506379 1363 KTIITIAH 1370
Cdd:cd03226 177 KAVIVITH 184
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
400-594 |
1.53e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 88.48 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 400 SFTLKEGKTYAFVGESGCGKSTI---LKLIERlydPTEG-------DIIVNDSHNLKDInlkwwRSKIGVVSQDPllfsn 469
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLarlLTMIET---PTGGelyyqgqDLLKADPEAQKLL-----RQKIQIVFQNP----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 470 siknnikYSlySLKDLEAMENYYEENTndtyenknfsLISNSMTSNEllemKKEyqtikdsDVVDVSKKVLIHdfvsslP 549
Cdd:PRK11308 102 -------YG--SLNPRKKVGQILEEPL----------LINTSLSAAE----RRE-------KALAMMAKVGLR------P 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 124506379 550 DKYDTLvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK11308 146 EHYDRY----PHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
378-622 |
1.54e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.75 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVeiyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIVNdSHNL-----KD 447
Cdd:PRK14239 6 LQVSDLSVYYNKKKAL---NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYN-GHNIysprtDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 448 INLkwwRSKIGVVSQDPLLFSNSIKNNIKYSLY--SLKDLEAMENYYEEntndtyenknfSLISNSMtsnellemkkeYQ 525
Cdd:PRK14239 82 VDL---RKEIGMVFQQPNPFPMSIYENVVYGLRlkGIKDKQVLDEAVEK-----------SLKGASI-----------WD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 526 TIKDSdvvdvskkvlIHDfvsslpdkydtlvgsNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTI 605
Cdd:PRK14239 137 EVKDR----------LHD---------------SALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETL 191
|
250
....*....|....*..
gi 124506379 606 NNLKgneNRITIIIAHR 622
Cdd:PRK14239 192 LGLK---DDYTMLLVTR 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1126-1384 |
1.68e-18 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 85.62 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPnvpiyKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYdlkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFE--------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefSNQSGSaedytvfnnngeILLDDInicDYNLRDL-RNLFSIVSQEPMLF-NMSIYENIKFGREDA---TLED 1280
Cdd:cd03298 49 --------TPQSGR------------VLINGV---DVTAAPPaDRPVSMLFQENNLFaHLTVEQNVGLGLSPGlklTAED 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1281 VKRVSKFAA---IDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1357
Cdd:cd03298 106 RQAIEVALArvgLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
250 260
....*....|....*....|....*..
gi 124506379 1358 KDKADKTIITIAHRIASIKRSDKIVVF 1384
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVF 201
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
390-621 |
1.93e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 85.79 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 390 RKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDP---TEGDIIVNDSHNLKDInlkwWRSKIGVVSQDPLL 466
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQ----FQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 467 fsnsiknnikyslysLKDLEAMEN-YYEENTNDTYENKNFslisnsmtsnellemkkeyqtikdsdvvdVSKKVlihDFV 545
Cdd:cd03234 93 ---------------LPGLTVRETlTYTAILRLPRKSSDA-----------------------------IRKKR---VED 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 546 SSLPDKYDTLVGSNASK-LSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAH 621
Cdd:cd03234 126 VLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQL-ARRNRIVILTIH 201
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
378-627 |
1.93e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 86.22 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTrkdVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSH-------NLKDINL 450
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkpSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 451 kwWRSKIGVVSQdpllfsnsiknniKYSLYSlkDLEAMENyyeentndtyenknfsLISNSMtsnELLEMKKEyqtikds 530
Cdd:COG4161 80 --LRQKVGMVFQ-------------QYNLWP--HLTVMEN----------------LIEAPC---KVLGLSKE------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 531 DVVDVSKKVL----IHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTIN 606
Cdd:COG4161 117 QAREKAMKLLarlrLTDKADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIR 185
|
250 260
....*....|....*....|..
gi 124506379 607 NLKGNEnrIT-IIIAHRLSTIR 627
Cdd:COG4161 186 ELSQTG--ITqVIVTHEVEFAR 205
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1145-1385 |
2.13e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 86.76 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRFYDLKNDHIilkndmtnfqdyqnnnnnslvlknvnefsnQSGSAEdyt 1224
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKST----ILRCFNRLNDLI------------------------------PGFRVE--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1225 vfnnnGEILLDDINICDYNLR--DLRNLFSIVSQEPMLFNMSIYENIKFGredatledvKRVSKFAA-IDEFIE------ 1295
Cdd:PRK14243 70 -----GKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPKSIYDNIAYG---------ARINGYKGdMDELVErslrqa 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1296 SLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASI 1375
Cdd:PRK14243 136 ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQA 213
|
250
....*....|.
gi 124506379 1376 KR-SDKIVVFN 1385
Cdd:PRK14243 214 ARvSDMTAFFN 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1136-1343 |
2.61e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 85.23 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1136 ISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLrfydlkndhiilkndmtnfqdyqnnnnnslvlknvnefsn 1215
Cdd:COG4136 9 ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA---------------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1216 qsGSAEDytVFNNNGEILLDDINICDYN--LRDLRNLFsivsQEPMLF-NMSIYENIKFgredATLEDVKRVSKFAAIDE 1292
Cdd:COG4136 49 --GTLSP--AFSASGEVLLNGRRLTALPaeQRRIGILF----QDDLLFpHLSVGENLAF----ALPPTIGRAQRRARVEQ 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 124506379 1293 FIES--LPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1343
Cdd:COG4136 117 ALEEagLAGFADRDPA----TLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1125-1415 |
4.36e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.35 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1125 KVDIKDVNfryISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnns 1204
Cdd:PRK14247 3 KIEIRDLK---VSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIEL------------------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1205 lvlknvnefsnqsgsaedYTVFNNNGEILLDDINICDYNLRDLRNLFSIVSQEPM-LFNMSIYENIKFGREDATLEDVK- 1282
Cdd:PRK14247 56 ------------------YPEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpIPNLSIFENVALGLKLNRLVKSKk 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1283 ----RVSKFAAIDEFIESLPNKYDtnvGPYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1358
Cdd:PRK14247 118 elqeRVRWALEKAQLWDEVKDRLD---APAGK-LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELK 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1359 DkaDKTIITIAHRIASIKRSDKIVVFNnpdRNGTFVQSHGTHDELLSAQDGIYKKYV 1415
Cdd:PRK14247 194 K--DMTIVLVTHFPQQAARISDYVAFL---YKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
378-628 |
4.81e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.07 E-value: 4.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTR----------KDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNdSHNLKD 447
Cdd:PRK15079 9 LEVADLKVHFDIKdgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL-GKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 448 INLKWW---RSKIGVVSQDPLLFSN---SIKNNIKyslyslkdlEAMENYYEentndtyenknfslisnsmtsnellEMK 521
Cdd:PRK15079 88 MKDDEWravRSDIQMIFQDPLASLNprmTIGEIIA---------EPLRTYHP-------------------------KLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 522 KeyQTIKDSdVVDVSKKV-LIHDFVSSLPDKYdtlvgsnasklSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYL 600
Cdd:PRK15079 134 R--QEVKDR-VKAMMLKVgLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 199
|
250 260 270
....*....|....*....|....*....|.
gi 124506379 601 VqktINNLKG--NENRITII-IAHRLSTIRY 628
Cdd:PRK15079 200 V---VNLLQQlqREMGLSLIfIAHDLAVVKH 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
391-626 |
6.66e-18 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 83.81 E-value: 6.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 391 KDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDINLkwwRSKIGVVSQDPLLFSNs 470
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA---LRRIGALIEAPGFYPN- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 471 iknnikyslyslkdLEAMENYYeenTNDTYENKNFSLIsnsmtsNELLEMKKEYQTIKdsdvvdvsKKVlihdfvsslpd 550
Cdd:cd03268 87 --------------LTARENLR---LLARLLGIRKKRI------DEVLDVVGLKDSAK--------KKV----------- 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 551 kydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnrITIIIA-HRLSTI 626
Cdd:cd03268 125 ----------KGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQG--ITVLISsHLLSEI 189
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
378-596 |
6.73e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 87.31 E-value: 6.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRkdvEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDIN-LKWWRSK 456
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG----QDIThVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSN-SIKNNIKYSLyslkdleamenyyeentndtyenknfslisnsmtsnellEMKK-EYQTIKdSDVVD 534
Cdd:PRK09452 88 VNTVFQSYALFPHmTVFENVAFGL---------------------------------------RMQKtPAAEIT-PRVME 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 535 VSKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNK 596
Cdd:PRK09452 128 ALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
378-635 |
8.03e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.52 E-value: 8.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHY-DTRKDVEIY--KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDINLKWWR 454
Cdd:PRK13633 5 IKCKNVSYKYeSNEESTEKLalDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 455 SKIGVVSQDPllfSNSIKNNIkyslyslkdleamenyYEENTNDTYENKNFslisnsmtsnELLEMKKEyqtikdsdVVD 534
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVATI----------------VEEDVAFGPENLGI----------PPEEIRER--------VDE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 535 VSKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 614
Cdd:PRK13633 128 SLKKVGMYEYRRHAP-----------HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGI 196
|
250 260
....*....|....*....|.
gi 124506379 615 ITIIIAHRLSTIRYANTIFVL 635
Cdd:PRK13633 197 TIILITHYMEEAVEADRIIVM 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1140-1382 |
1.10e-17 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 84.16 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1140 NVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRfydlkndHIilkndmtnfqdyqnnnnNSLVlknvnefsnqsgs 1219
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKST----LLR-------CL-----------------NGLV------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1220 aEDytvfnNNGEILLDDINICDYNLRDLRNLFS---IVSQEPMLFN-MSIYENIKFGREDA-----------TLEDVKRV 1284
Cdd:cd03256 52 -EP-----TSGSVLIDGTDINKLKGKALRQLRRqigMIFQQFNLIErLSVLENVLSGRLGRrstwrslfglfPKEEKQRA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1285 skFAAIDEF-IESLPNKY-DTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAD 1362
Cdd:cd03256 126 --LAALERVgLLDKAYQRaDQ--------LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEG 195
|
250 260
....*....|....*....|.
gi 124506379 1363 KTIITIAHRIASIKR-SDKIV 1382
Cdd:cd03256 196 ITVIVSLHQVDLAREyADRIV 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
378-628 |
1.15e-17 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 84.47 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDT------RKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDIN 449
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 450 LKWWRSKIGVVSQDPLLFSN---SIKNNIKYSLYSLKDLEAMENyyEENTNdtyenknfslisnsmtsnELLEMkkeyqt 526
Cdd:TIGR02769 83 RRAFRRDVQLVFQDSPSAVNprmTVRQIIGEPLRHLTSLDESEQ--KARIA------------------ELLDM------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 527 ikdsdvVDVSKKVLihdfvsslpDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTIN 606
Cdd:TIGR02769 137 ------VGLRSEDA---------DKL-------PRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLR 194
|
250 260
....*....|....*....|..
gi 124506379 607 NLKGNENRITIIIAHRLSTIRY 628
Cdd:TIGR02769 195 KLQQAFGTAYLFITHDLRLVQS 216
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
791-1082 |
1.21e-17 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 85.29 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 791 IIFFSILVAGGLYPVFALLYARYVSTLFDFANLEYNsNKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFEN 870
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLL-LWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 871 ILYQEMSFFdqDKNTPGVLSAHINRDVHLLKTGLVNNIVIFSHFIMLFLVSMVMSFYFCP---IVAAVLTFIYFINMRVF 947
Cdd:cd07346 82 LQRLSLSFF--DRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWkltLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 948 AVRARLTkSKEI-EKKENMSSgvfafssddemfkdpsfLIQEAFYNMHTVINYGLEDY----FCNLIEKAIDYKNKGQKR 1022
Cdd:cd07346 160 RRRIRKA-SREVrESLAELSA-----------------FLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1023 RIIVNAALWGFSQSAQLFInsfaYWFGSFLIKRGTILVDDfmksLFTFIftgSYAGKLMS 1082
Cdd:cd07346 222 SALFSPLIGLLTALGTALV----LLYGGYLVLQGSLTIGE----LVAFL---AYLGMLFG 270
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
378-596 |
2.09e-17 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 83.16 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVEiykDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND----SHNLKDINlkww 453
Cdd:cd03296 3 IEVRNVSKRFGDFVALD---DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatDVPVQERN---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 454 rskIGVVSQDPLLFSN-SIKNNIKYSLyslkdleAMENYYEENTNDTYENKnfslisnsmtSNELLEMKKeyqtikdsdv 532
Cdd:cd03296 76 ---VGFVFQHYALFRHmTVFDNVAFGL-------RVKPRSERPPEAEIRAK----------VHELLKLVQ---------- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 533 vdvskkvlihdfVSSLPDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNK 596
Cdd:cd03296 126 ------------LDWLADRY-------PAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
378-637 |
2.95e-17 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 81.86 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVeiyKDLSFTLKEGkTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDINlkWWRSKI 457
Cdd:cd03264 1 LQLENLTKRYGKKRAL---DGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ--KLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSNsiknnikyslyslkdleamenyyeentndtyenknfslisnsMTSNELLE----MKKEYQTIKDSDVV 533
Cdd:cd03264 75 GYLPQEFGVYPN------------------------------------------FTVREFLDyiawLKGIPSKEVKARVD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 DVSKKVlihdfvsSLPDKYDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkgNEN 613
Cdd:cd03264 113 EVLELV-------NLGDRAKKKIGS----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL--GED 179
|
250 260
....*....|....*....|....*
gi 124506379 614 RITIIIAHRLSTIRY-ANTIFVLSN 637
Cdd:cd03264 180 RIVILSTHIVEDVESlCNQVAVLNK 204
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1139-1386 |
2.95e-17 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 82.38 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1139 PNVPIYKNLSFTCDSKKTTAIVGETGSGKStfmnlllrfydlkndhiilkndmtnfqdyqnnnnnSLVLKNVNEFSNQSG 1218
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKS-----------------------------------SLLLAILGEMQTLEG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1219 SaedytVFNNNgeILLDDINICDynlRDLRNLFSIV--SQEPMLFNMSIYENIKFGrEDATLEDVKRVSKFAAIDEFIES 1296
Cdd:cd03290 57 K-----VHWSN--KNESEPSFEA---TRSRNRYSVAyaAQKPWLLNATVEENITFG-SPFNKQRYKAVTDACSLQPDIDL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1297 LPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRIASI 1375
Cdd:cd03290 126 LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYL 205
|
250
....*....|.
gi 124506379 1376 KRSDKIVVFNN 1386
Cdd:cd03290 206 PHADWIIAMKD 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
378-637 |
3.04e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 81.94 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYdtrKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDInlkwwRSKI 457
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSN-SIKNNIKY--SLYSLKDLEAMENyyeentndtyenknfslisnsmtSNELLE----MKKEYQTIKds 530
Cdd:cd03269 73 GYLPEERGLYPKmKVIDQLVYlaQLKGLKKEEARRR-----------------------IDEWLErlelSEYANKRVE-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 531 dvvdvskkvlihdfvsslpdkydtlvgsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKG 610
Cdd:cd03269 128 -------------------------------ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELAR 176
|
250 260
....*....|....*....|....*...
gi 124506379 611 NENRItIIIAHRLSTI-RYANTIFVLSN 637
Cdd:cd03269 177 AGKTV-ILSTHQMELVeELCDRVLLLNK 203
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
398-637 |
3.20e-17 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 85.16 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 398 DLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDS---HNLKDINLKWWRSKIGVVSQDPLLFSN-SIKN 473
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 474 NIkysLYSLKDLEAmenyyeentndtyenknfslisnsmtsnellemkkEYQTIKDSDVVDVSKkvlihdfvsslpdkYD 553
Cdd:TIGR02142 95 NL---RYGMKRARP-----------------------------------SERRISFERVIELLG--------------IG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 554 TLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITII-IAHRLSTI-RYANT 631
Cdd:TIGR02142 123 HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLH-AEFGIPILyVSHSLQEVlRLADR 201
|
....*.
gi 124506379 632 IFVLSN 637
Cdd:TIGR02142 202 VVVLED 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1230-1387 |
3.86e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 84.36 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDDINICDYN---LRDLR----------NLFSivsqepmlfNMSIYENIKFGredatLEdVKRVSKfAAIDEFIES 1296
Cdd:COG1135 60 GSVLVDGVDLTALSereLRAARrkigmifqhfNLLS---------SRTVAENVALP-----LE-IAGVPK-AEIRKRVAE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1297 LPNKydtnVGPYGKS------LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTI--IT- 1367
Cdd:COG1135 124 LLEL----VGLSDKAdaypsqLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIvlITh 199
|
170 180 190
....*....|....*....|....*....|....
gi 124506379 1368 -------IAHRIASIKRSdKIV-------VFNNP 1387
Cdd:COG1135 200 emdvvrrICDRVAVLENG-RIVeqgpvldVFANP 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1128-1415 |
3.92e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 83.73 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYISRPNVPIYK----NLSFTCDSKKTTAIVGETGSGKSTFMNlllrfydlkndHIilkndmtnfqdyqnnnnN 1203
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKkgldNISFELEEGSFVALVGHTGSGKSTLMQ-----------HF-----------------N 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1204 SLVLKNvnefsnqSGSAE--DYTVFNNNGeillddinicDYNLRDLRNLFSIVSQ--EPMLFNMSIYENIKFG------- 1272
Cdd:PRK13641 55 ALLKPS-------SGTITiaGYHITPETG----------NKNLKKLRKKVSLVFQfpEAQLFENTVLKDVEFGpknfgfs 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1273 REDATLEDVKRVSKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1352
Cdd:PRK13641 118 EDEAKEKALKWLKKVGLSEDLISKSPFE-----------LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 1353 TIVDIKdKADKTIITIAHRIASI-KRSDKIVVFNnpdrNGTFVQsHGTHDELLSAQDGIYKKYV 1415
Cdd:PRK13641 187 LFKDYQ-KAGHTVILVTHNMDDVaEYADDVLVLE----HGKLIK-HASPKEIFSDKEWLKKHYL 244
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
376-639 |
4.62e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.22 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 376 KKIEFKNVRFHYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGdIIVNDSHNLKDINLKWWRS 455
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-KVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 456 KIGVVSQDPllfsnsiknnikyslyslkDLEAMENYYEENTNDTYENKNFSlisnsmtsnellemkkEYQTIKDSDVVDV 535
Cdd:PRK13642 82 KIGMVFQNP-------------------DNQFVGATVEDDVAFGMENQGIP----------------REEMIKRVDEALL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 536 SKKVLihDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 615
Cdd:PRK13642 127 AVNML--DFKTREP-----------ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLT 193
|
250 260
....*....|....*....|....
gi 124506379 616 TIIIAHRLSTIRYANTIFVLSNRE 639
Cdd:PRK13642 194 VLSITHDLDEAASSDRILVMKAGE 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
397-627 |
6.44e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.91 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKST----ILKLIerlydPTEGDIIVNDS--HNLKDINLKWWRSKIGVVSQDPllfsNS 470
Cdd:PRK15134 303 KNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQplHNLNRRQLLPVRHRIQVVFQDP----NS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 471 iknnikyslySLKDLEAMENYYEENTNDTYEnknfslisnsmtsnELLEMKKEYQtikdsdVVDVSKKV-LIHDFVSSLP 549
Cdd:PRK15134 374 ----------SLNPRLNVLQIIEEGLRVHQP--------------TLSAAQREQQ------VIAVMEEVgLDPETRHRYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 550 dkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKseylVQKTI-NNLKG--NENRIT-IIIAHRLST 625
Cdd:PRK15134 424 -----------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT----VQAQIlALLKSlqQKHQLAyLFISHDLHV 488
|
..
gi 124506379 626 IR 627
Cdd:PRK15134 489 VR 490
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1147-1408 |
7.24e-17 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 84.01 E-value: 7.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1147 LSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILkndmtnfqdyqnnnnnslvlknvnefsnqsgsaedytvf 1226
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL--------------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1227 nnNGEILLDD-INICdynLRDLRNLFSIVSQEPMLF-NMSIYENIKFGREDATLEDVK----RVSKFAAIDEFIESLPNK 1300
Cdd:TIGR02142 57 --NGRTLFDSrKGIF---LPPEKRRIGYVFQEARLFpHLSVRGNLRYGMKRARPSERRisfeRVIELLGIGHLLGRLPGR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1301 ydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SD 1379
Cdd:TIGR02142 132 -----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlAD 200
|
250 260
....*....|....*....|....*....
gi 124506379 1380 KIVVFnnpdRNGTfVQSHGTHDELLSAQD 1408
Cdd:TIGR02142 201 RVVVL----EDGR-VAAAGPIAEVWASPD 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1312-1394 |
8.95e-17 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 79.01 E-value: 8.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1312 LSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIeKTIVDIKDKaDKTIITIAHRIASIKR-SDKIVVFnnpdR 1389
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAeVERLF-KVIRRLRAQ-GVAVIFISHRLDEVFEiADRVTVL----R 156
|
....*
gi 124506379 1390 NGTFV 1394
Cdd:cd03216 157 DGRVV 161
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
378-632 |
9.06e-17 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 80.60 E-value: 9.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLKWwRSKI 457
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG-EPIRDAREDY-RRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSnsiknnikyslyslkDLEAMENyyeentndtyenknfslisnsmtsnelLEMkkeYQTIKDSDVVDVSK 537
Cdd:COG4133 78 AYLGHADGLKP---------------ELTVREN---------------------------LRF---WAALYGLRADREAI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 KVLIHDFvsSLPDKYDTLVGsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNeNRITI 617
Cdd:COG4133 113 DEALEAV--GLAGLADLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVL 185
|
250
....*....|....*
gi 124506379 618 IIAHRLSTIRYANTI 632
Cdd:COG4133 186 LTTHQPLELAAARVL 200
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1124-1375 |
1.11e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 86.50 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1124 GKVDIKDVNFRYISRPNVpIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiilkndmtnfqdyqnnnnn 1203
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR--------------------------- 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1204 slvlknvnefsnqsgsaedytVFNNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKfGREDATLEDVKR 1283
Cdd:TIGR01271 1268 ---------------------LLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWK 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1284 VSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADK 1363
Cdd:TIGR01271 1326 VAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLK--QSFSNC 1403
|
250
....*....|..
gi 124506379 1364 TIITIAHRIASI 1375
Cdd:TIGR01271 1404 TVILSEHRVEAL 1415
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1145-1413 |
1.20e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 81.42 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILKNDMTNFQDYQNNNNN-SLVLKNVNefsnqsgsaedy 1223
Cdd:COG4167 30 KPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHiRMIFQDPN------------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1224 TVFN---NNGEILlddinicdynlrdlrnlfsivsQEPMLFN--MSIYEnikfgREDATLEDVKRVSKfaaidefiesLP 1298
Cdd:COG4167 98 TSLNprlNIGQIL----------------------EEPLRLNtdLTAEE-----REERIFATLRLVGL----------LP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1299 NKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR- 1377
Cdd:COG4167 141 EHANF----YPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHi 216
|
250 260 270
....*....|....*....|....*....|....*.
gi 124506379 1378 SDKIVVFnnpdRNGTFVQSHGTHDELLSAQDGIYKK 1413
Cdd:COG4167 217 SDKVLVM----HQGEVVEYGKTAEVFANPQHEVTKR 248
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1126-1375 |
1.51e-16 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 80.90 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPnvpIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydlkndhiilkndmtNFQDYQNnnnnsl 1205
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGD---------------LPPTYGN------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaeDYTVFnnnGEILlddiniCDYNLRDLRNLFSIVS---QEPMLFNMSIYENI---KFG----RED 1275
Cdd:COG1119 60 ----------------DVRLF---GERR------GGEDVWELRKRIGLVSpalQLRFPRDETVLDVVlsgFFDsiglYRE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1276 ATLEDVKRVskFAAIDEF-IESLPNKydtnvgPYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIEkT 1353
Cdd:COG1119 115 PTDEQRERA--RELLELLgLAHLADR------PFG-TLSQGEQRRVLIARALVKDPELLILDEPTAGLDlGARELLLA-L 184
|
250 260
....*....|....*....|..
gi 124506379 1354 IVDIKDKADKTIITIAHRIASI 1375
Cdd:COG1119 185 LDKLAAEGAPTLVLVTHHVEEI 206
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
397-639 |
2.19e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.16 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDINLKW-WRSKIGVVSQDPLLFSNsikn 473
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvDIAKISDAELREvRRKKIAMVFQSFALMPH---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 474 nikyslyslkdleamenyyeentndtyenknFSLISNSMTSNELLEMKKEYQTIKdsdVVDVSKKVLIHDFVSSLPDKyd 553
Cdd:PRK10070 121 -------------------------------MTVLDNTAFGMELAGINAEERREK---ALDALRQVGLENYAHSYPDE-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 554 tlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL-STIRYANTI 632
Cdd:PRK10070 165 ---------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRI 235
|
....*..
gi 124506379 633 FVLSNRE 639
Cdd:PRK10070 236 AIMQNGE 242
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1128-1370 |
2.54e-16 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 80.10 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYISrpNVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRfydlkndHIilkndmtnfqdyqnnnnNSLVl 1207
Cdd:COG3638 5 LRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKST----LLR-------CL-----------------NGLV- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqSGSAedytvfnnnGEILLDDINICDYNLRDLRNLFS---IVSQEPMLF-NMSIYENIKFGRedatL----- 1278
Cdd:COG3638 54 ---------EPTS---------GEILVDGQDVTALRGRALRRLRRrigMIFQQFNLVpRLSVLTNVLAGR----Lgrtst 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1279 ----------EDVKRVskFAAIDEFieSLPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSE 1347
Cdd:COG3638 112 wrsllglfppEDRERA--LEALERV--GLADKAYQRAD----QLSGGQQQRVAIARALVQEPKLILADEPVASLDpKTAR 183
|
250 260
....*....|....*....|...
gi 124506379 1348 KLIEkTIVDIKDKADKTIITIAH 1370
Cdd:COG3638 184 QVMD-LLRRIAREDGITVVVNLH 205
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
378-635 |
2.61e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.94 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVE--IYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND------SHNlKDIn 449
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstSKN-KDI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 450 lKWWRSKIGVVSQDP--LLFSNSIknnikyslysLKDLeamenyyeentndTYENKNFSLisnSMTSNELLEMKKeyqti 527
Cdd:PRK13649 81 -KQIRKKVGLVFQFPesQLFEETV----------LKDV-------------AFGPQNFGV---SQEEAEALAREK----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 528 kdSDVVDVSkkvlihdfvsslpdkyDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINN 607
Cdd:PRK13649 129 --LALVGIS----------------ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKK 190
|
250 260 270
....*....|....*....|....*....|
gi 124506379 608 LkgNENRITIIIAHRL--STIRYANTIFVL 635
Cdd:PRK13649 191 L--HQSGMTIVLVTHLmdDVANYADFVYVL 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1145-1386 |
2.74e-16 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 79.79 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYdlkndhiilkndmtnfqdyqnnnnnslvlknvnefsnqSGSAedyt 1224
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFL--------------------------------------RPTS---- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1225 vfnnnGEILLDDINICDYNLRDLRNL-----FSIVSqepmLF-NMSIYENIKFG---REDATLEDVKRVSKFAAIDEFIE 1295
Cdd:cd03219 55 -----GSVLFDGEDITGLPPHEIARLgigrtFQIPR----LFpELTVLENVMVAaqaRTGSGLLLARARREEREARERAE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1296 S------LPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIEkTIVDIKDKaDKTIITI 1368
Cdd:cd03219 126 EllervgLADLADRPAG----ELSYGQQRRLEIARALATDPKLLLLDEPAAGLnPEETEELAE-LIRELRER-GITVLLV 199
|
250
....*....|....*....
gi 124506379 1369 AHRIASIKR-SDKIVVFNN 1386
Cdd:cd03219 200 EHDMDVVMSlADRVTVLDQ 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1127-1405 |
2.91e-16 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 79.40 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1127 DIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNdhiilkndmtnfqdyqnnnnnslv 1206
Cdd:cd03224 2 EVENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRS------------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1207 lknvnefsnqsgsaedytvfnnnGEILLDDinicdynlRDLRNL--FSI-------VSQEPMLF-NMSIYENIKFG---- 1272
Cdd:cd03224 55 -----------------------GSIRFDG--------RDITGLppHERaragigyVPEGRRIFpELTVEENLLLGayar 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1273 ---REDATLEDVkrVSKFAAIDEFIESLpnkydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLdsnSEKL 1349
Cdd:cd03224 104 rraKRKARLERV--YELFPRLKERRKQL-----------AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL---APKI 167
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 1350 IE---KTIVDIKDKaDKTIITI---AHRIASIkrSDKIVVFnnpdRNGTFVQShGTHDELLS 1405
Cdd:cd03224 168 VEeifEAIRELRDE-GVTILLVeqnARFALEI--ADRAYVL----ERGRVVLE-GTAAELLA 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
398-597 |
3.24e-16 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 82.07 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 398 DLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN-----DSHnlKDINLKWWRSKIGVVSQDPLLFSN-SI 471
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqDSA--RGIFLPPHRRRIGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 472 KNNIkysLYSLKDLEAMENYYEENtndtyenknfSLIsnsmtsnELLEMkkeyqtikdsdvvdvskkvlihdfvsslpdk 551
Cdd:COG4148 95 RGNL---LYGRKRAPRAERRISFD----------EVV-------ELLGI------------------------------- 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 124506379 552 yDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKS 597
Cdd:COG4148 124 -GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1123-1415 |
4.32e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 79.71 E-value: 4.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1123 KGKVDIKDVNFRYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILkndmtnfqdyqnnnn 1202
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV--------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1203 nslvlknvnefsnqsgsaedytvfnnNGEILLDDINICDYNLRDLRNLFSIVSQEPMLF-NMSIYENIKFGREDATLEDV 1281
Cdd:PRK14246 70 --------------------------DGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpHLSIYDNIAYPLKSHGIKEK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1282 KRVSKFaaIDEFIESL---PNKYDTNVGPyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1358
Cdd:PRK14246 124 REIKKI--VEECLRKVglwKEVYDRLNSP-ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1359 DKAdkTIITIAHRIASIKRSDKIVVFNnpdRNGTFVQSHGTHDELLSAQDGIYKKYV 1415
Cdd:PRK14246 201 NEI--AIVIVSHNPQQVARVADYVAFL---YNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
378-637 |
4.76e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 77.98 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRF---HYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLI--ERLYDPTEGDIIVNDshnlKDINLKW 452
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING----RPLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 453 WRSKIGVVSQDPLLFSN-SIKNNIKYSlyslkdleamenyyeentndtyenknfslisnsmtsnellemkkeyqtikdsd 531
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMFA----------------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 532 vvdvskkvlihdfvsslpdkydtlvgSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkGN 611
Cdd:cd03213 107 --------------------------AKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-AD 159
|
250 260
....*....|....*....|....*...
gi 124506379 612 ENRITIIIAHRLSTIRYA--NTIFVLSN 637
Cdd:cd03213 160 TGRTIICSIHQPSSEIFElfDKLLLLSQ 187
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1142-1383 |
5.14e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 77.98 E-value: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1142 PIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnslvlknvnefsnqSGSAE 1221
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL------------------------------------------AGRRT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1222 DYTVfnnNGEILLDDINIcdyNLRDLRNLFSIVSQEPMLF-NMSIYENIKFGredatledvkrvskfAAIdefieslpnk 1300
Cdd:cd03213 61 GLGV---SGEVLINGRPL---DKRSFRKIIGYVPQDDILHpTLTVRETLMFA---------------AKL---------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1301 ydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIAS--IKRS 1378
Cdd:cd03213 110 ---------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTG-RTIICSIHQPSSeiFELF 179
|
....*
gi 124506379 1379 DKIVV 1383
Cdd:cd03213 180 DKLLL 184
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
362-623 |
5.30e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 84.19 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 362 LVENNDDGETLPNIKKIEFKNVRFHYdTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDpTEGDIIVnD 441
Cdd:TIGR01271 1202 VIENPHAQKCWPSGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQI-D 1278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 442 SHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdleamenyyeentnDTYENKNfslisnsmtsnellemk 521
Cdd:TIGR01271 1279 GVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL----------------------DPYEQWS----------------- 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 522 keyqtikDSDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLV 601
Cdd:TIGR01271 1320 -------DEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQII 1392
|
250 260
....*....|....*....|...
gi 124506379 602 QKTinnLKGNENRITIIIA-HRL 623
Cdd:TIGR01271 1393 RKT---LKQSFSNCTVILSeHRV 1412
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1126-1370 |
5.95e-16 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 78.22 E-value: 5.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:cd03292 1 IEFINVTKTY--PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYK----------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsAEDYTvfnnNGEILLDDINICDYNLRD---LRNLFSIVSQE-PMLFNMSIYENIKFGRE--DATLE 1279
Cdd:cd03292 50 --------------EELPT----SGTIRVNGQDVSDLRGRAipyLRRKIGVVFQDfRLLPDRNVYENVAFALEvtGVPPR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1280 DV-KRVSkfAAIDEFieSLPNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1358
Cdd:cd03292 112 EIrKRVP--AALELV--GLSHKHRA----LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKI- 182
|
250
....*....|..
gi 124506379 1359 DKADKTIITIAH 1370
Cdd:cd03292 183 NKAGTTVVVATH 194
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
378-635 |
7.83e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.49 E-value: 7.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVEI--YKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSH---NLKDINLKW 452
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 453 WRSKIGVVSQDP--LLFSNSIknnikyslysLKDLEamenyyeentndtYENKNFSLISNSMTSNELLEMKKeyqtikds 530
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTV----------LKDVE-------------FGPKNFGFSEDEAKEKALKWLKK-------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 531 dvVDVSkkvlihdfvsslpdkyDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKg 610
Cdd:PRK13641 132 --VGLS----------------EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQ- 192
|
250 260
....*....|....*....|....*.
gi 124506379 611 NENRITIIIAHRLSTI-RYANTIFVL 635
Cdd:PRK13641 193 KAGHTVILVTHNMDDVaEYADDVLVL 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1274-1371 |
8.47e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1274 EDATLEDVKRVSKFAAIDEFIESLpnkyDTnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1353
Cdd:COG4178 453 EAFSDAELREALEAVGLGHLAERL----DE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL 527
|
90
....*....|....*...
gi 124506379 1354 IVDIKDKAdkTIITIAHR 1371
Cdd:COG4178 528 LREELPGT--TVISVGHR 543
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
378-634 |
8.58e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.60 E-value: 8.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND-SHNLKDINLKWWRSK 456
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSNsiknnikyslyslkdLEAMENYYeentndtyenknFSLISNSMTSNEllemkkeyqtikdsDVVDVS 536
Cdd:PRK09493 79 AGMVFQQFYLFPH---------------LTALENVM------------FGPLRVRGASKE--------------EAEKQA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 537 KKVLIHDFVSSLPDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRIT 616
Cdd:PRK09493 118 RELLAKVGLAERAHHY-------PSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTM 189
|
250 260
....*....|....*....|
gi 124506379 617 IIIAHRLSTIRYANT--IFV 634
Cdd:PRK09493 190 VIVTHEIGFAEKVASrlIFI 209
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
324-640 |
1.03e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.16 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 324 LGVLISMFmltiilPNITEYMKALEATNSLYEIINRKPLVENNDDGETLPNIKKIEFKNVRFHydTRKDVEIYKDLSFTL 403
Cdd:COG4178 315 LSWFVDNY------QSLAEWRATVDRLAGFEEALEAADALPEAASRIETSEDGALALEDLTLR--TPDGRPLLEDLSLSL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 404 KEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlkdinlkwwRSKIGVVSQDPLLFSNSIKNNIKYSlyslk 483
Cdd:COG4178 387 KPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA------------GARVLFLPQRPYLPLGTLREALLYP----- 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 484 dleamenyyeeNTNDTYEnknfslisnsmtsnellemkkeyqtikDSDVVDVSKKVLIHDFVSSLPDKYDTlvgsnASKL 563
Cdd:COG4178 450 -----------ATAEAFS---------------------------DAELREALEAVGLGHLAERLDEEADW-----DQVL 486
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 564 SGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINN-LKGnenrITII-IAHRLSTIRYANTIFVLSNRER 640
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPG----TTVIsVGHRSTLAAFHDRVLELTGDGS 561
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1307-1371 |
1.14e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.04 E-value: 1.14e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 1307 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikdkADKTIITIAHR 1371
Cdd:cd03223 87 PWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE----LGITVISVGHR 147
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
378-639 |
1.34e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.58 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDIN--LKWWRS 455
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI-KGEPIKYDKksLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 456 KIGVVSQDP--LLFSNSIKNNIKYSLYSLKdleamenyyeentndtyenknfslisnsmtsnelLEMKKEYQTIKDSdvv 533
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFGPLNLG----------------------------------LSKEEVEKRVKEA--- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 dvSKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkgNEN 613
Cdd:PRK13639 122 --LKAVGMEGFENKPP-----------HHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL--NKE 186
|
250 260
....*....|....*....|....*...
gi 124506379 614 RITIIIA-HRLSTI-RYANTIFVLSNRE 639
Cdd:PRK13639 187 GITIIIStHDVDLVpVYADKVYVMSDGK 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1136-1356 |
1.68e-15 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 76.75 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1136 ISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRfydlkndhiILkndmtnfqdyqnnnnnslvlknvnefsn 1215
Cdd:COG4133 10 CRRGERLLFSGLSFTLAAGEALALTGPNGSGKTT----LLR---------IL---------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1216 qSGSAEDYTvfnnnGEILLDDINIcDYNLRDLRNLFSIVSQEPMLF-NMSIYENIKF----GREDATLEDVKrvskfAAI 1290
Cdd:COG4133 49 -AGLLPPSA-----GEVLWNGEPI-RDAREDYRRRLAYLGHADGLKpELTVRENLRFwaalYGLRADREAID-----EAL 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1291 DEF----IESLPnkydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1356
Cdd:COG4133 117 EAVglagLADLP----------VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1308-1383 |
1.85e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 79.46 E-value: 1.85e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1308 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1383
Cdd:PRK11153 137 YPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAV 213
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
377-626 |
1.95e-15 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 78.36 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 377 KIEFKNVRFHYdTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDpTEGDIIVnDSHNLKDINLKWWRSK 456
Cdd:cd03289 2 QMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQI-DGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSNSIKNNIkyslyslkdleamenyyeentnDTYENKNfslisnsmtsnellemkkeyqtikDSDVVDVS 536
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNL----------------------DPYGKWS------------------------DEEIWKVA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 537 KKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTinnLKGNENRIT 616
Cdd:cd03289 113 EEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKT---LKQAFADCT 189
|
250
....*....|.
gi 124506379 617 IIIA-HRLSTI 626
Cdd:cd03289 190 VILSeHRIEAM 200
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
397-594 |
2.17e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.80 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDS--HNLKDINLKWWRSKIGVVSQDPLLFSN---SI 471
Cdd:PRK10419 29 NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplAKLNRAQRKAFRRDIQMVFQDSISAVNprkTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 472 KNNIKYSLYSLKDLEAMENyyeentndtyenknfslisnSMTSNELLEMkkeyqtikdsdvVDVSKKVLihdfvSSLPdk 551
Cdd:PRK10419 109 REIIREPLRHLLSLDKAER--------------------LARASEMLRA------------VDLDDSVL-----DKRP-- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124506379 552 ydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK10419 150 ---------PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
380-594 |
2.24e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.69 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 380 FKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHnLKDINLKwwRSKIGV 459
Cdd:PRK11000 6 LRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR-MNDVPPA--ERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 460 VSQdpllfsnsiknniKYSLYSLKDLeamenyyeentndtYENKNFSLisnsmtsnELLEMKKEyqtikdsdvvDVSKKV 539
Cdd:PRK11000 80 VFQ-------------SYALYPHLSV--------------AENMSFGL--------KLAGAKKE----------EINQRV 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 540 lihDFVSSLPdKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK11000 115 ---NQVAEVL-QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1229-1386 |
2.35e-15 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 77.38 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1229 NGEILLDDINICDYNLRDlRNLfSIVSQEPMLF-NMSIYENIKFG----------REDATLEDVKRVSKFAAIDEFIESL 1297
Cdd:cd03296 56 SGTILFGGEDATDVPVQE-RNV-GFVFQHYALFrHMTVFDNVAFGlrvkprserpPEAEIRAKVHELLKLVQLDWLADRY 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1298 PNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIK 1376
Cdd:cd03296 134 PAQ-----------LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEeALE 202
|
170
....*....|
gi 124506379 1377 RSDKIVVFNN 1386
Cdd:cd03296 203 VADRVVVMNK 212
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
397-609 |
2.95e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 76.70 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKD---------INLKwwRSKIGVVSQdpllF 467
Cdd:COG4778 28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDlaqaspreiLALR--RRTIGYVSQ----F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 468 snsiknnikysLYSLKDLEAMENYYEentndtyenknfSLISNSMTSNELLEMKKEyqtikdsdvvdvskkvLIHDFvsS 547
Cdd:COG4778 102 -----------LRVIPRVSALDVVAE------------PLLERGVDREEARARARE----------------LLARL--N 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 548 LPDKydtLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLK 609
Cdd:COG4778 141 LPER---LWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAK 199
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1228-1386 |
3.04e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.22 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1228 NNGEILLDDINICDY--NLRDLRNLFsivsQEPMLF-NMSIYENIKFG---REDATLEDVKRVS---KFAAIDEFIESLP 1298
Cdd:PRK09452 67 DSGRIMLDGQDITHVpaENRHVNTVF----QSYALFpHMTVFENVAFGlrmQKTPAAEITPRVMealRMVQLEEFAQRKP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1299 nkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKR 1377
Cdd:PRK09452 143 -----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHdQEEALTM 211
|
....*....
gi 124506379 1378 SDKIVVFNN 1386
Cdd:PRK09452 212 SDRIVVMRD 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1133-1415 |
3.35e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.52 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1133 FRY----ISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnslvlk 1208
Cdd:PRK15112 14 FRYrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKML---------------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1209 nvnefsnqSGSAEDytvfnNNGEILLDDINIC--DYNLRDLRnlFSIVSQEPmlfNMSIYENIKFG-------REDATLE 1279
Cdd:PRK15112 60 --------AGMIEP-----TSGELLIDDHPLHfgDYSYRSQR--IRMIFQDP---STSLNPRQRISqildfplRLNTDLE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1280 DVKRVSKFAAIDEFIESLPNkydtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1359
Cdd:PRK15112 122 PEQREKQIIETLRQVGLLPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQE 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1360 KADKTIITIAHRIASIKR-SDKIVVFNnpdrNGTFVQSHGTHDELLSAQDGIYKKYV 1415
Cdd:PRK15112 198 KQGISYIYVTQHLGMMKHiSDQVLVMH----QGEVVERGSTADVLASPLHELTKRLI 250
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
378-678 |
3.37e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.98 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRkdvEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-IVNDSHNL------KDINL 450
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLnIAGNHFDFsktpsdKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 451 kwWRSKIGVVSQdpllfsnsiknniKYSLYSlkDLEAMENyyeentndtyenknfsLISNSMtsnELLEMKKEyQTIKDS 530
Cdd:PRK11124 80 --LRRNVGMVFQ-------------QYNLWP--HLTVQQN----------------LIEAPC---RVLGLSKD-QALARA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 531 DvvDVSKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKg 610
Cdd:PRK11124 123 E--KLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELA- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 611 nENRIT-IIIAHRLSTIRYANTIFVlsnrersdnnnnnnnddnnnnnnnnnnkiNNEGSYIIEQGTHDS 678
Cdd:PRK11124 189 -ETGITqVIVTHEVEVARKTASRVV-----------------------------YMENGHIVEQGDASC 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1158-1401 |
5.01e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1158 AIVGETGSGKSTFMNLLLRFYdlKNDHiilkndmtnfqdyqnnnnnslvlknvnefsnqsgsaedytvfnnnGEILLD-- 1235
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLY--QPDS---------------------------------------------GEILIDgk 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1236 --DINicdyNLRDLRNLfSI--VSQEPMLF-NMSIYENIKFGREDATLEDVKRvskfAAIDEFIESLPNKYDTNVGPYGK 1310
Cdd:COG3845 68 pvRIR----SPRDAIAL-GIgmVHQHFMLVpNLTVAENIVLGLEPTKGGRLDR----KAARARIRELSERYGLDVDPDAK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1311 --SLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIEkTIVDIKDkADKTIITIAHRIASIKR-SDKIVVFnn 1386
Cdd:COG3845 139 veDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE-ILRRLAA-EGKSIIFITHKLREVMAiADRVTVL-- 214
|
250
....*....|....*
gi 124506379 1387 pdRNGTFVqshGTHD 1401
Cdd:COG3845 215 --RRGKVV---GTVD 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1230-1385 |
5.18e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.95 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDDINICDYN-LRDLRNLFSIVSQEP--MLFNMSIYENIKFGREDATL---EDVKRVSKFAAidefieslpnkyDT 1303
Cdd:PRK13644 57 GKVLVSGIDTGDFSkLQGIRKLVGIVFQNPetQFVGRTVEEDLAFGPENLCLppiEIRKRVDRALA------------EI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1304 NVGPY----GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRSD 1379
Cdd:PRK13644 125 GLEKYrhrsPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKG-KTIVYITHNLEELHDAD 203
|
....*.
gi 124506379 1380 KIVVFN 1385
Cdd:PRK13644 204 RIIVMD 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
378-635 |
6.08e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 76.98 E-value: 6.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVE---IYkDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND---SHNLKDINLK 451
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFErraLY-DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErviTAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 WWRSKIGVVSQDP--LLFSNSIknnikyslysLKDLeamenyyeentndTYENKNFslisnSMTSNELLEMKKEyqTIKd 529
Cdd:PRK13634 82 PLRKKVGIVFQFPehQLFEETV----------EKDI-------------CFGPMNF-----GVSEEDAKQKARE--MIE- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 530 sdVVDVSKKVLIHD-FvsslpdkydtlvgsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNL 608
Cdd:PRK13634 131 --LVGLPEELLARSpF-----------------ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKL 191
|
250 260
....*....|....*....|....*...
gi 124506379 609 KGNENRITIIIAHRLSTI-RYANTIFVL 635
Cdd:PRK13634 192 HKEKGLTTVLVTHSMEDAaRYADQIVVM 219
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
57-338 |
6.74e-15 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 77.09 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 57 LFISFVCAVLSGG---TLPFFISVF--GVILKNmnLGDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEY 131
Cdd:cd18542 1 YLLAILALLLATAlnlLIPLLIRRIidSVIGGG--LRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 132 LRSVFYQDGQFHDNNP-G---SKLRSDLD----FyleqVSSGIGTKFITIFTYASSFLGLYIWslikNARLTLCITCVFP 203
Cdd:cd18542 79 YDHLQRLSFSFHDKARtGdlmSRCTSDVDtirrF----LAFGLVELVRAVLLFIGALIIMFSI----NWKLTLISLAIIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 204 LIYVCGVICNKKV-----KLNKKTSLLynnntMSIIEEALMGIRTVASYCGEKTILNKFN-LSETFYSKYIlKANFVEAL 277
Cdd:cd18542 151 FIALFSYVFFKKVrpafeEIREQEGEL-----NTVLQENLTGVRVVKAFAREDYEIEKFDkENEEYRDLNI-KLAKLLAK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124506379 278 HIGLINGLILVSYAFGFWYGTRIIINSatnqypnndfngasviSILLGVLI--SMFMLTIILP 338
Cdd:cd18542 225 YWPLMDFLSGLQIVLVLWVGGYLVING----------------EITLGELVafISYLWMLIWP 271
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1126-1408 |
7.05e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.67 E-value: 7.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDlkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnEFSnqsgsaedytvfnnnGEILLDDINICDYNLRDLRNLFSIVSQEP--MLFNMSIYENIKFGREDatlEDVKR 1283
Cdd:PRK13642 59 ------EFE---------------GKVKIDGELLTAENVWNLRRKIGMVFQNPdnQFVGATVEDDVAFGMEN---QGIPR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1284 VSKFAAIDEFIESLpNKYDTNVGPYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADK 1363
Cdd:PRK13642 115 EEMIKRVDEALLAV-NMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQL 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 124506379 1364 TIITIAHRIASIKRSDKIVVFnnpdRNGTFVQSHGTHDELLSAQD 1408
Cdd:PRK13642 193 TVLSITHDLDEAASSDRILVM----KAGEIIKEAAPSELFATSED 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
378-596 |
7.84e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.95 E-value: 7.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVEiykDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDInlKWWRSKI 457
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHV--PPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSN-SIKNNIKYSLyslkdleamenyyeentndtyenKNFSLISNSMTS--NELLEMkkeyqtikdsdvvd 534
Cdd:PRK11607 94 NMMFQSYALFPHmTVEQNIAFGL-----------------------KQDKLPKAEIASrvNEMLGL-------------- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 535 vskkVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNK 596
Cdd:PRK11607 137 ----VHMQEFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
378-594 |
8.54e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.45 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNV--RFHYDTRKDveiykDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKwwRS 455
Cdd:PRK11432 7 VVLKNItkRFGSNTVID-----NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-DGEDVTHRSIQ--QR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 456 KIGVVSQDPLLFSN-SIKNNIKYSLyslkdleAMENYYEEntndtyenknfslisnsmtsnellEMKkeyQTIKDS-DVV 533
Cdd:PRK11432 79 DICMVFQSYALFPHmSLGENVGYGL-------KMLGVPKE------------------------ERK---QRVKEAlELV 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124506379 534 DvskkvlihdfVSSLPDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK11432 125 D----------LAGFEDRY-------VDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
392-639 |
8.65e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.85 E-value: 8.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 392 DVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDS-----HNLKDINLKWWRSKIGVVSQDPLL 466
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 467 FSN-SIKNNIKYSLYS--LKDleamenyyeentndtyenknfslisnsmtsnellemKKEYQTIKDSDVVDVSKKVLIHD 543
Cdd:PRK14246 102 FPHlSIYDNIAYPLKShgIKE------------------------------------KREIKKIVEECLRKVGLWKEVYD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 544 FVSSlpdkydtlvgsNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRL 623
Cdd:PRK14246 146 RLNS-----------PASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK-NEIAIVIVSHNPQ 213
|
250
....*....|....*.
gi 124506379 624 STIRYANTIFVLSNRE 639
Cdd:PRK14246 214 QVARVADYVAFLYNGE 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
378-637 |
8.95e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.31 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYdtRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHnLKDINLKWWRSKI 457
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE-VNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDP--LLFSNSIknnikyslyslkdleamenyyeentndtYENKNFSLISNSMTSNELLEMkkeyqtikdsdVVDV 535
Cdd:PRK13647 82 GLVFQDPddQVFSSTV----------------------------WDDVAFGPVNMGLDKDEVERR-----------VEEA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 536 SKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRI 615
Cdd:PRK13647 123 LKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRL--HNQGK 189
|
250 260
....*....|....*....|....
gi 124506379 616 TIIIA-HRLS-TIRYANTIFVLSN 637
Cdd:PRK13647 190 TVIVAtHDVDlAAEWADQVIVLKE 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1182-1383 |
9.41e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 76.28 E-value: 9.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1182 NDHIILKNDMTNFQDYQNNNNNSLVLKNVN------EF-----SNQSGSAEDYTVFN-----NNGEILLDDINICDY-NL 1244
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEKLALDDVNlevkkgEFlvilgRNGSGKSTIAKHMNallipSEGKVYVDGLDTSDEeNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1245 RDLRNLFSIVSQEP--MLFNMSIYENIKFGRED---ATLEDVKRVskfaaiDEFIESLpNKYDtnvgpYGKS----LSGG 1315
Cdd:PRK13633 81 WDIRNKAGMVFQNPdnQIVATIVEEDVAFGPENlgiPPEEIRERV------DESLKKV-GMYE-----YRRHaphlLSGG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 1316 QKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVV 1383
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIV 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
378-608 |
9.67e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.18 E-value: 9.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYdtrKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDINLKwwRSKI 457
Cdd:PRK13536 42 IDLAGVSKSY---GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA--RARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQ-DPLLFSNSIKNNI----KYSLYSLKDLEAMenyyeentndtyenknfslisnsMTSneLLEMKKeyqtikdsdv 532
Cdd:PRK13536 117 GVVPQfDNLDLEFTVRENLlvfgRYFGMSTREIEAV-----------------------IPS--LLEFAR---------- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 533 vdvskkvlihdfvssLPDKYDTLVgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNL 608
Cdd:PRK13536 162 ---------------LESKADARV----SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSL 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
378-619 |
9.89e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 74.71 E-value: 9.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDInlKWWRSKI 457
Cdd:cd03265 1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLfsnsiknnikyslyslkdleamenyyeentndtyenknfsliSNSMTSNELLEMKKEYQTIKDSDVVDVSK 537
Cdd:cd03265 76 GIVFQDLSV------------------------------------------DDELTGWENLYIHARLYGVPGAERRERID 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 KVLihDFVsSLPDKYDTLVgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITI 617
Cdd:cd03265 114 ELL--DFV-GLLEAADRLV----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLK-EEFGMTI 185
|
..
gi 124506379 618 II 619
Cdd:cd03265 186 LL 187
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1126-1374 |
1.05e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 75.43 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISrpnVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRFYDL----KNDHIILKNDMTNFQDYQNNN 1201
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSS----LLRVLNLletpDSGQLNIAGHQFDFSQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1202 NNSLVLKNVNefsnqsgsaedyTVFNNngeillddinicdYNLRdlrnlfsivsqePmlfNMSIYENI--------KFGR 1273
Cdd:COG4161 76 AIRLLRQKVG------------MVFQQ-------------YNLW------------P---HLTVMENLieapckvlGLSK 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1274 EDAtLEDVKRVSKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKT 1353
Cdd:COG4161 116 EQA-REKAMKLLARLRLTDKADRFPLH-----------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----ITAQ 179
|
250 260 270
....*....|....*....|....*....|
gi 124506379 1354 IVDIKDKADKTIIT---------IAHRIAS 1374
Cdd:COG4161 180 VVEIIRELSQTGITqvivtheveFARKVAS 209
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1146-1372 |
1.22e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.81 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1146 NLSFTCDSKKTTAIVGETGSGKSTFMnlllrfydlkndhiilkndmTNFQDYQNNNNNSLVLKNVneFSNQSGSAEDYTV 1225
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLV--------------------THFNGLIKSKYGTIQVGDI--YIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1226 FNNNGEIllddinicdYNLRDLRNLFSIVSQEP--MLFNMSIYENIKFG-------REDATLEDVKRVSKFAAIDEFIEs 1296
Cdd:PRK13631 102 NPYSKKI---------KNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYLE- 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 1297 lpnkydtnVGPYGksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRI 1372
Cdd:PRK13631 172 --------RSPFG--LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTM 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1148-1408 |
1.40e-14 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 77.06 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1148 SFTCDSKKTTAIVGETGSGKSTFMNL---LLRfydLKNDHIILkndmtnfqdyqnnnnnslvlknvnefsnqsgsaedyt 1224
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRL------------------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1225 vfnnNGEILLDD---INIcdynLRDLRNLfSIVSQEPMLF-NMSIYENIKFGREDATLEDvkRVSKFAAIDEF--IESLP 1298
Cdd:COG4148 59 ----GGEVLQDSargIFL----PPHRRRI-GYVFQEARLFpHLSVRGNLLYGRKRAPRAE--RRISFDEVVELlgIGHLL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1299 NKYDTNvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLD--SNSEKL--IEKtivdIKDKADKTIITIAHRIAS 1374
Cdd:COG4148 128 DRRPAT-------LSGGERQRVAIGRALLSSPRLLLMDEPLAALDlaRKAEILpyLER----LRDELDIPILYVSHSLDE 196
|
250 260 270
....*....|....*....|....*....|....*
gi 124506379 1375 IKR-SDKIVVFnnpdRNGTfVQSHGTHDELLSAQD 1408
Cdd:COG4148 197 VARlADHVVLL----EQGR-VVASGPLAEVLSRPD 226
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
792-1072 |
1.99e-14 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 75.54 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 792 IFFSILVAGglypvFALLYARYVSTLFDFANLEYNSNKYSIYILLIAIAMF---ISETLKNYYNNKIGEKVEKTMKRRLF 868
Cdd:cd18552 5 ILGMILVAA-----TTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLlrgLASYLQTYLMAYVGQRVVRDLRNDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 869 ENILYQEMSFFdqDKNTPGVLSAHINRDVHLLKTGLVNNIV--------IFSHFIMLFLVSMVMSFYFCpIVAAVLTFIy 940
Cdd:cd18552 80 DKLLRLPLSFF--DRNSSGDLISRITNDVNQVQNALTSALTvlvrdpltVIGLLGVLFYLDWKLTLIAL-VVLPLAALP- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 941 finMRVFAVRARLTKSKEIEKKENMSSgvfafssddemfkdpsfLIQEAFYNMHTVINYGLEDYFCNLIEKAIDYKNKGQ 1020
Cdd:cd18552 156 ---IRRIGKRLRKISRRSQESMGDLTS-----------------VLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLS 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 1021 KRRIIVNAALWGFSQsaqlFINSFA----YWFGSFLIKRGTILVDDFMkSLFTFIF 1072
Cdd:cd18552 216 MKIARARALSSPLME----LLGAIAialvLWYGGYQVISGELTPGEFI-SFITALL 266
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1158-1384 |
1.99e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.88 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1158 AIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnnslvlknvnefsNQSGSAEdytvfnnnGEILLDDI 1237
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFNRLLEL----------------------------------NEEARVE--------GEVRLFGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1238 NI--CDYNLRDLRNLFSIVSQEPMLF-NMSIYENIKFGREDATL--------EDVKRVSKFAAIDEFIESLPNKYDTNvg 1306
Cdd:PRK14267 72 NIysPDVDPIEVRREVGMVFQYPNPFpHLTIYDNVAIGVKLNGLvkskkeldERVEWALKKAALWDEVKDRLNDYPSN-- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 1307 pygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVF 1384
Cdd:PRK14267 150 -----LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAF 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
394-634 |
2.44e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.62 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 394 EIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDINLKwwRSKIGvvsqdpllfsnSIKN 473
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG----QTINLV--RDKDG-----------QLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 474 NIKYSLYSLKdleamenyyeenTNDTYENKNFSLISNsMTSNELLeMKKEYQTIKDSDVVDVSKKVLIHDFV---SSLPD 550
Cdd:PRK10619 82 ADKNQLRLLR------------TRLTMVFQHFNLWSH-MTVLENV-MEAPIQVLGLSKQEARERAVKYLAKVgidERAQG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 551 KYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIRYAN 630
Cdd:PRK10619 148 KY-------PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVS 219
|
....*.
gi 124506379 631 T--IFV 634
Cdd:PRK10619 220 ShvIFL 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
378-593 |
2.99e-14 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 73.62 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDI-NLKWW--- 453
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG----RDItGLPPHera 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 454 RSKIGVVSQDPLLFSN-SIKNNIKYSLYSLKDleamenyyeENTNDTYEnknfslisnsmtsnELLEMkkeyqtikdsdv 532
Cdd:cd03224 74 RAGIGYVPEGRRIFPElTVEENLLLGAYARRR---------AKRKARLE--------------RVYEL------------ 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124506379 533 vdvskkvlihdFvSSLPDKYDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSL 593
Cdd:cd03224 119 -----------F-PRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
397-635 |
3.02e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.37 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDS----HNLKD-INLKwwrskIGVVSQDPLLFSNsi 471
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvriRSPRDaIALG-----IGMVHQHFMLVPN-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 472 knnikyslyslkdLEAMENYyeentndtyenknfsLISNSMTSNELLEMKKEYQTIKDsdvvdvskkvlihdfvssLPDK 551
Cdd:COG3845 95 -------------LTVAENI---------------VLGLEPTKGGRLDRKAARARIRE------------------LSER 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 552 Y------DTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSL-DNKSEYLVqKTINNLKgnENRITII-IAHRL 623
Cdd:COG3845 129 YgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELF-EILRRLA--AEGKSIIfITHKL 201
|
250
....*....|...
gi 124506379 624 STIR-YANTIFVL 635
Cdd:COG3845 202 REVMaIADRVTVL 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
378-635 |
3.29e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.35 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVR--FHYDTRKDVEIYKDLSFTLKEGKtyaFV---GESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDI-NLK 451
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGD---FVtviGSNGAGKSTLLNAIAGSLPPDSGSILIDG----KDVtKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 -WWRSK-IGVVSQDPLL---FSNSIKNNIkySLYSLKdleamenyyeentndtyeNKNFSLiSNSMTSnellEMKKEYQt 526
Cdd:COG1101 75 eYKRAKyIGRVFQDPMMgtaPSMTIEENL--ALAYRR------------------GKRRGL-RRGLTK----KRRELFR- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 527 ikdsdvvdvskkvlihDFVSS----LPDKYDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQ 602
Cdd:COG1101 129 ----------------ELLATlglgLENRLDTKVGL----LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVL 188
|
250 260 270
....*....|....*....|....*....|....
gi 124506379 603 KTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 635
Cdd:COG1101 189 ELTEKIVEENNLTTLMVTHNMEqALDYGNRLIMM 222
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
794-1079 |
3.58e-14 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 75.01 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 794 FSILVAGGLYPVFALLYARYVSTLFD-------------------FANLEYNSNKYSIYILLIAIAMFISETLKNYYNNK 854
Cdd:cd18558 6 LCAIIHGGLLPAFMVIFGDMTDSFTNggmtnitgnssglnssagpFEKLEEEMTLYAYYYLIIGAIVLITAYIQGSFWGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 855 IGEKVEKTMKRRLFENILYQEMSFFdqDKNTPGVLSAHINRDVHLLKTGLVNNIVIFSHFIMLFLVSMVMSFYFCPIVAA 934
Cdd:cd18558 86 AAGRQTKKIRYKFFHAIMRQEIGWF--DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 935 VLTFIYFINMRVFAVRAR-LTKSKEIEKKENMSSGVFAfssddemfkdpsfliQEAFYNMHTVINYGLEDYFCNLIEKAI 1013
Cdd:cd18558 164 VILAISPVLGLSAVVWAKiLSGFTDKEKKAYAKAGAVA---------------EEVLEAFRTVIAFGGQQKEETRYAQNL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1014 -DYKNKGQKRRIIVNAALwGFSQSAQLFINSFAYWFGSFLIKRGTILVDDFMKSLFTFIFTGSYAGK 1079
Cdd:cd18558 229 eIAKRNGIKKAITFNISM-GAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQ 294
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1230-1405 |
4.39e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDDINIC---DYNLRDLR-NLFSIVSQE-PMLFNMSIYENIKFGREDATLEDVKRVSKfaAIDEFIESLPNKYDTN 1304
Cdd:PRK10070 83 GQVLIDGVDIAkisDAELREVRrKKIAMVFQSfALMPHMTVLDNTAFGMELAGINAEERREK--ALDALRQVGLENYAHS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1305 vgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1383
Cdd:PRK10070 161 ---YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAI 237
|
170 180
....*....|....*....|..
gi 124506379 1384 FnnpdRNGTFVQShGTHDELLS 1405
Cdd:PRK10070 238 M----QNGEVVQV-GTPDEILN 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1131-1373 |
4.56e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.59 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1131 VNFRYISRP--NVPIYKNLSFTCDSKKTTAIVGETGSGKSTFmnlllrfydlkndhiilkndmtnfqdyqnnnnnslvLK 1208
Cdd:PRK09493 2 IEFKNVSKHfgPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTL------------------------------------LR 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1209 NVNEFSNQSGsaedytvfnnnGEILLDDINICD--YNLRDLRNLFSIVSQEPMLF-NMSIYENIKFGREDatledVKRVS 1285
Cdd:PRK09493 46 CINKLEEITS-----------GDLIVDGLKVNDpkVDERLIRQEAGMVFQQFYLFpHLTALENVMFGPLR-----VRGAS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1286 KFAAIDEFIESLpnkydTNVG------PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKD 1359
Cdd:PRK09493 110 KEEAEKQARELL-----AKVGlaerahHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP---ELRHEVLKVMQD 181
|
250
....*....|....*.
gi 124506379 1360 KADK--TIITIAHRIA 1373
Cdd:PRK09493 182 LAEEgmTMVIVTHEIG 197
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1145-1406 |
6.93e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 76.26 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiilkndmtnfqdyqnnnnnsLVlknvnefsnQSGsaedyt 1224
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLR----------------------------LI---------PSE------ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1225 vfnnnGEILLDDINICDYNLRDLRNL---FSIVSQEPM-LFN--MSIYENIKFG------------RED---ATLEDVkr 1283
Cdd:COG4172 340 -----GEIRFDGQDLDGLSRRALRPLrrrMQVVFQDPFgSLSprMTVGQIIAEGlrvhgpglsaaeRRArvaEALEEV-- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1284 vskfaAIDEfiESLpNKYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDsnseKLIEKTIV----DIKD 1359
Cdd:COG4172 413 -----GLDP--AAR-HRY-----PH--EFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQILdllrDLQR 473
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 124506379 1360 KADKTIITIAHRIASIKR-SDKIVVFnnpdRNGTFVQShGTHDELLSA 1406
Cdd:COG4172 474 EHGLAYLFISHDLAVVRAlAHRVMVM----KDGKVVEQ-GPTEQVFDA 516
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
377-594 |
7.58e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.02 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 377 KIEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIVnDSHNLKDINLK 451
Cdd:PRK14247 3 KIEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYL-DGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 WWRSKIGVVSQDPllfsNSIKNnikyslyslkdLEAMENyyeentndtyenknfslISNSMTSNELLEMKKEYQtikdSD 531
Cdd:PRK14247 79 ELRRRVQMVFQIP----NPIPN-----------LSIFEN-----------------VALGLKLNRLVKSKKELQ----ER 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124506379 532 VVDVSKKvlihdfvSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK14247 123 VRWALEK-------AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1133-1406 |
9.33e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1133 FRYISR--PNVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRfydlkndhiILkndmtnfqdyqnnnnnslvlknv 1210
Cdd:PRK11288 7 FDGIGKtfPGVKALDDISFDCRAGQVHALMGENGAGKST----LLK---------IL----------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1211 nefsnqSGsaeDYTVfnNNGEILLDDINICDYNLRD-LRNLFSIVSQEPMLF-NMSIYENIKFGREDATLEDVKRVSKFA 1288
Cdd:PRK11288 51 ------SG---NYQP--DAGSILIDGQEMRFASTTAaLAAGVAIIYQELHLVpEMTVAENLYLGQLPHKGGIVNRRLLNY 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1289 AIDEFIESLPNKYD--TNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIeKTIVDIKDKAdKTI 1365
Cdd:PRK11288 120 EAREQLEHLGVDIDpdTPL----KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLF-RVIRELRAEG-RVI 193
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 124506379 1366 ITIAHRIASIKR-SDKIVVFnnpdRNGTFVQSHG-----THDELLSA 1406
Cdd:PRK11288 194 LYVSHRMEEIFAlCDAITVF----KDGRYVATFDdmaqvDRDQLVQA 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1254-1415 |
1.12e-13 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 72.17 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1254 VSQEPMLF-NMSIYENIKFGredatLEDVKRVSKfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKI 1332
Cdd:TIGR03410 80 VPQGREIFpRLTVEENLLTG-----LAALPRRSR--KIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1333 LLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII----------TIAHRIASIKRsdkivvfnnpdrnGTFVQShGTHDE 1402
Cdd:TIGR03410 153 LLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILlveqyldfarELADRYYVMER-------------GRVVAS-GAGDE 218
|
170
....*....|...
gi 124506379 1403 LlsAQDGIyKKYV 1415
Cdd:TIGR03410 219 L--DEDKV-RRYL 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
378-594 |
1.42e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 71.71 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRkdveiYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND-SHNLKDINlkwwRSK 456
Cdd:COG3840 2 LRLDDLTYRYGDF-----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLTALPPA----ERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSN-SIKNNIKYSLY-SLKdleamenyyeentndtyenknfslisnsMTSNELlemkkeyqtikdSDVVD 534
Cdd:COG3840 73 VSMLFQENNLFPHlTVAQNIGLGLRpGLK----------------------------LTAEQR------------AQVEQ 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 535 VSKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:COG3840 113 ALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1126-1386 |
1.75e-13 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 71.38 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPNvPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknVNEFSNQSGsaedytvfnnngEILLDDINIcDYNLRDLRNLFSIVSQEPMLF-NMSIYENIKF-GRedatLEDVKR 1283
Cdd:cd03263 49 ----TGELRPTSG------------TAYINGYSI-RTDRKAARQSLGYCPQFDALFdELTVREHLRFyAR----LKGLPK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1284 VSKFAAIDEFIE--SLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKA 1361
Cdd:cd03263 108 SEIKEEVELLLRvlGLTDKANKRA----RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV--RK 181
|
250 260
....*....|....*....|....*.
gi 124506379 1362 DKTIITIAHRIASIKR-SDKIVVFNN 1386
Cdd:cd03263 182 GRSIILTTHSMDEAEAlCDRIAIMSD 207
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1230-1382 |
1.92e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.28 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFG---REDATleDVKRVSKFAAIDEFIESLPNKYDTnvg 1306
Cdd:PRK10247 62 GTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIFPwqiRNQQP--DPAIFLDDLERFALPDTILTKNIA--- 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 1307 pygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1382
Cdd:PRK10247 137 ----ELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1128-1405 |
1.98e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 72.36 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYisRPNVPIYK------NLSFtcDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnn 1201
Cdd:PRK13634 5 FQKVEHRY--QYKTPFERralydvNVSI--PSGSYVAIIGHTGSGKSTLLQHL--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1202 nNSLvLKNVNefsnqsgsaedytvfnnnGEILLDDINIC----DYNLRDLRNLFSIVSQ--EPMLFNMSIYENIKFG--- 1272
Cdd:PRK13634 54 -NGL-LQPTS------------------GTVTIGERVITagkkNKKLKPLRKKVGIVFQfpEHQLFEETVEKDICFGpmn 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1273 ----REDAtLEDVKRVSKFAAIDEfieSLPNKydtnvGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1348
Cdd:PRK13634 114 fgvsEEDA-KQKAREMIELVGLPE---ELLAR-----SPF--ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 1349 LIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNnpdrNGTfVQSHGTHDELLS 1405
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMH----KGT-VFLQGTPREIFA 235
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1148-1383 |
2.27e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 72.84 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1148 SFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDlkndhiilkndMTNfqdyqnnnnnslvlknvnefsnqsgsaedytvfn 1227
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEE-----------PTS---------------------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1228 nnGEILLDDINICDYNLRDLRNL---FSIVSQEPM--LfN--MSIYENIKFGREDATLEDVkrvskfAAIDEFIESL--- 1297
Cdd:COG4608 73 --GEILFDGQDITGLSGRELRPLrrrMQMVFQDPYasL-NprMTVGDIIAEPLRIHGLASK------AERRERVAELlel 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1298 ----PNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SnseklIEKTIV----DIKDKADKTIITI 1368
Cdd:COG4608 144 vglrPEHADR----YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvS-----IQAQVLnlleDLQDELGLTYLFI 214
|
250
....*....|....*.
gi 124506379 1369 AHRIASIKR-SDKIVV 1383
Cdd:COG4608 215 SHDLSVVRHiSDRVAV 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1127-1383 |
3.27e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.45 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1127 DIKDVNFRYiSRP--NVPIYKNLSFTCDSKKTTAIVGETGSGKS----TFMNLLLrfydlKNDHIilkndmtnfqdyqnn 1200
Cdd:PRK09473 14 DVKDLRVTF-STPdgDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLA-----ANGRI--------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1201 nnnslvlknvnefsnqSGSAEdytvFNNNgEILlddiNICDYNLRDLR-NLFSIVSQEPMlfnMSIYENIKFGREdatLE 1279
Cdd:PRK09473 73 ----------------GGSAT----FNGR-EIL----NLPEKELNKLRaEQISMIFQDPM---TSLNPYMRVGEQ---LM 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1280 DV----KRVSKFAAIDEFIESL-----PNKYdTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1350
Cdd:PRK09473 122 EVlmlhKGMSKAEAFEESVRMLdavkmPEAR-KRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQI 200
|
250 260 270
....*....|....*....|....*....|....*.
gi 124506379 1351 EKTIVDIKDKADKTIITIAHR---IASIkrSDKIVV 1383
Cdd:PRK09473 201 MTLLNELKREFNTAIIMITHDlgvVAGI--CDKVLV 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
378-619 |
4.19e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDI-IVNDSHNLKDINLK 451
Cdd:PRK14267 5 IETVNLRVYYG---SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVrLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 WWRSKIGVVSQDPLLFSN-SIknnikyslyslkdleamenyyeentndtYENknfslISNSMTSNELLEMKKEYqtikDS 530
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHlTI----------------------------YDN-----VAIGVKLNGLVKSKKEL----DE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 531 DVVDVSKKVLIHDFVSSLPDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKg 610
Cdd:PRK14267 125 RVEWALKKAALWDEVKDRLNDY-------PSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK- 196
|
....*....
gi 124506379 611 neNRITIII 619
Cdd:PRK14267 197 --KEYTIVL 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
378-621 |
4.34e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.68 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERL--YDPTEGDIIVNDSH------------ 443
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 444 ----------NLKDINLKWWRskigvvsqdpllFSNSIKNNIKyslyslKDLEAMEnyyeENTNDTYENKnfSLISNSMT 513
Cdd:TIGR03269 78 vgepcpvcggTLEPEEVDFWN------------LSDKLRRRIR------KRIAIML----QRTFALYGDD--TVLDNVLE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 514 SNELLEMKKEYQTIKDSDVVDVSKkvLIHDFVSSlpdkydtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSL 593
Cdd:TIGR03269 134 ALEEIGYEGKEAVGRAVDLIEMVQ--LSHRITHI------------ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTL 199
|
250 260
....*....|....*....|....*...
gi 124506379 594 DNKSEYLVQKTINNLKGNENRITIIIAH 621
Cdd:TIGR03269 200 DPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1263-1385 |
4.39e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.75 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1263 MSIYENIKFGREDATL---EDVKRVSKFAAI---DEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLD 1336
Cdd:PRK11000 90 LSVAENMSFGLKLAGAkkeEINQRVNQVAEVlqlAHLLDRKP-----------KALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 124506379 1337 EATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFN 1385
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLD 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1143-1386 |
5.43e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 69.99 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1143 IYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnslvlknvnefsnqSGSAED 1222
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAI------------------------------------------SGRVEG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1223 YTVFNnnGEILlddINICDYNLRDLRNLFSIVSQ-EPMLFNMSIYENIKF------GREDATLEDVKRVSkfaaidefIE 1295
Cdd:cd03234 60 GGTTS--GQIL---FNGQPRKPDQFQKCVAYVRQdDILLPGLTVRETLTYtailrlPRKSSDAIRKKRVE--------DV 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1296 SLPNKYDTNVG-PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRias 1374
Cdd:cd03234 127 LLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLA-RRNRIVILTIHQ--- 202
|
250
....*....|..
gi 124506379 1375 iKRSDKIVVFNN 1386
Cdd:cd03234 203 -PRSDLFRLFDR 213
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1126-1404 |
5.57e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.50 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiILKNDmtnfqdyqnnnnnsl 1205
Cdd:COG4604 2 IEIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISR---------LLPPD--------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnnNGEILLDDINICDYNLRDL-RNLfSIVSQEPMlFNM--SIYENIKFGR-----EDAT 1277
Cdd:COG4604 55 -----------------------SGEVLVDGLDVATTPSRELaKRL-AILRQENH-INSrlTVRELVAFGRfpyskGRLT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1278 LEDVKRVSKfaAIDEF-IESLPNKY-DTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1355
Cdd:COG4604 110 AEDREIIDE--AIAYLdLEDLADRYlDE--------LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLR 179
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 124506379 1356 DIKDKADKTIITIAHRI--ASiKRSDKIVVFnnpdRNGTfVQSHGTHDELL 1404
Cdd:COG4604 180 RLADELGKTVVIVLHDInfAS-CYADHIVAM----KDGR-VVAQGTPEEII 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
378-627 |
5.64e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.55 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNV--RFHYDTrkdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDINL----- 450
Cdd:PRK11264 4 IEVKNLvkKFHGQT-----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 451 --KWWRSKIGVVSQDPLLFSNSiknnikyslyslkdlEAMENYYEENtndtyenknfslisnsmtsnelLEMKKEyqtiK 528
Cdd:PRK11264 79 liRQLRQHVGFVFQNFNLFPHR---------------TVLENIIEGP----------------------VIVKGE----P 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 529 DSDVVDVSKKVLIHDFVSSLPDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKseyLVQKTINNL 608
Cdd:PRK11264 118 KEEATARARELLAKVGLAGKETSY-------PRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE---LVGEVLNTI 187
|
250 260
....*....|....*....|.
gi 124506379 609 KG--NENRITIIIAHRLSTIR 627
Cdd:PRK11264 188 RQlaQEKRTMVIVTHEMSFAR 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
378-619 |
6.04e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 70.05 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTR------------------KDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIV 439
Cdd:cd03267 1 IEVSNLSKSYRVYskepgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 440 NDshnlkdinLKWWRSKIGVVSQDPLLFSNsiKNNIKYslyslkDLEAMENYyeentndtYENKNFSLISNSMTSNELLE 519
Cdd:cd03267 81 AG--------LVPWKRRKKFLRRIGVVFGQ--KTQLWW------DLPVIDSF--------YLLAAIYDLPPARFKKRLDE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 520 MkkeyqtikdSDVVDVSKkvlihdfvsslpdkydtLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEY 599
Cdd:cd03267 137 L---------SELLDLEE-----------------LLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
250 260
....*....|....*....|
gi 124506379 600 LVQKTINNLkgNENRITIII 619
Cdd:cd03267 191 NIRNFLKEY--NRERGTTVL 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
378-621 |
6.70e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.91 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDT--RKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDINLKWW-- 453
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 454 --RSK--IGVVSQDpllfsnsiknnikYSLYSLKDLeaMENYYEEntndtyenknfslISnsmtsnelLEMKKEYQTIKd 529
Cdd:TIGR03269 360 rgRAKryIGILHQE-------------YDLYPHRTV--LDNLTEA-------------IG--------LELPDELARMK- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 530 sdVVDVSKKV-LIHDFVSSLPDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNL 608
Cdd:TIGR03269 403 --AVITLKMVgFDEEKAEEILDKY-------PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKA 473
|
250
....*....|...
gi 124506379 609 KGNENRITIIIAH 621
Cdd:TIGR03269 474 REEMEQTFIIVSH 486
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
397-635 |
7.47e-13 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 69.77 E-value: 7.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDI-NLK---WWRSKIGVVSQDPLLFSN-SI 471
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG----EDItGLPpheIARLGIGRTFQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 472 KNNI--------KYSLYSLKDLEAMENYYEEntndtyenknfslisnsmtSNELLEMKKeyqtikdsdvvdvskkvlihd 543
Cdd:cd03219 93 LENVmvaaqartGSGLLLARARREEREARER-------------------AEELLERVG--------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 544 fvssLPDKYDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSLdNKSEylVQKTINNLKG-NENRITI-IIAH 621
Cdd:cd03219 133 ----LADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPAAGL-NPEE--TEELAELIRElRERGITVlLVEH 201
|
250
....*....|....*
gi 124506379 622 RLSTI-RYANTIFVL 635
Cdd:cd03219 202 DMDVVmSLADRVTVL 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1146-1386 |
7.93e-13 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 70.07 E-value: 7.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1146 NLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLkndhiilkndmtnfqdyqnnnnnslvlknvnefsnqsgsaedytv 1225
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRP--------------------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1226 fnNNGEILLDDinicdynlRDLRNL--FSIVS-------QEPMLF-NMSIYENIKFGREDAT----LEDVKRVSKFAA-- 1289
Cdd:COG0411 57 --TSGRILFDG--------RDITGLppHRIARlgiartfQNPRLFpELTVLENVLVAAHARLgrglLAALLRLPRARRee 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1290 ------IDEFIE--SLPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEkTIVDIKDK 1360
Cdd:COG0411 127 rearerAEELLErvGLADRADEPAG----NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEeTEELAE-LIRRLRDE 201
|
250 260
....*....|....*....|....*..
gi 124506379 1361 ADKTIITIAHRIASIKR-SDKIVVFNN 1386
Cdd:COG0411 202 RGITILLIEHDMDLVMGlADRIVVLDF 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
376-635 |
8.33e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.81 E-value: 8.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 376 KKIEFKNVRFHYDTRKDVEI--YKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND---SHNLKDIN- 449
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEFkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaiPANLKKIKe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 450 LKWWRSKIGVVSQDP--LLFSNSIKNNIKYSLYSLKdleamenyyeENTNDTYENknfslisnsmtSNELLEMkkeyqti 527
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLG----------ENKQEAYKK-----------VPELLKL------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 528 kdsdvvdvskkvlihdfvSSLPDKYdtlVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINN 607
Cdd:PRK13645 137 ------------------VQLPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFER 195
|
250 260
....*....|....*....|....*....
gi 124506379 608 LKGNENRITIIIAHRLSTI-RYANTIFVL 635
Cdd:PRK13645 196 LNKEYKKRIIMVTHNMDQVlRIADEVIVM 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1125-1384 |
8.62e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.00 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1125 KVDIKDVNFRYISRPnvpIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtNFqdyqnnnnns 1204
Cdd:PRK10619 5 KLNVIDLHKRYGEHE---VLKGVSLQANAGDVISIIGSSGSGKSTFLRCI------------------NF---------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1205 lvLKNVNEFSNQSGSAEDYTVFNNNGEILLDDINicdyNLRDLRNLFSIVSQEPMLFN-MSIYENIK--------FGRED 1275
Cdd:PRK10619 54 --LEKPSEGSIVVNGQTINLVRDKDGQLKVADKN----QLRLLRTRLTMVFQHFNLWShMTVLENVMeapiqvlgLSKQE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1276 ATLEDVKRVSKfAAIDEFIEslpnkydtnvGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIV 1355
Cdd:PRK10619 128 ARERAVKYLAK-VGIDERAQ----------GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP---ELVGEVLR 193
|
250 260 270
....*....|....*....|....*....|.
gi 124506379 1356 DIKDKAD--KTIITIAHRIASIKRSDKIVVF 1384
Cdd:PRK10619 194 IMQQLAEegKTMVVVTHEMGFARHVSSHVIF 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
393-635 |
9.04e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 393 VEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDINLKWWRSKIGVVSQDPLLFSN-SI 471
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 472 KNNIKyslyslkdleamenyyeentndtyenknFSLISNSMTSNELLEMKKEYQTIKDSDVvdvskkvlihdfvsslpdk 551
Cdd:PRK15439 104 KENIL----------------------------FGLPKRQASMQKMKQLLAALGCQLDLDS------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 552 ydtlvgsNASKLSGGQKQRISIARAIMRNPKILILDEATSSLD-NKSEYLVQKtINNLKGNENRItIIIAHRLSTIR-YA 629
Cdd:PRK15439 137 -------SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAETERLFSR-IRELLAQGVGI-VFISHKLPEIRqLA 207
|
....*.
gi 124506379 630 NTIFVL 635
Cdd:PRK15439 208 DRISVM 213
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
378-639 |
9.07e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 67.09 E-value: 9.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlkdinlkwwRSKI 457
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------TVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQdpllfsnsiknnikyslyslkdleamenyyeentndtyenknfslisnsmtsnellemkkeyqtikdsdvvdvsk 537
Cdd:cd03221 66 GYFEQ--------------------------------------------------------------------------- 70
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 kvlihdfvsslpdkydtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGnenrITI 617
Cdd:cd03221 71 -------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVI 121
|
250 260
....*....|....*....|....*
gi 124506379 618 IIAH-R--LSTIryANTIFVLSNRE 639
Cdd:cd03221 122 LVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
388-594 |
9.71e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 68.93 E-value: 9.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 388 DTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND---SHNLKDInlkwwRSKIGVVSQDP 464
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvVKEPAEA-----RRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 465 LLFSN-SIKNNIKY--SLYSLKDLEAMENYYEentndtyenknfslISNSMTSNELLEMKkeyqtikdsdvvdvskkvli 541
Cdd:cd03266 88 GLYDRlTARENLEYfaGLYGLKGDELTARLEE--------------LADRLGMEELLDRR-------------------- 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 124506379 542 hdfvsslpdkydtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:cd03266 134 ------------------VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1126-1372 |
1.06e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 70.26 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPNVpiYKNLSFTCDSKKTTAIVGETGSGKSTFmnlllrfydlkndhiilkndmtnfqdYQNNNNnsl 1205
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTL--------------------------FQNLNG--- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 VLKNVNefsnqsgsaedytvfnnnGEILLDDINIcDYN---LRDLRNLFSIVSQEP--MLFNMSIYENIKFGREDATL-- 1278
Cdd:PRK13636 55 ILKPSS------------------GRILFDGKPI-DYSrkgLMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpe 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1279 EDVKRVSKFAAIDEFIESLPNKydtnvgPyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1358
Cdd:PRK13636 116 DEVRKRVDNALKRTGIEHLKDK------P-THCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQ 188
|
250
....*....|....
gi 124506379 1359 DKADKTIITIAHRI 1372
Cdd:PRK13636 189 KELGLTIIIATHDI 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
378-635 |
1.06e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.53 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDV--EIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTE-----GDIIVNDSHNLKDInl 450
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEgkvtvGDIVVSSTSKQKEI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 451 KWWRSKIGVVSQDP--LLFSNSIknnikyslysLKDLeamenyyeentndTYENKNFSLisnsmtsnelleMKKEYQTI- 527
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETV----------LKDV-------------AFGPQNFGI------------PKEKAEKIa 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 528 -KDSDVVDVSKkvlihDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTIN 606
Cdd:PRK13643 125 aEKLEMVGLAD-----EFWEKSP-----------FELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFE 188
|
250 260 270
....*....|....*....|....*....|
gi 124506379 607 NLKgNENRITIIIAHRLSTIR-YANTIFVL 635
Cdd:PRK13643 189 SIH-QSGQTVVLVTHLMDDVAdYADYVYLL 217
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1228-1389 |
1.10e-12 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 69.11 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1228 NNGEILLDDINICDYNL--RDLRNLfSIVSQEPMLF-NMSIYENIKFGREDATLEDVKRVSKFAA-IDEF-IESLPNKYd 1302
Cdd:cd03218 53 DSGKILLDGQDITKLPMhkRARLGI-GYLPQEASIFrKLTVEENILAVLEIRGLSKKEREEKLEElLEEFhITHLRKSK- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1303 tnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT---------IAHRiA 1373
Cdd:cd03218 131 ------ASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdhnvretlsITDR-A 203
|
170
....*....|....*.
gi 124506379 1374 SIKRSDKIVVFNNPDR 1389
Cdd:cd03218 204 YIIYEGKVLAEGTPEE 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
392-621 |
1.13e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.33 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 392 DVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLI---ERlYDPTEGDIIVNDshnlKDInLKW---WRSK--IGVVSQD 463
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDG----EDI-LELspdERARagIFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 464 PL--------LFSNSIKNNIKYSLYSLKDLEAmenyyeentndtyenknfsLISNSMtsnELLEMKKEYqtiKDSDVvdv 535
Cdd:COG0396 86 PVeipgvsvsNFLRTALNARRGEELSAREFLK-------------------LLKEKM---KELGLDEDF---LDRYV--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 536 skkvlihdfvsslpdkydtlvgsNASkLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRI 615
Cdd:COG0396 138 -----------------------NEG-FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLR-SPDRG 192
|
....*.
gi 124506379 616 TIIIAH 621
Cdd:COG0396 193 ILIITH 198
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1143-1415 |
1.18e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.12 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1143 IYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydlkNDHIilkndmtnfqdyqnnnnnslvlknvnefsnqSGsaed 1222
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRM----NDKV-------------------------------SG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1223 ytvFNNNGEILLDDINICDY-NLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVK--------RVSKFAAIDEF 1293
Cdd:PRK14271 77 ---YRYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKefrgvaqaRLTEVGLWDAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1294 IESLPNKydtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIA 1373
Cdd:PRK14271 154 KDRLSDS------PF--RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLA 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 124506379 1374 SIKR-SDKIVVFnnpdRNGTFVQSHGTHDELLSAQDGIYKKYV 1415
Cdd:PRK14271 224 QAARiSDRAALF----FDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
563-637 |
1.21e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 67.18 E-value: 1.21e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 563 LSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnenrITII-IAHRLSTIRYANTIFVLSN 637
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG-----ITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
378-637 |
1.35e-12 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 68.71 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDT-------------------RKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII 438
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 439 VNdshnlkdinlkwwrskiGVVSqdPLLFSNSIKNNikyslyslkDLEAMENYYeentndtyenknFSLISNSMTSNELL 518
Cdd:cd03220 81 VR-----------------GRVS--SLLGLGGGFNP---------ELTGRENIY------------LNGRLLGLSRKEID 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 519 EMKKEyqtikdsdvvdvskkvlIHDFvSSLPDKYDTLVgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSE 598
Cdd:cd03220 121 EKIDE-----------------IIEF-SELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 124506379 599 YLVQKTINNLKgNENRITIIIAHRLSTIR-YANTIFVLSN 637
Cdd:cd03220 179 EKCQRRLRELL-KQGKTVILVSHDPSSIKrLCDRALVLEK 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1197-1353 |
1.44e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.34 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1197 YQNNNNNSLVLKNVN------EF-----SNQSG-SaedyTVFN--------NNGEILLDDINICdyNLRDLR--NLFSIV 1254
Cdd:COG1101 12 NPGTVNEKRALDGLNltieegDFvtvigSNGAGkS----TLLNaiagslppDSGSILIDGKDVT--KLPEYKraKYIGRV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1255 SQEPML---FNMSIYEN--IKFGR-EDATLedVKRVSKfAAIDEFIES-------LPNKYDTNVGpygkSLSGGQKQRIA 1321
Cdd:COG1101 86 FQDPMMgtaPSMTIEENlaLAYRRgKRRGL--RRGLTK-KRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALS 158
|
170 180 190
....*....|....*....|....*....|...
gi 124506379 1322 IARALLREPKILLLDEATSSLD-SNSEKLIEKT 1353
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDpKTAALVLELT 191
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1128-1403 |
1.49e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.11 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYISRPNVPIY----KNLSFTCDSKKTTAIVGETGSGKSTF---MNLLLrfydlkndhiiLKNDMTNFQDYQNN 1200
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkalDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALL-----------LPDTGTIEWIFKDE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1201 NNNslvlKNVNEFsnqsgsaedytvfnnngEILLDDINICD------YNLRDLRNLFSIVSQ--EPMLFNMSIYENIKFG 1272
Cdd:PRK13651 72 KNK----KKTKEK-----------------EKVLEKLVIQKtrfkkiKKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1273 -------REDAtLEDVKRVSKFAAIDEfiESLPNKydtnvgPYGksLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1345
Cdd:PRK13651 131 pvsmgvsKEEA-KKRAAKYIELVGLDE--SYLQRS------PFE--LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQ 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 1346 SEKLIEKtIVDIKDKADKTIITIAHRIASI-KRSDKIVVFNnpdrNGTFVQSHGTHDEL 1403
Cdd:PRK13651 200 GVKEILE-IFDNLNKQGKTIILVTHDLDNVlEWTKRTIFFK----DGKIIKDGDTYDIL 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1139-1394 |
1.54e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1139 PNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYdlkndhiilkndmtnfqdyqnnnnnslvlknvnefsnQSG 1218
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-------------------------------------PHG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1219 SAEdytvfnnnGEILLDDINICDYNLRDL-RNLFSIVSQEPMLF-NMSIYENIKFGREdatledvkrVSKFAAID----- 1291
Cdd:PRK13549 59 TYE--------GEIIFEGEELQASNIRDTeRAGIAIIHQELALVkELSVLENIFLGNE---------ITPGGIMDydamy 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1292 ----EFIESLpnKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLdSNSEKLIEKTIV-DIKDKaDKTII 1366
Cdd:PRK13549 122 lraqKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL-TESETAVLLDIIrDLKAH-GIACI 197
|
250 260
....*....|....*....|....*....
gi 124506379 1367 TIAHRIASIKR-SDKIVVFnnpdRNGTFV 1394
Cdd:PRK13549 198 YISHKLNEVKAiSDTICVI----RDGRHI 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1128-1408 |
1.72e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 69.45 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFmnlllrfydLKNDHIILKNdmtnfqdyqnnnnnslvl 1207
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTL---------FRHFNGILKP------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqsgsaedytvfnNNGEILLDDINICDYNLRDLRNLFSIVSQEP--MLFNMSIYENIKFG------REDATLE 1279
Cdd:PRK13652 57 --------------------TSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDIAFGpinlglDEETVAH 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1280 DVKRVSKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1359
Cdd:PRK13652 117 RVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPE 185
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 124506379 1360 KADKTIITIAHRIASI-KRSDKIVVFNnpdrNGTFVqSHGTHDELLSAQD 1408
Cdd:PRK13652 186 TYGMTVIFSTHQLDLVpEMADYIYVMD----KGRIV-AYGTVEEIFLQPD 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
385-636 |
1.81e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.26 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 385 FHYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND--------------SHNLKDI-N 449
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitNPYSKKIkN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 450 LKWWRSKIGVVSQDP--LLFSNSIKNNIKYSLYSLKdleamenyyeentndtyenknfslisnsMTSNELLEMKKEYqti 527
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALG----------------------------VKKSEAKKLAKFY--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 528 kdsdvvdVSKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINN 607
Cdd:PRK13631 160 -------LNKMGLDDSYLERSP-----------FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD 221
|
250 260 270
....*....|....*....|....*....|
gi 124506379 608 LKGNeNRITIIIAHRLSTI-RYANTIFVLS 636
Cdd:PRK13631 222 AKAN-NKTVFVITHTMEHVlEVADEVIVMD 250
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1142-1386 |
2.02e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 72.25 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1142 PIYKNLSFTCDSKKTTAIVGETGSGKStfmnlllrfydlkndhiilkndmtnfqdyqnnnnnSLVLKNVNEFSNQSGSae 1221
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKS-----------------------------------SLLMMIMGELEPSEGK-- 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1222 dytvFNNNGEIllddinicdynlrdlrnlfSIVSQEPMLFNMSIYENIKFGredATLEDVKRVSKFAA--IDEFIESLPN 1299
Cdd:TIGR01271 483 ----IKHSGRI-------------------SFSPQTSWIMPGTIKDNIIFG---LSYDEYRYTSVIKAcqLEEDIALFPE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1300 KYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdIKDKADKTIITIAHRIASIKRSD 1379
Cdd:TIGR01271 537 KDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCL-CKLMSNKTRILVTSKLEHLKKAD 615
|
....*..
gi 124506379 1380 KIVVFNN 1386
Cdd:TIGR01271 616 KILLLHE 622
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1126-1386 |
2.12e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnLLLRFydlkndhiilkndmtnfqdyqnnnnNSL 1205
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKST---LLLHL-------------------------NGI 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 VLKnvnefsnQSGSAedyTVFNnngeillddINICDYNLRDLRNLFSIVSQEP--MLFNMSIYENIKFG------REDAT 1277
Cdd:PRK13647 55 YLP-------QRGRV---KVMG---------REVNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAFGpvnmglDKDEV 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1278 LEDVKRVSKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIeKTIVDI 1357
Cdd:PRK13647 116 ERRVEEALKAVRMWDFRDKPPYH-----------LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL-MEILDR 183
|
250 260 270
....*....|....*....|....*....|
gi 124506379 1358 KDKADKTIITIAHRI-ASIKRSDKIVVFNN 1386
Cdd:PRK13647 184 LHNQGKTVIVATHDVdLAAEWADQVIVLKE 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
393-627 |
2.34e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 393 VEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND-SHNLKDINLKWwRSKIGVVSQDpllfsnsi 471
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNiNYNKLDHKLAA-QLGIGIIYQE-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 472 knnikysLYSLKDLEAMENYYeentndtyenknfslISNSMTsnellemKKeyqtIKDSDVVDVSK---KVLIHDFVSSL 548
Cdd:PRK09700 89 -------LSVIDELTVLENLY---------------IGRHLT-------KK----VCGVNIIDWREmrvRAAMMLLRVGL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 549 PDKYDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKS-EYLVQkTINNLKgNENRITIIIAHRLSTIR 627
Cdd:PRK09700 136 KVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEvDYLFL-IMNQLR-KEGTAIVYISHKLAEIR 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1313-1387 |
2.75e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 67.84 E-value: 2.75e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1313 SGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIEKtIVDIKDkADKTIITIAHRIASIKR-SDKIVVFNNP 1387
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAaNRAVVVEL-IEEAKA-RGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
378-594 |
2.81e-12 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 67.84 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTR-KDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDIN----LKW 452
Cdd:COG4181 9 IELRGLTKTVGTGaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG-QDLFALDedarARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 453 WRSKIGVVSQDPLLFSNsiknnikyslyslkdLEAMENYyeentndtyenknfslisnsMTSNELLEMKKEYQTIKDS-D 531
Cdd:COG4181 88 RARHVGFVFQSFQLLPT---------------LTALENV--------------------MLPLELAGRRDARARARALlE 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124506379 532 VVDVSKKvLIHdfvssLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:COG4181 133 RVGLGHR-LDH-----YP-----------AQLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
391-594 |
2.85e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 391 KDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSH--NLKDINLKWWRSKIGVVSQDPLLfS 468
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidTLSPGKLQALRRDIQFIFQDPYA-S 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 469 NSIKNNIKYSLyslkdleaMEnyyeentndtyenknfslisnSMTSNELLEMKKeyqtikdsdvvdVSKKVL-IHDFVSS 547
Cdd:PRK10261 414 LDPRQTVGDSI--------ME---------------------PLRVHGLLPGKA------------AAARVAwLLERVGL 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 124506379 548 LPD---KYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK10261 453 LPEhawRY-------PHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
392-637 |
2.86e-12 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 67.74 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 392 DVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII---VNDSHNLKDINLKWWRSKIGVVSQDPLLFS 468
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 469 NSIKNNIkyslyslkdleamenyyeentndTYENKnFSlisnsmtsnellemKKEYQTIKDSdvvdvskkVLIHDFVSSL 548
Cdd:cd03290 93 ATVEENI-----------------------TFGSP-FN--------------KQRYKAVTDA--------CSLQPDIDLL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 549 PDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRLSTIR 627
Cdd:cd03290 127 PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLP 206
|
250
....*....|
gi 124506379 628 YANTIFVLSN 637
Cdd:cd03290 207 HADWIIAMKD 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1146-1412 |
2.86e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.88 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1146 NLSFTCDSKKTTAIVGETGSGKSTFMNLllrfydlKNDHIILKNDMTNFQDYQNNNNnslvLKNVNEfsnqsgsaedytv 1225
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQL-------TNGLIISETGQTIVGDYAIPAN----LKKIKE------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1226 fnnngeillddinicdynLRDLRNLFSIVSQEP--MLFNMSIYENIKFGREDATlEDVKRVSKfaAIDEFIE--SLPNKY 1301
Cdd:PRK13645 85 ------------------VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLG-ENKQEAYK--KVPELLKlvQLPEDY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1302 dTNVGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDK 1380
Cdd:PRK13645 144 -VKRSPF--ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADE 220
|
250 260 270
....*....|....*....|....*....|..
gi 124506379 1381 IVVFNNPDrngtfVQSHGTHDELLSAQDGIYK 1412
Cdd:PRK13645 221 VIVMHEGK-----VISIGSPFEIFSNQELLTK 247
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1263-1386 |
4.16e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 67.49 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1263 MSIYENIKFGrEDATLEDVKRVSKFAAIDEFIE--SLPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATS 1340
Cdd:TIGR01184 69 LTVRENIALA-VDRVLPDLSKSERRAIVEEHIAlvGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 124506379 1341 SLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNN 1386
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHRVTVLMVTHDVdEALLLSDRVVMLTN 190
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1128-1416 |
4.96e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYISRPnvpIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRFYDLKNdhiILKNDMTNFQDYQNNnnnslvl 1207
Cdd:PRK11124 5 LNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSS----LLRVLNLLE---MPRSGTLNIAGNHFD------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvneFSNQSGSAEdytvfnnngeillddinicdynLRDLRNLFSIVSQEPMLF-NMSIYENIkfgredatLEDVKRV-- 1284
Cdd:PRK11124 68 -----FSKTPSDKA----------------------IRELRRNVGMVFQQYNLWpHLTVQQNL--------IEAPCRVlg 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1285 -SKFAAIDEFIESLPN-KYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKAD 1362
Cdd:PRK11124 113 lSKDQALARAEKLLERlRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----ITAQIVSIIRELA 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1363 KTIIT---IAHRIASIKRSDKIVVFNnpdRNGTFVQsHGTHDELLSAQDGIYKKYVK 1416
Cdd:PRK11124 189 ETGITqviVTHEVEVARKTASRVVYM---ENGHIVE-QGDASCFTQPQTEAFKNYLS 241
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
387-619 |
5.04e-12 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 67.18 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 387 YDTRKDVeiyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDINL----KWWRSKIGVVSQ 462
Cdd:cd03218 10 YGKRKVV---NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG----QDITKlpmhKRARLGIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 463 DPLLFSN-SIKNNIKYSLyslkdleamenyyeentndtyenknfslisnsmtsnELLEMKKEYQTIKdsdvvdvsKKVLI 541
Cdd:cd03218 83 EASIFRKlTVEENILAVL------------------------------------EIRGLSKKEREEK--------LEELL 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 542 HDFvsslpdKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIII 619
Cdd:cd03218 119 EEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK--DRGIGVLI 188
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1230-1395 |
5.46e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.09 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDDINICDYN--LRDLRNLFsivsQEPMLF-NMSIYENIKFGREDATL---EDVKRVSKFAAI---DEFIESLPNK 1300
Cdd:PRK11607 74 GQIMLDGVDLSHVPpyQRPINMMF----QSYALFpHMTVEQNIAFGLKQDKLpkaEIASRVNEMLGLvhmQEFAKRKPHQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1301 ydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSD 1379
Cdd:PRK11607 150 -----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHdQEEAMTMAG 218
|
170
....*....|....*.
gi 124506379 1380 KIVVFNnpdrNGTFVQ 1395
Cdd:PRK11607 219 RIAIMN----RGKFVQ 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1252-1386 |
6.44e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 67.96 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1252 SIVSQEPMLFNMSIYENIKFGredATLEDV--KRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLRE 1329
Cdd:cd03291 101 SFSSQFSWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKD 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1330 PKILLLDEATSSLDSNSEKLIEKTIVdIKDKADKTIITIAHRIASIKRSDKIVVFNN 1386
Cdd:cd03291 178 ADLYLLDSPFGYLDVFTEKEIFESCV-CKLMANKTRILVTSKMEHLKKADKILILHE 233
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
60-303 |
6.55e-12 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 67.95 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 60 SFVCAVLSGGT---LPFFIS--VFGVILKNMnlGDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYLRS 134
Cdd:cd18572 1 AFVFLVVAALSelaIPHYTGavIDAVVADGS--REAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 135 VFYQDGQFHD-NNPG---SKLRSDLDfyleQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIyvcgV 210
Cdd:cd18572 79 LLRQDIAFFDaTKTGeltSRLTSDCQ----KVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVI----A 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 211 ICNKKV-----KLNKKTSLLYnNNTMSIIEEALMGIRTVASYCGEKTILNKFN-LSETFYSKYILKAnFVEALHIGLING 284
Cdd:cd18572 151 LITKVYgryyrKLSKEIQDAL-AEANQVAEEALSNIRTVRSFATEEREARRYErALDKALKLSVRQA-LAYAGYVAVNTL 228
|
250
....*....|....*....
gi 124506379 285 LILVSYAFGFWYGTRIIIN 303
Cdd:cd18572 229 LQNGTQVLVLFYGGHLVLS 247
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1245-1386 |
6.72e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.57 E-value: 6.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1245 RDLRNLFsiVSQEPMLF-NMSIYENIKFG------REDATLEDVKRvsKFAAIDEFI--ESLPNKYDTNvgpygksLSGG 1315
Cdd:PRK10851 72 RDRKVGF--VFQHYALFrHMTVFDNIAFGltvlprRERPNAAAIKA--KVTQLLEMVqlAHLADRYPAQ-------LSGG 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 1316 QKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFNN 1386
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHdQEEAMEVADRVVVMSQ 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
378-636 |
8.26e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 67.57 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDS---HNLKDI-NLkww 453
Cdd:PRK13636 6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidYSRKGLmKL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 454 RSKIGVVSQDP--LLFSNSIKNNIKYSLYSLKdleamenyyeentndtyenknfslisnsmtsnellemkkeyqtIKDSD 531
Cdd:PRK13636 81 RESVGMVFQDPdnQLFSASVYQDVSFGAVNLK-------------------------------------------LPEDE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 532 VVDVSKKVLIHDFVSSLPDKydtlvgsNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgN 611
Cdd:PRK13636 118 VRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQ-K 189
|
250 260
....*....|....*....|....*..
gi 124506379 612 ENRITIIIA-HRLSTIR-YANTIFVLS 636
Cdd:PRK13636 190 ELGLTIIIAtHDIDIVPlYCDNVFVMK 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1230-1385 |
8.46e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.59 E-value: 8.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDDINICDYNL--RDLrnlfSIVSQEPMLF-NMSIYENIKFG-------REdatlEDVKRVSK-FAAIDefIESLP 1298
Cdd:PRK11432 61 GQIFIDGEDVTHRSIqqRDI----CMVFQSYALFpHMSLGENVGYGlkmlgvpKE----ERKQRVKEaLELVD--LAGFE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1299 NKY-DtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIK 1376
Cdd:PRK11432 131 DRYvD--------QISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHdQSEAFA 202
|
....*....
gi 124506379 1377 RSDKIVVFN 1385
Cdd:PRK11432 203 VSDTVIVMN 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1263-1383 |
9.02e-12 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 66.24 E-value: 9.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1263 MSIYENIK-FGRedatLEDVKRVSKFAAIDEFIESLpnkydtNVGPY----GKSLSGGQKQRIAIARALLREPKILLLDE 1337
Cdd:cd03266 93 LTARENLEyFAG----LYGLKGDELTARLEELADRL------GMEELldrrVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 124506379 1338 ATSSLDSNSEKLIEKTIVDIKDkADKTIITIAHRIASIKR-SDKIVV 1383
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVERlCDRVVV 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
378-594 |
9.12e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.19 E-value: 9.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIivndSHNLKDINLKWWRS-K 456
Cdd:PRK10851 3 IEIANIKKSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI----RFHGTDVSRLHARDrK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSN-SIKNNIKYSLYSLKdleamenyyeentndTYENKNFSLISNSMTsnELLEMKKeyqtikdsdvvdv 535
Cdd:PRK10851 76 VGFVFQHYALFRHmTVFDNIAFGLTVLP---------------RRERPNAAAIKAKVT--QLLEMVQ------------- 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 536 skkvLIHdfvssLPDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK10851 126 ----LAH-----LADRY-------PAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1138-1383 |
9.13e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1138 RPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDlkndhiilkndmtnfQDYQNNNNNSLVLKNVN----EF 1213
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLE---------------QAGGLVQCDKMLLRRRSrqviEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1214 SNQSgsaedytvfnnngeillddinicDYNLRDLRNL-FSIVSQEPM-----LFNM--SIYENIK----FGREDATLEdV 1281
Cdd:PRK10261 91 SEQS-----------------------AAQMRHVRGAdMAMIFQEPMtslnpVFTVgeQIAESIRlhqgASREEAMVE-A 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1282 KRVSKFAAIDEfieslpnkYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1361
Cdd:PRK10261 147 KRMLDQVRIPE--------AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEM 218
|
250 260
....*....|....*....|...
gi 124506379 1362 DKTIITIAHRIASIKR-SDKIVV 1383
Cdd:PRK10261 219 SMGVIFITHDMGVVAEiADRVLV 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
985-1418 |
1.00e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.00 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 985 LIQEAFYNMHTVINYGLEDYFCNLIEKaidyknkgqkrriIVNAALWGFsQSAQLF--INSF----------AYWFGSFL 1052
Cdd:PLN03232 481 IINEILASMDTVKCYAWEKSFESRIQG-------------IRNEELSWF-RKAQLLsaFNSFilnsipvvvtLVSFGVFV 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1053 IKRGTILVDDFMKSLFTFIFTGSYAGKLMSLKGDSENAKLSFEKYYPLMIRKSNIdvrddggIRINKNLIKG--KVDIKD 1130
Cdd:PLN03232 547 LLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERI-------LAQNPPLQPGapAISIKN 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1131 VNFRYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLrfydlkndhiilkndmtnfqdyqnnnnnslvlknv 1210
Cdd:PLN03232 620 GYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML----------------------------------- 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1211 NEFSNqsgsAEDYTVfnnngeillddinicdynlrDLRNLFSIVSQEPMLFNMSIYENIKFGrEDATLEDVKRVSKFAAI 1290
Cdd:PLN03232 665 GELSH----AETSSV--------------------VIRGSVAYVPQVSWIFNATVRENILFG-SDFESERYWRAIDVTAL 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1291 DEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVD--IKDK-ADKTIIT 1367
Cdd:PLN03232 720 QHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH----VAHQVFDscMKDElKGKTRVL 795
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 124506379 1368 IAHRIASIKRSDKIVVFNNpdrngTFVQSHGTHDElLSAQDGIYKKYVKLA 1418
Cdd:PLN03232 796 VTNQLHFLPLMDRIILVSE-----GMIKEEGTFAE-LSKSGSLFKKLMENA 840
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
397-621 |
1.12e-11 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 66.34 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNdshnlkdinlkwwrskiGVVSQDP-----LLFSNsi 471
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILE-----------------GKQITEPgpdrmVVFQN-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 472 knnikYSLysLKDLEAMENYYeentndtyenknfslisnsMTSNELLEM--KKEYQTIKDSDVVDVSkkvlihdfVSSLP 549
Cdd:TIGR01184 63 -----YSL--LPWLTVRENIA-------------------LAVDRVLPDlsKSERRAIVEEHIALVG--------LTEAA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124506379 550 DKYDTlvgsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRIT-IIIAH 621
Cdd:TIGR01184 109 DKRPG-------QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI-WEEHRVTvLMVTH 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1230-1386 |
1.17e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 65.68 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDDINICDyNLRDLRNLFSIVSQEPMLF-NMSIYENIKFGredATLEDVKRVSKFAAIDEFIEslpnkyDTNVGPY 1308
Cdd:cd03264 54 GTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYpNFTVREFLDYI---AWLKGIPSKEVKARVDEVLE------LVNLGDR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1309 GK----SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRS-DKIVV 1383
Cdd:cd03264 124 AKkkigSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLcNQVAV 201
|
...
gi 124506379 1384 FNN 1386
Cdd:cd03264 202 LNK 204
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1105-1370 |
1.56e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.92 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1105 SNIDV----RDDGGIRINKNLIKGKVDIKdvnfryisRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLrFYDL 1180
Cdd:TIGR00955 6 RNSDVfgrvAQDGSWKQLVSRLRGCFCRE--------RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1181 KNDHIilkndmtnfqdyqnnnnnslvlknvnefsnqsgsaedytvfnnNGEILLDDINIcdyNLRDLRNLFSIVSQEPML 1260
Cdd:TIGR00955 77 KGVKG-------------------------------------------SGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1261 F-NMSIYENIKFGREDATLEDVKRVSKFAAIDEFIE--SLPNKYDTNVGPYG--KSLSGGQKQRIAIARALLREPKILLL 1335
Cdd:TIGR00955 111 IpTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGrvKGLSGGERKRLAFASELLTDPPLLFC 190
|
250 260 270
....*....|....*....|....*....|....*
gi 124506379 1336 DEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAH 1370
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKG-KTIICTIH 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
379-590 |
1.94e-11 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 65.39 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 379 EFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDI-NLKWW---R 454
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG----EDItGLPPHriaR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 455 SKIGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEAMEnyyeentndtyenknfslisnsmtsnELLEMkkeyqtikdsdvv 533
Cdd:COG0410 78 LGIGYVPEGRRIFPSlTVEENLLLGAYARRDRAEVR--------------------------ADLER------------- 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 534 dvskkvlIHDFVSSLPDKYDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEAT 590
Cdd:COG0410 119 -------VYELFPRLKERRRQRAGT----LSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1145-1385 |
2.00e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 66.34 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKKTTAIVGETGSGKSTFMnlllrfydlkndhiilkndmtnfqdyQNNNNnslVLKNvnefsnqsgsaedyt 1224
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLI--------------------------QNINA---LLKP--------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1225 vfnNNGEILLDDINIC----DYNLRDLRNLFSIVSQ--EPMLFNMSIYENIKFGREDATLeDVKRVsKFAAIDEFIESLP 1298
Cdd:PRK13646 60 ---TTGTVTVDDITIThktkDKYIRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKM-NLDEV-KNYAHRLLMDLGF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1299 NKYDTNVGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR- 1377
Cdd:PRK13646 135 SRDVMSQSPF--QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARy 212
|
....*...
gi 124506379 1378 SDKIVVFN 1385
Cdd:PRK13646 213 ADEVIVMK 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1127-1406 |
2.24e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 68.17 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1127 DIKD--VNFRYISRPnVPIYKNLSFTCDSKKTTAIVGETGSGKS----TFMNLLlrfydlkndhiilkndmtnfqdyqnn 1200
Cdd:COG4172 8 SVEDlsVAFGQGGGT-VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLL-------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1201 nnnslvlknvnefsnQSGSAEDytvfnnNGEILLDDINICDYNLRDLRNL----FSIVSQEPM--LfN--MSIYENIkfg 1272
Cdd:COG4172 61 ---------------PDPAAHP------SGSILFDGQDLLGLSERELRRIrgnrIAMIFQEPMtsL-NplHTIGKQI--- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1273 REdaTLEDVKRVSKFAAIDEFIESLpnkydTNVG---P------YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1343
Cdd:COG4172 116 AE--VLRLHRGLSGAAARARALELL-----ERVGipdPerrldaYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 1344 SNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFnnpdRNGTFVQsHGTHDELLSA 1406
Cdd:COG4172 189 VTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVM----RQGEIVE-QGPTAELFAA 247
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
389-594 |
2.27e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.81 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 389 TRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDP---TEGDIIVNDshnlKDIN-LKWWRSKIGVVSQDP 464
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNG----RRLTaLPAEQRRIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 465 LLFSN-SIKNNIKYSLyslkdleamenyyeentndtyenknfsliSNSMTSNEllemkkeyqtiKDSDVVDVSKKVLIHD 543
Cdd:COG4136 86 LLFPHlSVGENLAFAL-----------------------------PPTIGRAQ-----------RRARVEQALEEAGLAG 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 124506379 544 FVSSLPDkydtlvgsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:COG4136 126 FADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1252-1343 |
2.61e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.99 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1252 SIVSQEPMLFN-MSIYENIKFG---------REDATLEDV-KRVSkfaaIDEFIESLPNKydtnvgpygksLSGGQKQRI 1320
Cdd:PRK10771 74 SMLFQENNLFShLTVAQNIGLGlnpglklnaAQREKLHAIaRQMG----IEDLLARLPGQ-----------LSGGQRQRV 138
|
90 100
....*....|....*....|...
gi 124506379 1321 AIARALLREPKILLLDEATSSLD 1343
Cdd:PRK10771 139 ALARCLVREQPILLLDEPFSALD 161
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1125-1383 |
3.17e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 68.65 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1125 KVDIKDVNFRYISRPNVpIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLrfydlkndhiilkndmtnfqdyqnnnnns 1204
Cdd:PTZ00243 658 KTPKMKTDDFFELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLL----------------------------- 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1205 lvlknvNEFSNQSGS--AEdytvfnnngeillddinicdynlrdlRNlFSIVSQEPMLFNMSIYENIKFGRED--ATLED 1280
Cdd:PTZ00243 708 ------SQFEISEGRvwAE--------------------------RS-IAYVPQQAWIMNATVRGNILFFDEEdaARLAD 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1281 VKRVSKFAAiDefIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIvdIKD 1359
Cdd:PTZ00243 755 AVRVSQLEA-D--LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECF--LGA 829
|
250 260
....*....|....*....|....
gi 124506379 1360 KADKTIITIAHRIASIKRSDKIVV 1383
Cdd:PTZ00243 830 LAGKTRVLATHQVHVVPRADYVVA 853
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
378-594 |
3.48e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVndSHNLkdinlkwwrsKI 457
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--GETV----------KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDpllfsnsiknnikyslyslkdleamenyyeentndtyenknfslisnsmtsNELLEMKKeyqTIKD--SDVVDV 535
Cdd:COG0488 381 GYFDQH---------------------------------------------------QEELDPDK---TVLDelRDGAPG 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 536 SKKVLIHDFVSSL---PDKYDTLVGsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:COG0488 407 GTEQEVRGYLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1148-1343 |
3.63e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.14 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1148 SFTCDSKKTTAIVGETGSGKSTFMNLLLR---------FYD----LKNDHIILKNDMTNFQdyqnnnnnsLVlknvneFS 1214
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMietptggelYYQgqdlLKADPEAQKLLRQKIQ---------IV------FQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1215 NQSGSaedytvFNNN---GEILlddinicdynlrdlrnlfsivsQEPMLFNmsiyenikfgredATLEDVKRVSKFAAID 1291
Cdd:PRK11308 100 NPYGS------LNPRkkvGQIL----------------------EEPLLIN-------------TSLSAAERREKALAMM 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 124506379 1292 EFIESLPNKYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1343
Cdd:PRK11308 139 AKVGLRPEHYDR----YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
60-303 |
4.02e-11 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 65.58 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 60 SFVCAVLSGGT---LPFFI-SVFGVILKNMNLGDdINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYLRSV 135
Cdd:cd18576 1 GLILLLLSSAIglvFPLLAgQLIDAALGGGDTAS-LNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 136 FYQDGQFHDNN-PG---SKLRSDLdfylEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVCGVI 211
Cdd:cd18576 80 QRLPLSFFHERrVGeltSRLSNDV----TQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 212 CNKKV-KLNKKT--SLlynNNTMSIIEEALMGIRTVASYCGEKTILNKFN--LSETFysKYILKANFVEALHIGLINGLI 286
Cdd:cd18576 156 FGRRIrKLSKKVqdEL---AEANTIVEETLQGIRVVKAFTREDYEIERYRkaLERVV--KLALKRARIRALFSSFIIFLL 230
|
250
....*....|....*..
gi 124506379 287 LVSYAFGFWYGTRIIIN 303
Cdd:cd18576 231 FGAIVAVLWYGGRLVLA 247
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1305-1399 |
4.40e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 63.36 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1305 VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1383
Cdd:cd03222 65 YKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYlSDRIHV 144
|
90
....*....|....*..
gi 124506379 1384 F-NNPDRNGTFVQSHGT 1399
Cdd:cd03222 145 FeGEPGVYGIASQPKGT 161
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1145-1350 |
4.45e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiilkndmtnfqdyqnnnnnslvlknvnefsnqsgsaedyt 1224
Cdd:PRK15134 303 KNISFTLRPGETLGLVGESGSGKSTTGLALLR------------------------------------------------ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1225 VFNNNGEILLDDINICDYNLRDL---RNLFSIVSQEPmlfNMSIyeNIKFGREDATLEDV----KRVSKFAAIDEFIESL 1297
Cdd:PRK15134 335 LINSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP---NSSL--NPRLNVLQIIEEGLrvhqPTLSAAQREQQVIAVM 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1298 pnkydTNVG-------PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1350
Cdd:PRK15134 410 -----EEVGldpetrhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI 464
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
398-637 |
4.85e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.05 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 398 DLSFTLK-----EGKTYAFvGESGCGKSTILKLIERLYDPTEGDIIVNDsHNL----KDINLKWWRSKIGVVSQDPLLFS 468
Cdd:PRK11144 12 DLCLTVNltlpaQGITAIF-GRSGAGKTSLINAISGLTRPQKGRIVLNG-RVLfdaeKGICLPPEKRRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 469 N-SIKNNIKYSlyslkdleamenyyeentndtyenknfslisnsmtsnelleMKKEYQTIKDsDVVdvskKVL-IHDFVS 546
Cdd:PRK11144 90 HyKVRGNLRYG-----------------------------------------MAKSMVAQFD-KIV----ALLgIEPLLD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 547 SLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLD--NKSE---YL--VQKTINnlkgnenrITII- 618
Cdd:PRK11144 124 RYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlpRKREllpYLerLAREIN--------IPILy 184
|
250 260
....*....|....*....|
gi 124506379 619 IAHRLSTI-RYANTIFVLSN 637
Cdd:PRK11144 185 VSHSLDEIlRLADRVVVLEQ 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1145-1405 |
5.38e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.75 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKND--HIILKNDMTNFQDYqnnnnnslvlknvneFSNQSGSAED 1222
Cdd:TIGR03269 17 KNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTsgRIIYHVALCEKCGY---------------VERPSKVGEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1223 YTVFNNN-GEILLDDINICDYNLRDLRNLFSIVSQEPMLF--NMSIYENIKFGREDATLEDVKRVSKFAaidEFIESLpn 1299
Cdd:TIGR03269 82 CPVCGGTlEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAV---DLIEMV-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1300 KYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRS 1378
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIeDLS 236
|
250 260
....*....|....*....|....*..
gi 124506379 1379 DKIVVFNnpdrNGTFVQShGTHDELLS 1405
Cdd:TIGR03269 237 DKAIWLE----NGEIKEE-GTPDEVVA 258
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
57-305 |
7.11e-11 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 64.72 E-value: 7.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 57 LFISFVCAVLSGGT---LPFFISVF--GVILKNMNLGDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEY 131
Cdd:cd18544 1 FILALLLLLLATALellGPLLIKRAidDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 132 LRSVFYQDGQFHDNNPGSKL--R--SDLDFYLEQVSSGIgtkfITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYV 207
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLvtRvtNDTEALNELFTSGL----VTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 208 CGVICNKKVKLN-----KKTSLLynnNTMsiIEEALMGIRTVASYCGEKTILNKFN-LSETFYsKYILKANFVEALHIGL 281
Cdd:cd18544 157 ATYLFRKKSRKAyrevrEKLSRL---NAF--LQESISGMSVIQLFNREKREFEEFDeINQEYR-KANLKSIKLFALFRPL 230
|
250 260
....*....|....*....|....
gi 124506379 282 INGLILVSYAFGFWYGTRIIINSA 305
Cdd:cd18544 231 VELLSSLALALVLWYGGGQVLSGA 254
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
398-637 |
7.40e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 398 DLSFTLKEGKTYAFVGESGCGKS-TILKLIERLYDP----TEGDIIVNDSHNLK--DINLKWWR-SKIGVVSQDPLLFSN 469
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHasEQTLRGVRgNKIAMIFQEPMVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 470 SIkNNIKYSLYSLKDLEAmenyyeentndtyenknfslisnsmtsnellEMKKEyqtIKDSDVVDVSKKVLIHDFVSSLP 549
Cdd:PRK15134 107 PL-HTLEKQLYEVLSLHR-------------------------------GMRRE---AARGEILNCLDRVGIRQAAKRLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 550 DKydtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIR-Y 628
Cdd:PRK15134 152 DY--------PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRkL 223
|
....*....
gi 124506379 629 ANTIFVLSN 637
Cdd:PRK15134 224 ADRVAVMQN 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1245-1388 |
7.48e-11 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 63.54 E-value: 7.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1245 RDLRNLFSIVSQEPMLFN-MSIYENIK-FGRedatLEDVKRVSKFAAIDEFIE--SLPNKYDTNVGPYgkslSGGQKQRI 1320
Cdd:cd03265 69 REVRRRIGIVFQDLSVDDeLTGWENLYiHAR----LYGVPGAERRERIDELLDfvGLLEAADRLVKTY----SGGMRRRL 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 1321 AIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH----------RIASIKRSdKIVVFNNPD 1388
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHymeeaeqlcdRVAIIDHG-RIIAEGTPE 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1128-1396 |
7.56e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.93 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFryiSRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnslvl 1207
Cdd:COG0396 3 IKNLHV---SVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqSGSaEDYTVfnNNGEILLDDINICDY--NLRDLRNLFsiVS-QEP--------MLFNMSIYENIKFGREDA 1276
Cdd:COG0396 47 ---------MGH-PKYEV--TSGSILLDGEDILELspDERARAGIF--LAfQYPveipgvsvSNFLRTALNARRGEELSA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1277 tLEDVKRVSKFAAIDEFIESLPNKYdTNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1356
Cdd:COG0396 113 -REFLKLLKEKMKELGLDEDFLDRY-VNEG-----FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNK 185
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 124506379 1357 IKDKaDKTIITIAH--RIASIKRSDKIVVFnnpdRNGTFVQS 1396
Cdd:COG0396 186 LRSP-DRGILIITHyqRILDYIKPDFVHVL----VDGRIVKS 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
377-596 |
7.56e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 65.63 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 377 KIEFKNVRFHYDTrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-----IVNDshnL--KDIN 449
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIwiggrVVNE---LepADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 450 lkwwrskIGVVSQDPLLFSN-SIKNNIKYSLyslkdleamenyyeentndtyenKNFSlisnsmtsnelleMKKEyqTIk 528
Cdd:PRK11650 78 -------IAMVFQNYALYPHmSVRENMAYGL-----------------------KIRG-------------MPKA--EI- 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 529 DSDVVDVSKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNK 596
Cdd:PRK11650 112 EERVAEAARILELEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1128-1343 |
8.12e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.24 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnslvl 1207
Cdd:COG0488 1 LENLSKSF---GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKIL--------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqSGSAEDYTvfnnnGEILLDdinicdynlRDLRnlFSIVSQEPMLF-NMSIYENIKFG-------------- 1272
Cdd:COG0488 45 ---------AGELEPDS-----GEVSIP---------KGLR--IGYLPQEPPLDdDLTVLDTVLDGdaelraleaeleel 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1273 --REDATLEDVKRVS----KFAAIDEF-----IESL-------PNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILL 1334
Cdd:COG0488 100 eaKLAEPDEDLERLAelqeEFEALGGWeaearAEEIlsglgfpEEDLDRPVS----ELSGGWRRRVALARALLSEPDLLL 175
|
....*....
gi 124506379 1335 LDEATSSLD 1343
Cdd:COG0488 176 LDEPTNHLD 184
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1254-1343 |
8.68e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.28 E-value: 8.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1254 VSQEPMLF-NMSIYENIKFGredatledVKRVSK--FAAIDEF--IESLPNKYdtnvgPYgkSLSGGQKQRIAIARALLR 1328
Cdd:PRK11144 81 VFQDARLFpHYKVRGNLRYG--------MAKSMVaqFDKIVALlgIEPLLDRY-----PG--SLSGGEKQRVAIGRALLT 145
|
90
....*....|....*
gi 124506379 1329 EPKILLLDEATSSLD 1343
Cdd:PRK11144 146 APELLLMDEPLASLD 160
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
364-637 |
1.04e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 64.11 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 364 ENNDDGETLPNIKKIEFKNVRFHYDTrkdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIivndSH 443
Cdd:cd03291 26 QENNDRKHSSDDNNLFFSNLCLVGAP-----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----KH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 444 NlkdinlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLyslkdleamenyyeenTNDTYENKNfslisnsmtsnellemkke 523
Cdd:cd03291 97 S----------GRISFSSQFSWIMPGTIKENIIFGV----------------SYDEYRYKS------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 524 yqtikdsdvvdVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLV-Q 602
Cdd:cd03291 132 -----------VVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfE 200
|
250 260 270
....*....|....*....|....*....|....*
gi 124506379 603 KTINNLKGNENRitIIIAHRLSTIRYANTIFVLSN 637
Cdd:cd03291 201 SCVCKLMANKTR--ILVTSKMEHLKKADKILILHE 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
398-635 |
1.11e-10 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 63.52 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 398 DLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDIN-LK-WWRSKIGVVS--QDPLLFsnsikn 473
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG----RDITgLPpHRIARLGIARtfQNPRLF------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 474 nikyslyslKDLEAMEN---YYEENTNDTYENKNFSLISNSMTSNELLEMKKEyqtikdsdvvdvskkVLihDFVSsLPD 550
Cdd:COG0411 92 ---------PELTVLENvlvAAHARLGRGLLAALLRLPRARREEREARERAEE---------------LL--ERVG-LAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 551 KYDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNK-SEYLVQkTINNLKGNENrITI-IIAHRLSTI-R 627
Cdd:COG0411 145 RADEPAGN----LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEeTEELAE-LIRRLRDERG-ITIlLIEHDMDLVmG 218
|
....*...
gi 124506379 628 YANTIFVL 635
Cdd:COG0411 219 LADRIVVL 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1311-1382 |
1.13e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.88 E-value: 1.13e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124506379 1311 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIV 1382
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVdYALRYCERIV 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1156-1383 |
1.25e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 64.73 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1156 TTAIVGETGSGKSTFMNLLLRFYDLKNDHII-LKNDMTNFQDYQnnnnnslvlknvnefsnqsgsaedytvfnnngeill 1234
Cdd:PRK15079 49 TLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMKDDE------------------------------------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1235 ddinicdynLRDLRNLFSIVSQEP-------MLFNMSIYENIKFGREDATLEDVK-RVSKFAAIDEFIESLPNKYdtnvg 1306
Cdd:PRK15079 93 ---------WRAVRSDIQMIFQDPlaslnprMTIGEIIAEPLRTYHPKLSRQEVKdRVKAMMLKVGLLPNLINRY----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1307 PYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADK----TIITIAHRIASIKR-SDKI 1381
Cdd:PRK15079 159 PH--EFSGGQCQRIGIARALILEPKLIICDEPVSALDVS----IQAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRV 232
|
..
gi 124506379 1382 VV 1383
Cdd:PRK15079 233 LV 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
382-626 |
1.35e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 382 NVRFHYDtRKDVEIYKDLSFTLKEGKTYAFVGESGCGKS-TILKLIeRLYDPTEGDiivndshnlkdinlkwwrskigvV 460
Cdd:PRK10261 19 NIAFMQE-QQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGL-----------------------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 461 SQDPLLFSNSIKNNIKYSLYSLKDLEA-----MENYYEENTndTYENKNFSLisnsmtSNELLEMKKEYQTIKDSDVVDV 535
Cdd:PRK10261 74 QCDKMLLRRRSRQVIELSEQSAAQMRHvrgadMAMIFQEPM--TSLNPVFTV------GEQIAESIRLHQGASREEAMVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 536 SKKVLihDFVsSLPDKyDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 615
Cdd:PRK10261 146 AKRML--DQV-RIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMG 221
|
250
....*....|.
gi 124506379 616 TIIIAHRLSTI 626
Cdd:PRK10261 222 VIFITHDMGVV 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
400-594 |
1.44e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.06 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 400 SFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDS-HNLKDINlkwwRSKIGVVSQDPLLFSN-SIKNNIKY 477
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdHTTTPPS----RRPVSMLFQENNLFSHlTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 478 SLY-SLKdLEAmenyyeentndtyenknfslisnsmtsnellemkkeYQTIKdsdVVDVSKKVLIHDFVSSLPdkydtlv 556
Cdd:PRK10771 95 GLNpGLK-LNA------------------------------------AQREK---LHAIARQMGIEDLLARLP------- 127
|
170 180 190
....*....|....*....|....*....|....*...
gi 124506379 557 gsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK10771 128 ----GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
56-305 |
1.55e-10 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 63.69 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 56 LLFISfvcavlSGGTL--PFFI-----SVFGVILKNMNLGDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLK 128
Cdd:cd18573 4 LLLVS------SAVTMsvPFAIgklidVASKESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 129 LEYLRSVFYQDGQFHDNNPGSKLRSDL--DFYL------EQVSSGIGTkfiTIFTYASSFLGLYIwslikNARLTLCITC 200
Cdd:cd18573 78 KRLFKSILRQDAAFFDKNKTGELVSRLssDTSVvgksltQNLSDGLRS---LVSGVGGIGMMLYI-----SPKLTLVMLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 201 VFPLIYVCGVICNKKVK-LNKKT--SLlynNNTMSIIEEALMGIRTVASYCGEKTILNKFN--LSETFysKYILKANFVE 275
Cdd:cd18573 150 VVPPIAVGAVFYGRYVRkLSKQVqdAL---ADATKVAEERLSNIRTVRAFAAERKEVERYAkkVDEVF--DLAKKEALAS 224
|
250 260 270
....*....|....*....|....*....|
gi 124506379 276 ALHIGLINGLILVSYAFGFWYGTRIIINSA 305
Cdd:cd18573 225 GLFFGSTGFSGNLSLLSVLYYGGSLVASGE 254
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
378-637 |
1.62e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.97 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVeiyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINlkwwRSKI 457
Cdd:COG4152 2 LELKGLTKRFGDKTAV---DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-EPLDPED----RRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPLLFSN-SIKNNIKYsLYSLKDL---EAMENyyeentndtyenknfslisnsmtSNELLEmkkeyqtikdsdvv 533
Cdd:COG4152 74 GYLPEERGLYPKmKVGEQLVY-LARLKGLskaEAKRR-----------------------ADEWLE-------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 dvskKVlihdfvsSLPDKYDTLVgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLD--NKSeyLVQKTINNLKgn 611
Cdd:COG4152 116 ----RL-------GLGDRANKKV----EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpvNVE--LLKDVIRELA-- 176
|
250 260
....*....|....*....|....*...
gi 124506379 612 ENRITIIIA-HRLSTI-RYANTIFVLSN 637
Cdd:COG4152 177 AKGTTVIFSsHQMELVeELCDRIVIINK 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1311-1384 |
1.65e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 61.87 E-value: 1.65e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 1311 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAHRIASIKRSDKIVVF 1384
Cdd:NF040873 119 ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
378-608 |
1.91e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.67 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKDVEiykDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI------IVNDSHNLkdinlk 451
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVD---GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcgepVPSRARHA------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 wwRSKIGVVSQ-DPLLFSNSIKNNIK-YSLYslkdleamenyyeentndtyenknFSLisNSMTSNELLEMKKEYqtikd 529
Cdd:PRK13537 79 --RQRVGVVPQfDNLDPDFTVRENLLvFGRY------------------------FGL--SAAAARALVPPLLEF----- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 530 sdvvdvskkvlihdfvSSLPDKYDTLVGsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNL 608
Cdd:PRK13537 126 ----------------AKLENKADAKVG----ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL 184
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
399-595 |
1.91e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.20 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 399 LSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIV--NDSHNLKDINLKWWRSKIGVVSQD-PLLFSNSIknni 475
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsgHDITRLKNREVPFLRRQIGMIFQDhHLLMDRTV---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 476 kyslyslkdleamenyyeentndtYENKNFSLISNSMTSNELLEmkkeyqtiKDSDVVDvskKVLIHDFVSSLPdkydtl 555
Cdd:PRK10908 97 ------------------------YDNVAIPLIIAGASGDDIRR--------RVSAALD---KVGLLDKAKNFP------ 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 124506379 556 vgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDN 595
Cdd:PRK10908 136 -----IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1126-1386 |
2.05e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.48 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNfryISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRfydlkndhiilkndmtnfqdyqnnnnnsl 1205
Cdd:PRK09536 4 IDVSDLS---VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTT----LLR----------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsAEDYTVFNNNGEILLDDINICDYNLRDLRNLFSIVSQEPML-FNMSIYENIKFGREDATledvkrv 1284
Cdd:PRK09536 48 --------------AINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVVEMGRTPHR------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1285 SKFAAIDE----FIESLPNKYDTN--VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKlieKTIVDIK 1358
Cdd:PRK09536 107 SRFDTWTEtdraAVERAMERTGVAqfADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQV---RTLELVR 183
|
250 260 270
....*....|....*....|....*....|.
gi 124506379 1359 DKAD--KTIITIAHRIASIKR-SDKIVVFNN 1386
Cdd:PRK09536 184 RLVDdgKTAVAAIHDLDLAARyCDELVLLAD 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
381-609 |
2.17e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.60 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 381 KNVRFHYDTRKDVEiykDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDINL----KWWRSK 456
Cdd:PRK10895 7 KNLAKAYKGRRVVE---DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD----EDISLlplhARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEAmenyyeENTNDTyenknfslisnsmtSNELLEmkkEYQtikdsdvvdv 535
Cdd:PRK10895 80 IGYLPQEASIFRRlSVYDNLMAVLQIRDDLSA------EQREDR--------------ANELME---EFH---------- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 536 skkvlihdfVSSLPDkydtlvgSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLK 609
Cdd:PRK10895 127 ---------IEHLRD-------SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLR 184
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
326-467 |
2.26e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 64.82 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 326 VLISMFM---LTIILPNITEYMKALEATNSLYEI----INRKPLVENNDDGETLPNIKKIEFKNVRFHYDTRKDVEIYK- 397
Cdd:COG4615 269 VLVLLFLrgpLSQLVGALPTLSRANVALRKIEELelalAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDEGFTl 348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124506379 398 -DLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDsHNLKDINLKWWRSKIGVVSQDPLLF 467
Cdd:COG4615 349 gPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG-QPVTADNREAYRQLFSAVFSDFHLF 418
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
398-638 |
2.38e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 398 DLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSH----NLKD-INlkwwrSKIGVVSQDpllfsnsik 472
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfaSTTAaLA-----AGVAIIYQE--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 473 nnikysLYSLKDLEAMENYYeentndtyenknfslisnsmtsneLLEMKKEYQTIKDSDVVDVSKKVLIH---DFVSSLP 549
Cdd:PRK11288 88 ------LHLVPEMTVAENLY------------------------LGQLPHKGGIVNRRLLNYEAREQLEHlgvDIDPDTP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 550 DKYdtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNK-SEYLVqKTINNLKgNENRITIIIAHRLstiry 628
Cdd:PRK11288 138 LKY----------LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAReIEQLF-RVIRELR-AEGRVILYVSHRM----- 200
|
250
....*....|
gi 124506379 629 aNTIFVLSNR 638
Cdd:PRK11288 201 -EEIFALCDA 209
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
394-614 |
2.50e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.14 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 394 EIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNdSHNLKDIN----LKWWRSKIGVVSQDPLLfsn 469
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN-GQPMSKLSsaakAELRNQKLGFIYQFHHL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 470 siknnikyslysLKDLEAMENyyeentndtyenknfslisnsmTSNELLEMKKEYQTIKDSdVVDVSKKVLIHDFVSSLP 549
Cdd:PRK11629 99 ------------LPDFTALEN----------------------VAMPLLIGKKKPAEINSR-ALEMLAAVGLEHRANHRP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 550 dkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSeylvQKTINNLKGNENR 614
Cdd:PRK11629 144 -----------SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN----ADSIFQLLGELNR 193
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1145-1386 |
2.56e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 61.91 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiILKNDmtnfqdyqnnnnnslvlknvnefsnqsgsaEDYT 1224
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILG---------IILPD------------------------------SGEV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1225 VFNNNGEILLDdinicdynlrdlRNLFSIVSQEPMLF-NMSIYENIKFGredATLEDVKRVSKFAAIDEFIESLpnkydt 1303
Cdd:cd03269 58 LFDGKPLDIAA------------RNRIGYLPEERGLYpKMKVIDQLVYL---AQLKGLKKEEARRRIDEWLERL------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1304 NVGPYGKS----LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR-S 1378
Cdd:cd03269 117 ELSEYANKrveeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAG-KTVILSTHQMELVEElC 195
|
....*...
gi 124506379 1379 DKIVVFNN 1386
Cdd:cd03269 196 DRVLLLNK 203
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
57-350 |
2.91e-10 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 63.04 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 57 LFISFVCAVLsggtLPFFI-SVFGVILKNMNLGDD-----INPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLE 130
Cdd:cd18780 5 LLVSSGTNLA----LPYFFgQVIDAVTNHSGSGGEealraLNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 131 YLRSVFYQDGQFHD-NNPG---SKLRSDldfylEQVSSGIGTKFITIF-TYASSFLGLYIWSLIKNARLTLCITCVFPLI 205
Cdd:cd18780 81 LFSAIIAQEIAFFDvTRTGellNRLSSD-----TQVLQNAVTVNLSMLlRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 206 YVCGVICNKKVK-LNKKTSLLYNNNTmSIIEEALMGIRTVASYCGEKTILNKFN--LSETFysKYILKANFVEALHIGLI 282
Cdd:cd18780 156 SIGAVIYGKYVRkLSKKFQDALAAAS-TVAEESISNIRTVRSFAKETKEVSRYSekINESY--LLGKKLARASGGFNGFM 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 283 NGLILVSYAFGFWYGTRIIINSAtnqypnndfngasvISIllGVLISMFMLTIILPN--------ITEYMKALEAT 350
Cdd:cd18780 233 GAAAQLAIVLVLWYGGRLVIDGE--------------LTT--GLLTSFLLYTLTVAMsfaflsslYGDFMQAVGAS 292
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
57-274 |
3.02e-10 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 63.19 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 57 LFISFVCAVLSGGT---LPFFIS-VFGVILKNMNLGDDIN-----PIILSLVSIGLVQFILSMISSYCMDVITSKILKTL 127
Cdd:cd18547 1 LILVIILAIISTLLsvlGPYLLGkAIDLIIEGLGGGGGVDfsgllRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 128 ------KLEYLrSVFYqdgqFHDNNPG---SKLRSDLDfyleQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCI 198
Cdd:cd18547 81 rkdlfeKLQRL-PLSY----FDTHSHGdimSRVTNDVD----NISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 199 TCVFPLIYVCGVIcnkkvkLNKKTSLLYNNNTMSI------IEEALMGIRTVASYCGEKTILNKFN-LSETFYsKYILKA 271
Cdd:cd18547 152 LVTVPLSLLVTKF------IAKRSQKYFRKQQKALgelngyIEEMISGQKVVKAFNREEEAIEEFDeINEELY-KASFKA 224
|
...
gi 124506379 272 NFV 274
Cdd:cd18547 225 QFY 227
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
792-1081 |
3.04e-10 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 62.81 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 792 IFFSILVAgglypVFALLYARYVSTLFD-FANLEYNSN---KYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRL 867
Cdd:cd18541 5 ILFLILVD-----LLQLLIPRIIGRAIDaLTAGTLTASqllRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 868 FENILYQEMSFFdqDKNTPGVLSAHINRDVHLLKTGLVNNIVIFSHFIMLFLVSMVMSFYfcpiVAAVLTFIYFINMRVF 947
Cdd:cd18541 80 FAHLLTLSPSFY--QKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFT----ISPKLTLIALLPLPLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 948 AVRARLTkSKEIEKKenmssgvfaFSSDDEMFKDPSFLIQEAFYNMHTVINYGLEDYFCNLIEKAI-DYKNKgQKRRIIV 1026
Cdd:cd18541 154 ALLVYRL-GKKIHKR---------FRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNeEYVEK-NLRLARV 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 1027 NAALWGFSQsaqlFINSFAY----WFGSFLIKRGTILVDDFMkslfTFIftgSYAGKLM 1081
Cdd:cd18541 223 DALFFPLIG----LLIGLSFlivlWYGGRLVIRGTITLGDLV----AFN---SYLGMLI 270
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
561-635 |
3.13e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.34 E-value: 3.13e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 561 SKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 635
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVAL 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
383-440 |
3.17e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.02 E-value: 3.17e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 383 VRFHYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN 440
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN 86
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
377-634 |
3.21e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.18 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 377 KIEFKNVRFHYDTRKDVEI--YKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI--IVNDSHNLKDINLKW 452
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 453 W---------------------RSKIGVVSQ--DPLLFSNSIKNNIKyslyslkdleamenyyeentndtyenknFSLIS 509
Cdd:PRK13651 82 KvleklviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQTIEKDII----------------------------FGPVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 510 NSMTSNELLEMKKEYQTIKDsdvvdvskkvlihdfvssLPDKYdtlVGSNASKLSGGQKQRISIARAIMRNPKILILDEA 589
Cdd:PRK13651 134 MGVSKEEAKKRAAKYIELVG------------------LDESY---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEP 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 124506379 590 TSSLDNKSEYLVQKTINNLkgNENRITIIIA-HRL-STIRYAN-TIFV 634
Cdd:PRK13651 193 TAGLDPQGVKEILEIFDNL--NKQGKTIILVtHDLdNVLEWTKrTIFF 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1308-1351 |
3.32e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 61.68 E-value: 3.32e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 124506379 1308 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIE 1351
Cdd:COG4181 143 YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAaTGEQIID 187
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
378-638 |
3.60e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 61.35 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkdvEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVND-SHNLKDINlkwwRSK 456
Cdd:cd03298 1 VRLDKIRFSYG-----EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPA----DRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDPLLFSN-SIKNNIKYSLyslkdleamenyyeentndtyeNKNFSLisnsmtsnellemkkeyqTIKDSDVVDV 535
Cdd:cd03298 72 VSMLFQENNLFAHlTVEQNVGLGL----------------------SPGLKL------------------TAEDRQAIEV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 536 S-KKVLIHDFVSSLPDKydtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 614
Cdd:cd03298 112 AlARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKM 180
|
250 260
....*....|....*....|....*.
gi 124506379 615 ITIIIAHRLSTIR--YANTIFVLSNR 638
Cdd:cd03298 181 TVLMVTHQPEDAKrlAQRVVFLDNGR 206
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1127-1414 |
4.02e-10 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 61.54 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1127 DIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNdhiilkndmtnfqdyqnnnnnslv 1206
Cdd:COG0410 5 EVENLHAGY---GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRS------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1207 lknvnefsnqsgsaedytvfnnnGEILLDDinicdynlRDLRNL---------FSIVSQEPMLF-NMSIYENIKFG---- 1272
Cdd:COG0410 58 -----------------------GSIRFDG--------EDITGLpphriarlgIGYVPEGRRIFpSLTVEENLLLGayar 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1273 ----REDATLEDVkrVSKFAAIDEFIESLpnkydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLdsnSEK 1348
Cdd:COG0410 107 rdraEVRADLERV--YELFPRLKERRRQR-----------AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL---APL 170
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 1349 LIEK---TIVDIKDkADKTIITI---AHRIASIkrSDKIVVFnnpdRNGTFVQShGTHDELLsAQDGIYKKY 1414
Cdd:COG0410 171 IVEEifeIIRRLNR-EGVTILLVeqnARFALEI--ADRAYVL----ERGRIVLE-GTAAELL-ADPEVREAY 233
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
378-623 |
4.45e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIvnDSHNLKdinlkwwrskI 457
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--RNGKLR----------I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQ----DPLLfsnsiknnikyslyslkdleamenyyeentndtyenknfslisnSMTSNELLEMKKeyqTIKDSDVV 533
Cdd:PRK09544 70 GYVPQklylDTTL--------------------------------------------PLTVNRFLRLRP---GTKKEDIL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 DVSKKVlihdfvsslpdKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEN 613
Cdd:PRK09544 103 PALKRV-----------QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELD 171
|
250
....*....|
gi 124506379 614 RITIIIAHRL 623
Cdd:PRK09544 172 CAVLMVSHDL 181
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1146-1409 |
4.66e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.69 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1146 NLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYdlkndhiilkndmtnfqdyqnnnnnslvlknvnefsnQSGSAEdytv 1225
Cdd:TIGR02633 19 GIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-------------------------------------PHGTWD---- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1226 fnnnGEILLDDINICDYNLRDL-RNLFSIVSQEPMLF-NMSIYENIKFGRE----------DATLEDVKRVSKFAAIDEF 1293
Cdd:TIGR02633 58 ----GEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpELSVAENIFLGNEitlpggrmayNAMYLRAKNLLRELQLDAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1294 IESLPnkydtnVGPYGkslsGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIA 1373
Cdd:TIGR02633 134 NVTRP------VGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHG-VACVYISHKLN 202
|
250 260 270
....*....|....*....|....*....|....*..
gi 124506379 1374 SIKR-SDKIVVFNNPDRNGTFVQSHGTHDELLSAQDG 1409
Cdd:TIGR02633 203 EVKAvCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
382-594 |
4.67e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 63.94 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 382 NVRFHYDTRkDVEIYKDLSFTLKEGKTYAFVGESGCGKS----TILKLIERLYDPTEGDIIVNDsHNLKDINLKWWR--- 454
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDG-QDLLGLSERELRrir 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 455 -SKIGVVSQDPL-----LFsnSIKNNIKYSLyslkdleamenyyeentndtyenknfsLISNSMTSNELLEMkkeyqtik 528
Cdd:COG4172 91 gNRIAMIFQEPMtslnpLH--TIGKQIAEVL---------------------------RLHRGLSGAAARAR-------- 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 529 dsdVVDVSKKVLIHDfvsslPDKydtLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:COG4172 134 ---ALELLERVGIPD-----PER---RLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
378-623 |
5.25e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.82 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRK-DVEIYKDLSFTLKEGKTYAFVGESGCGKS-TILKLIERLYDP--TEGDIIVNDSH--NLKDINLK 451
Cdd:PRK09473 13 LDVKDLRVTFSTPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREilNLPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 WWRS-KIGVVSQDPLLfsnsiknnikyslySLkdleameNYYEEntndtyenknfslisnsmTSNELLEMKKEYQTIKDS 530
Cdd:PRK09473 93 KLRAeQISMIFQDPMT--------------SL-------NPYMR------------------VGEQLMEVLMLHKGMSKA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 531 DVVDVSKKVLihDFVSsLPDKYDTLvGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKG 610
Cdd:PRK09473 134 EAFEESVRML--DAVK-MPEARKRM-KMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKR 209
|
250
....*....|...
gi 124506379 611 NENRITIIIAHRL 623
Cdd:PRK09473 210 EFNTAIIMITHDL 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1128-1372 |
6.27e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 61.42 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRY-ISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILkndmtnfqdyqnnNNNSLv 1206
Cdd:COG4525 6 VRHVSVRYpGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL-------------DGVPV- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1207 lknvnefsnQSGSAEDYTVFNNNGeiLLddinicdynlrdlrnlfsivsqePMLfnmSIYENIKFG----------REDA 1276
Cdd:COG4525 72 ---------TGPGADRGVVFQKDA--LL-----------------------PWL---NVLDNVAFGlrlrgvpkaeRRAR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1277 TLEDVKRVSKFAAIDEFIESLpnkydtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1356
Cdd:COG4525 115 AEELLALVGLADFARRRIWQL---------------SGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLD 179
|
250
....*....|....*.
gi 124506379 1357 IKDKADKTIITIAHRI 1372
Cdd:COG4525 180 VWQRTGKGVFLITHSV 195
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1229-1417 |
6.71e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.63 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1229 NGEILLDDINIcDYNLRDL---RNLFSIVSQEP--MLFNMSIYENIKFGREDATL--EDVKRVSKFAAIDEFIESLPNKy 1301
Cdd:PRK13639 56 SGEVLIKGEPI-KYDKKSLlevRKTVGIVFQNPddQLFAPTVEEDVAFGPLNLGLskEEVEKRVKEALKAVGMEGFENK- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1302 dtnvGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI-KRSDK 1380
Cdd:PRK13639 134 ----PPH--HLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVpVYADK 206
|
170 180 190
....*....|....*....|....*....|....*..
gi 124506379 1381 IVVFNnpdrNGTFVQShGTHDELLSAQDGIYKKYVKL 1417
Cdd:PRK13639 207 VYVMS----DGKIIKE-GTPKEVFSDIETIRKANLRL 238
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1230-1386 |
7.22e-10 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 60.31 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDDINICDyNLRDLRNLFSIVSqEPMLF-NMSIYENIKFGredATLEDVKRvskfAAIDEFIE--SLPNKYDTNVG 1306
Cdd:cd03268 55 GEITFDGKSYQK-NIEALRRIGALIE-APGFYpNLTARENLRLL---ARLLGIRK----KRIDEVLDvvGLKDSAKKKVK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1307 PYgkSLsgGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI-KRSDKIVVFN 1385
Cdd:cd03268 126 GF--SL--GMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQG-ITVLISSHLLSEIqKVADRIGIIN 200
|
.
gi 124506379 1386 N 1386
Cdd:cd03268 201 K 201
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
378-637 |
9.28e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYdtRKDVE-IYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDI---NLKWW 453
Cdd:PTZ00243 1309 LVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG----REIgayGLREL 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 454 RSKIGVVSQDPLLFSNSIKNNIkyslyslkD--LEAmenyyeentndtyenknfslisnsmTSNEL---LEMkkeyqtik 528
Cdd:PTZ00243 1383 RRQFSMIPQDPVLFDGTVRQNV--------DpfLEA-------------------------SSAEVwaaLEL-------- 1421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 529 dsdvvdvskkVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILIL-DEATSSLDNKSEYLVQKTINN 607
Cdd:PTZ00243 1422 ----------VGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMS 1491
|
250 260 270
....*....|....*....|....*....|
gi 124506379 608 LKGNENRITiiIAHRLSTIRYANTIFVLSN 637
Cdd:PTZ00243 1492 AFSAYTVIT--IAHRLHTVAQYDKIIVMDH 1519
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
410-624 |
1.26e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 410 AFVGESGCGKSTILKLIERLYDPTEG-----DIIVNDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKd 484
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHK- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 485 leamenyyeentndtyenknfslisnsmtsnelLEMKKEYQTIKDSDVVDVSKKVLIHDFVSSLPdkydtlvgsnaSKLS 564
Cdd:PRK14271 130 ---------------------------------LVPRKEFRGVAQARLTEVGLWDAVKDRLSDSP-----------FRLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124506379 565 GGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgneNRIT-IIIAHRLS 624
Cdd:PRK14271 166 GGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA---DRLTvIIVTHNLA 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1230-1367 |
1.30e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.29 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLD--DINICDYNLRDLRNLfSIVSQEPMLFN-MSIYENIKFG---REDATLEDVKRVSKfAAIDEF-IESLPNKYd 1302
Cdd:PRK10895 58 GNIIIDdeDISLLPLHARARRGI-GYLPQEASIFRrLSVYDNLMAVlqiRDDLSAEQREDRAN-ELMEEFhIEHLRDSM- 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 1303 tnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1367
Cdd:PRK10895 135 ------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLIT 193
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1128-1383 |
1.49e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.08 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVnfrYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydlkndhiilkndmtnfqdyqnnnnnslvl 1207
Cdd:cd03217 3 IKDL---HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH------------------------------ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsnqsgsaEDYTVfnNNGEILLDDINICDY--NLRDLRNLFsIVSQEPmlfnmsiyenikfgredATLEDVKrvs 1285
Cdd:cd03217 50 -------------PKYEV--TEGEILFKGEDITDLppEERARLGIF-LAFQYP-----------------PEIPGVK--- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1286 kfaaIDEFIESLpnkydtNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTI 1365
Cdd:cd03217 94 ----NADFLRYV------NEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSV 157
|
250 260
....*....|....*....|
gi 124506379 1366 ITIAH--RIASIKRSDKIVV 1383
Cdd:cd03217 158 LIITHyqRLLDYIKPDRVHV 177
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
400-635 |
1.55e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.07 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 400 SFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEgdIIVNDSHNLKDINL---------KWWRSKIGVVSQDPLLF--- 467
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNW--HVTADRFRWNGIDLlklsprerrKIIGREIAMIFQEPSSCldp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 468 SNSIKNNIKyslyslkdlEAMEnyyeentNDTYENKNFslisnsmtsnELLEMKKEYqtikdsdVVDVSKKVLIHDfvss 547
Cdd:COG4170 105 SAKIGDQLI---------EAIP-------SWTFKGKWW----------QRFKWRKKR-------AIELLHRVGIKD---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 548 lpdkYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITII--IAHRLST 625
Cdd:COG4170 148 ----HKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARL--NQLQGTSIllISHDLES 221
|
250
....*....|.
gi 124506379 626 I-RYANTIFVL 635
Cdd:COG4170 222 IsQWADTITVL 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1136-1343 |
1.57e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.17 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1136 ISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnslvlknvnefsn 1215
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL----------------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1216 qSGSAEDYTvfnnnGEILLDDINICDYNLRDLRNLFSIVSQEPML-FNMSIYENIKFGREDATLEDVKRVskfAAIDEFI 1294
Cdd:PRK13548 49 -SGELSPDS-----GEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDD---ALVAAAL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 1295 ESlpnkydTNVGPYGK----SLSGGQKQRIAIARALLR------EPKILLLDEATSSLD 1343
Cdd:PRK13548 120 AQ------VDLAHLAGrdypQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD 172
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
793-1034 |
1.63e-09 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 60.58 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 793 FFSILVAGGLypVFALLYA-RY-VSTLFDFANLEyNSNKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFEN 870
Cdd:cd18575 2 LIALLIAAAA--TLALGQGlRLlIDQGFAAGNTA-LLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 871 ILYQEMSFFdqDKNTPGVLSAHINRDVHLLKT--------GLVNNIVIFSHFIMLFLVSMVMSFYFCPIVAAVLTFIYFI 942
Cdd:cd18575 79 LLRLSPSFF--ETTRTGEVLSRLTTDTTLIQTvvgsslsiALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 943 NMRvfaVRaRLTKskeiekkenmssgvfafSSDDEMfKDPSFLIQEAFYNMHTVINYGLEDY----FCNLIEKAIDYknk 1018
Cdd:cd18575 157 GRR---VR-RLSR-----------------ASQDRL-ADLSAFAEETLSAIKTVQAFTREDAerqrFATAVEAAFAA--- 211
|
250
....*....|....*.
gi 124506379 1019 gQKRRIIVNAALWGFS 1034
Cdd:cd18575 212 -ALRRIRARALLTALV 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1262-1339 |
1.71e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.96 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1262 NMSIYENIkfgredaTLEDVKRVSKF---------AAIDEFIESL---PNKYDTNVGpygkSLSGGQKQRIAIARALLRE 1329
Cdd:COG1129 344 DLSIRENI-------TLASLDRLSRGglldrrrerALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATD 412
|
90
....*....|
gi 124506379 1330 PKILLLDEAT 1339
Cdd:COG1129 413 PKVLILDEPT 422
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
58-303 |
1.72e-09 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 60.58 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 58 FISFVCAvlSGGTLPFFISVFGVILKNMNLGD--DINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYLRSV 135
Cdd:cd18575 2 LIALLIA--AAATLALGQGLRLLIDQGFAAGNtaLLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 136 FYQDGQFHDNN-PG---SKLRSDLdfylEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVCGVI 211
Cdd:cd18575 80 LRLSPSFFETTrTGevlSRLTTDT----TLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 212 CNKKVKLNKKTSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNKFN--LSETFysKYILKANFVEALHIGLINGLILVS 289
Cdd:cd18575 156 FGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFAtaVEAAF--AAALRRIRARALLTALVIFLVFGA 233
|
250
....*....|....
gi 124506379 290 YAFGFWYGTRIIIN 303
Cdd:cd18575 234 IVFVLWLGAHDVLA 247
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1140-1406 |
1.80e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1140 NVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiILKNdmtnfqdyqnnnnnslvlknvnefsnQSGs 1219
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFAR---------LLTP--------------------------QSG- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1220 aedytvfnnngEILLDDINICDYNLRDLRNLFSIVSQEPML-FNMSIYENIKFGRE-------DATLEDVKRVSKfAAID 1291
Cdd:PRK11231 58 -----------TVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRELVAYGRSpwlslwgRLSAEDNARVNQ-AMEQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1292 EFIESLPNKYDTnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHR 1371
Cdd:PRK11231 126 TRINHLADRRLT-------DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQG-KTVVTVLHD 197
|
250 260 270
....*....|....*....|....*....|....*.
gi 124506379 1372 IASIKR-SDKIVVFnnpdRNGTFVqSHGTHDELLSA 1406
Cdd:PRK11231 198 LNQASRyCDHLVVL----ANGHVM-AQGTPEEVMTP 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1308-1373 |
2.11e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.76 E-value: 2.11e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 1308 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKAD--KTIITIAHRIA 1373
Cdd:PRK11264 141 YPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRQLAQekRTMVIVTHEMS 205
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1294-1392 |
2.25e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 59.73 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1294 IESLpnkYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA 1373
Cdd:cd03237 105 IEQI---LDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDII 177
|
90 100
....*....|....*....|.
gi 124506379 1374 SIKR-SDKIVVFN-NPDRNGT 1392
Cdd:cd03237 178 MIDYlADRLIVFEgEPSVNGV 198
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
399-594 |
3.65e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.42 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 399 LSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDShnlkdiNLKWWRSKigvvsqdplLFSNSIKnnikys 478
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ------PLESWSSK---------AFARKVA------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 479 lYSLKDLEAMEnyyeentndtyenknfslisnSMTSNELLEMKKeYQ--------TIKDSDVVD-----VSKKVLIHDFV 545
Cdd:PRK10575 89 -YLPQQLPAAE---------------------GMTVRELVAIGR-YPwhgalgrfGAADREKVEeaislVGLKPLAHRLV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 124506379 546 SSlpdkydtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK10575 146 DS---------------LSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1310-1386 |
3.67e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 59.74 E-value: 3.67e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 1310 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEkLIEKTIVDIKDKaDKTIITIAHRIASIKR-SDKIVVFNN 1386
Cdd:COG4152 128 EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPvNVE-LLKDVIRELAAK-GTTVIFSSHQMELVEElCDRIVIINK 204
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
828-1086 |
4.03e-09 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 59.57 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 828 NKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFdqDKNTPGVLSAHINRDVHLLKTGLVNN 907
Cdd:cd18780 42 NQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFF--DVTRTGELLNRLSSDTQVLQNAVTVN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 908 IVIFSHFIMLFLVSMVMSFYFCP----IVAAVLTFIyfinmrVFAVRARLTKSKEIEKKENMSSGvfafssddemfkDPS 983
Cdd:cd18780 120 LSMLLRYLVQIIGGLVFMFTTSWkltlVMLSVVPPL------SIGAVIYGKYVRKLSKKFQDALA------------AAS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 984 FLIQEAFYNMHTVINYGLEDYFCNLIEKAIDYKNKGQKRRIIVNAALWGF-SQSAQLFInSFAYWFGSFLIKRGTI---L 1059
Cdd:cd18780 182 TVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFmGAAAQLAI-VLVLWYGGRLVIDGELttgL 260
|
250 260
....*....|....*....|....*..
gi 124506379 1060 VDDFMksLFTFIFTGSYAGkLMSLKGD 1086
Cdd:cd18780 261 LTSFL--LYTLTVAMSFAF-LSSLYGD 284
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1292-1384 |
4.14e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1292 EFIE--SLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIA 1369
Cdd:PRK13409 436 EIIKplQLERLLDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVD 511
|
90
....*....|....*.
gi 124506379 1370 HRIASIKR-SDKIVVF 1384
Cdd:PRK13409 512 HDIYMIDYiSDRLMVF 527
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1263-1343 |
4.27e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.24 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1263 MSIYENIKFG---REDATLEDVKRVSKFAAI---DEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLD 1336
Cdd:PRK11650 91 MSVRENMAYGlkiRGMPKAEIEERVAEAARIlelEPLLDRKPRE-----------LSGGQRQRVAMGRAIVREPAVFLFD 159
|
....*..
gi 124506379 1337 EATSSLD 1343
Cdd:PRK11650 160 EPLSNLD 166
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1155-1394 |
4.32e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1155 KTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILKNDMTNFQDYQNnnnnslvlknvnefSNQSGsaedytvfnnngeill 1234
Cdd:PRK10762 31 RVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS--------------SQEAG---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1235 ddinicdynlrdlrnlFSIVSQEPMLF-NMSIYENIKFGREdatledvkRVSKFAAID---EFIES--------LPNKYD 1302
Cdd:PRK10762 81 ----------------IGIIHQELNLIpQLTIAENIFLGRE--------FVNRFGRIDwkkMYAEAdkllarlnLRFSSD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1303 TNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIeKTIVDIKDKaDKTIITIAHRIASI-KRSDK 1380
Cdd:PRK10762 137 KLVG----ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRELKSQ-GRGIVYISHRLKEIfEICDD 210
|
250
....*....|....
gi 124506379 1381 IVVFnnpdRNGTFV 1394
Cdd:PRK10762 211 VTVF----RDGQFI 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1228-1337 |
4.62e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 58.50 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1228 NNGEILLDDINICDYNLrDLRNLFSI--VSQEPMLF-NMSIYENIKfgredATLEdVKRVSKFAA-------IDEF-IES 1296
Cdd:COG1137 56 DSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASIFrKLTVEDNIL-----AVLE-LRKLSKKEReerleelLEEFgITH 128
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 124506379 1297 LPNKYdtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDE 1337
Cdd:COG1137 129 LRKSK-------AYSLSGGERRRVEIARALATNPKFILLDE 162
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1301-1392 |
5.09e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.57 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1301 YDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SD 1379
Cdd:COG1245 449 LDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYiSD 524
|
90
....*....|....
gi 124506379 1380 KIVVFN-NPDRNGT 1392
Cdd:COG1245 525 RLMVFEgEPGVHGH 538
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
398-635 |
5.54e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 398 DLSFTLKEGKTYAFVGESGCGKSTILKLIERLYdPT---EGDIIVNDSH-NLKDINLKwwrSKIGVV--SQD----PLLf 467
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVcRFKDIRDS---EALGIViiHQElaliPYL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 468 snSIknnikyslyslkdleaMENYYEENtndtyENKNFSLISNSMTSNELLEMKKeyqtikdsdvvdvskKVlihdfvsS 547
Cdd:NF040905 94 --SI----------------AENIFLGN-----ERAKRGVIDWNETNRRARELLA---------------KV-------G 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 548 LPDKYDTLVgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSL-DNKSEYLVQkTINNLKgnENRIT-IIIAHRLST 625
Cdd:NF040905 129 LDESPDTLV----TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD-LLLELK--AQGITsIIISHKLNE 201
|
250
....*....|.
gi 124506379 626 IRY-ANTIFVL 635
Cdd:NF040905 202 IRRvADSITVL 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1139-1372 |
5.74e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.56 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1139 PNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmTNFQDYQNNnnnSLVLKNVnefSNQSG 1218
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLI-----------------AGFVPYQHG---SITLDGK---PVEGP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1219 SAEDYTVFNNNGeiLLDDINICDynlrdlrnlfsivsqepmlfnmsiyeNIKFG----------REDATLEDVKRVSKFA 1288
Cdd:PRK11248 69 GAERGVVFQNEG--LLPWRNVQD--------------------------NVAFGlqlagvekmqRLEIAHQMLKKVGLEG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1289 AIDEFIESLpnkydtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1368
Cdd:PRK11248 121 AEKRYIWQL---------------SGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLI 185
|
....
gi 124506379 1369 AHRI 1372
Cdd:PRK11248 186 THDI 189
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
398-635 |
6.21e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 398 DLSFTLKEGKTYAFVGESGCGKSTILKLIERLYdPT---EGDIIVNDS----HNLKDINlkwwRSKIGVVSQDPLLfsns 470
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEelqaSNIRDTE----RAGIAIIHQELAL---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 471 iknnikyslysLKDLEAMENYYEENtndtyENKNFSLIS-NSMTsnelLEMKKEYQTIKDSdvVDVSKKVlihdfvsslp 549
Cdd:PRK13549 94 -----------VKELSVLENIFLGN-----EITPGGIMDyDAMY----LRAQKLLAQLKLD--INPATPV---------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 550 dkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTI-RY 628
Cdd:PRK13549 142 -----------GNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVkAI 209
|
....*..
gi 124506379 629 ANTIFVL 635
Cdd:PRK13549 210 SDTICVI 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
394-597 |
6.34e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.33 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 394 EIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLydptegdiivnDshnlKDINLKWWRS---KIGVVSQDPLLFSN- 469
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------D----KDFNGEARPQpgiKVGYLPQEPQLDPTk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 470 SIKNNIKYSLYSLKDleAMENYYEENTNDTYENKNFslisnsmtsNELLEMKKEYQTIKDS-DVVDVSKKVLIHDFVSSL 548
Cdd:TIGR03719 84 TVRENVEEGVAEIKD--ALDRFNEISAKYAEPDADF---------DKLAAEQAELQEIIDAaDAWDLDSQLEIAMDALRC 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 124506379 549 PDKyDTLVgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKS 597
Cdd:TIGR03719 153 PPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
392-637 |
6.45e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.54 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 392 DVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLI---ERlYDPTEGDIIVnDSHNLKDINLKWwRSKIGVVsqdpLLFS 468
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghPK-YEVTEGEILF-KGEDITDLPPEE-RARLGIF----LAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 469 NSIknnikyslyslkdleamenyyeentndtyenknfslisnsmtsnellemkkEYQTIKdsdvvdvskkvlIHDFVSSL 548
Cdd:cd03217 85 YPP---------------------------------------------------EIPGVK------------NADFLRYV 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 549 PDKydtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIRY 628
Cdd:cd03217 102 NEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLR-EEGKSVLIITHYQRLLDY 169
|
250
....*....|.
gi 124506379 629 --ANTIFVLSN 637
Cdd:cd03217 170 ikPDRVHVLYD 180
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
379-618 |
6.91e-09 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 57.92 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 379 EFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDINlKW---WRS 455
Cdd:TIGR03410 2 EVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDG----EDIT-KLpphERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 456 K--IGVVSQDPLLFSnsiknnikyslyslkdleamenyyeentndtyenknfslisnSMTSNELLEMKKEYQTIKDSDVV 533
Cdd:TIGR03410 74 RagIAYVPQGREIFP------------------------------------------RLTVEENLLTGLAALPRRSRKIP 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 534 DvskkvLIHDFVSSLPDkydtLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNEN 613
Cdd:TIGR03410 112 D-----EIYELFPVLKE----MLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLR-AEG 181
|
....*
gi 124506379 614 RITII 618
Cdd:TIGR03410 182 GMAIL 186
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
374-621 |
7.06e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 374 NIKKIEFKNVrfhYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLI--ERLYDPTEGDIIVNDShNLKDINLK 451
Cdd:CHL00131 4 NKPILEIKNL---HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGE-SILDLEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 452 WwRSKIGVVsqdpLLFSNSIK----NNIKYslyslkdleamenyyeentndtyenknFSLISNSmtsnellemKKEYQTI 527
Cdd:CHL00131 80 E-RAHLGIF----LAFQYPIEipgvSNADF---------------------------LRLAYNS---------KRKFQGL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 528 KDSDVVDvskkvlihdFVSSLPDKYDtLVGSNASKL--------SGGQKQRISIARAIMRNPKILILDEATSSLDNKSEY 599
Cdd:CHL00131 119 PELDPLE---------FLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALK 188
|
250 260
....*....|....*....|..
gi 124506379 600 LVQKTINNLKGNENRItIIIAH 621
Cdd:CHL00131 189 IIAEGINKLMTSENSI-ILITH 209
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
378-637 |
7.44e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.66 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYdtRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDiNLKWWRSKI 457
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKE-NIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDP--LLFSNSIKNNIKYSLYSLK-DLEAMENYYEEntndtyenknfslisnsmtsnellemkkeyqtikdsdvvd 534
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPINLGlDEETVAHRVSS---------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 535 VSKKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 614
Cdd:PRK13652 121 ALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGM 189
|
250 260
....*....|....*....|....
gi 124506379 615 ITIIIAHRLSTI-RYANTIFVLSN 637
Cdd:PRK13652 190 TVIFSTHQLDLVpEMADYIYVMDK 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1253-1406 |
7.70e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1253 IVSQEPMLF-NMSIYENIKFG--REDATLEDVKrvskfAAIDEFIESLpnKYDTNVGpygkSLSGGQKQRIAIARALLRE 1329
Cdd:PRK15439 90 LVPQEPLLFpNLSVKENILFGlpKRQASMQKMK-----QLLAALGCQL--DLDSSAG----SLEVADRQIVEILRGLMRD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1330 PKILLLDEATSSLD-SNSEKLIEKtIVDIKDKaDKTIITIAHRIASIKR-SDKIVVFnnpdRNGTFVQSHGT----HDEL 1403
Cdd:PRK15439 159 SRILILDEPTASLTpAETERLFSR-IRELLAQ-GVGIVFISHKLPEIRQlADRISVM----RDGTIALSGKTadlsTDDI 232
|
...
gi 124506379 1404 LSA 1406
Cdd:PRK15439 233 IQA 235
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
797-1078 |
7.84e-09 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 58.65 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 797 LVAGGLYPVFALLYARYVSTLFDFANLEYNSNKYSIyILLIAIAMFISETL----KNYYNNKIGEKVEKTMKRRLFENIL 872
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQ-IALLLLGLFLLQAVfsffRIYLFARVGERVVADLRKDLYRHLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 873 YQEMSFFDQdkNTPGVLSAHINRDVHLLKTGLVNNIVIF-SHFIMLfLVSMVMSFYFCP----IVAAVLTFIYFInMRVF 947
Cdd:cd18576 81 RLPLSFFHE--RRVGELTSRLSNDVTQIQDTLTTTLAEFlRQILTL-IGGVVLLFFISWkltlLMLATVPVVVLV-AVLF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 948 AVRARlTKSKEIEKKENMSSGVfafssddemfkdpsflIQEAFYNMHTVINYGLEDY----FCNLIEKAIDYknkgQKRR 1023
Cdd:cd18576 157 GRRIR-KLSKKVQDELAEANTI----------------VEETLQGIRVVKAFTREDYeierYRKALERVVKL----ALKR 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 1024 IIVNAALWGFSQSAqLFINSFA-YWFGSFLIKRGTILVDD---FMksLFTFIFTGSYAG 1078
Cdd:cd18576 216 ARIRALFSSFIIFL-LFGAIVAvLWYGGRLVLAGELTAGDlvaFL--LYTLFIAGSIGS 271
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1146-1406 |
8.30e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 8.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1146 NLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFydLKNDHIILKNDMTNFqdyqnnnnnslvlknvnefsnqsgsaedytv 1225
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRL--LPSPPVVYPSGDIRF------------------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1226 fnnNGEILLddiNICDYNLRDLR-NLFSIVSQEPM-----LFNM--SIYENIKFGREdatledvkrVSKFAAIDEFIESL 1297
Cdd:PRK15134 74 ---HGESLL---HASEQTLRGVRgNKIAMIFQEPMvslnpLHTLekQLYEVLSLHRG---------MRREAARGEILNCL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1298 P----NKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA 1373
Cdd:PRK15134 139 DrvgiRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLS 218
|
250 260 270
....*....|....*....|....*....|....
gi 124506379 1374 SIKR-SDKIVVFnnpdRNGTFVQsHGTHDELLSA 1406
Cdd:PRK15134 219 IVRKlADRVAVM----QNGRCVE-QNRAATLFSA 247
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
395-637 |
1.01e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 57.72 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 395 IYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDInlkwwrskigvvsqdpllfsnsiknn 474
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD----KPI-------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 475 ikySLYSLKDLeamenyyeentndtyeNKNFSLISNSMTSNELLEMKK--EYQ-----------TIKDSDVVDVSKKVLi 541
Cdd:PRK11231 67 ---SMLSSRQL----------------ARRLALLPQHHLTPEGITVRElvAYGrspwlslwgrlSAEDNARVNQAMEQT- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 542 hdfvsslpdKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAH 621
Cdd:PRK11231 127 ---------RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLH 196
|
250
....*....|....*..
gi 124506379 622 RLS-TIRYANTIFVLSN 637
Cdd:PRK11231 197 DLNqASRYCDHLVVLAN 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
378-621 |
1.15e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.74 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDT-RKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEG-------DIIVNDSHNLKDIN 449
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyrvagqDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 450 lkwwRSKIGVVSQdpllfsnsiknniKYSLysLKDLEAMENYYEENTNDTYENKNFSLISNSMTSNELLEMKKEYQtikd 529
Cdd:PRK10535 85 ----REHFGFIFQ-------------RYHL--LSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQ---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 530 sdvvdvskkvlihdfvsslpdkydtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLK 609
Cdd:PRK10535 142 ------------------------------PSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR 191
|
250
....*....|..
gi 124506379 610 gNENRITIIIAH 621
Cdd:PRK10535 192 -DRGHTVIIVTH 202
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1312-1386 |
1.16e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 55.15 E-value: 1.16e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 1312 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdkadKTIITIAHRIASIKR-SDKIVVFNN 1386
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP----GTVILVSHDRYFLDQvATKIIELED 142
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
389-605 |
1.18e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.81 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 389 TRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDINLKWWRSKIGVVSQdpllfS 468
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG----GDIDDPDVAEACHYLGH-----R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 469 NSIKNNikyslyslkdLEAMENyyeentndtyenknfslisnsmtsnelLEMKKEYQTIKDSDVVDVSKKVLIHDfVSSL 548
Cdd:PRK13539 82 NAMKPA----------LTVAEN---------------------------LEFWAAFLGGEELDIAAALEAVGLAP-LAHL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 549 PDKYdtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTI 605
Cdd:PRK13539 124 PFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1282-1388 |
1.21e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.46 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1282 KRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD----- 1356
Cdd:smart00382 31 GGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllll 110
|
90 100 110
....*....|....*....|....*....|....*...
gi 124506379 1357 IKDKADKTIITIAHRIASIK------RSDKIVVFNNPD 1388
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGpallrrRFDRRIVLLLIL 148
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1157-1348 |
1.22e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.83 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1157 TAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnNSLVLKNVnefsnqsgsaedytvfnnnGEILLDD 1236
Cdd:PRK13649 36 TAFIGHTGSGKSTIMQLL----------------------------NGLHVPTQ-------------------GSVRVDD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1237 INIC----DYNLRDLRNLFSIVSQ--EPMLFNMSIYENIKFGRED--ATLEDVKRVSK----FAAIDEfieslpNKYDTN 1304
Cdd:PRK13649 69 TLITstskNKDIKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAReklaLVGISE------SLFEKN 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 124506379 1305 vgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1348
Cdd:PRK13649 143 --PF--ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1308-1408 |
1.23e-08 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 57.89 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1308 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNn 1386
Cdd:TIGR02769 147 LPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMD- 225
|
90 100
....*....|....*....|..
gi 124506379 1387 pdrNGTFVQSHGTHDELLSAQD 1408
Cdd:TIGR02769 226 ---KGQIVEECDVAQLLSFKHP 244
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1158-1415 |
1.24e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1158 AIVGETGSGKSTFMNlllrfydlkndhiilkndmtnfqdyqnnnnnslVLKNVNEFsnqsGSAEdytvfnnnGEILLDDi 1237
Cdd:NF040905 31 ALCGENGAGKSTLMK---------------------------------VLSGVYPH----GSYE--------GEILFDG- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1238 NICDYnlRDLRNlfS------IVSQE----PMLfnmSIYENIKFGRE---------DATLEDVKRVSKFAAIDEfiesLP 1298
Cdd:NF040905 65 EVCRF--KDIRD--SealgivIIHQElaliPYL---SIAENIFLGNErakrgvidwNETNRRARELLAKVGLDE----SP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1299 nkyDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIEkTIVDIKDKADKTIItIAHRIASIKR 1377
Cdd:NF040905 134 ---DTLV----TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD-LLLELKAQGITSII-ISHKLNEIRR 204
|
250 260 270
....*....|....*....|....*....|....*....
gi 124506379 1378 -SDKIVVFnnpdRNGTFVQSHGTHDELLSaQDGIYKKYV 1415
Cdd:NF040905 205 vADSITVL----RDGRTIETLDCRADEVT-EDRIIRGMV 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
394-624 |
1.31e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.29 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 394 EIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIErLYDPT----EGDIIVNDshnlKDINLKWWRSKIGVVSQDPLLFSn 469
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNG----MPIDAKEMRAISAYVQQDDLFIP- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 470 siknnikyslyslkdleamenyyeenTNDTYENKNFSlisnSMtsnelLEMKKEYQTIKDSDVVDVskkvLIHDFvsSLP 549
Cdd:TIGR00955 113 --------------------------TLTVREHLMFQ----AH-----LRMPRRVTKKEKRERVDE----VLQAL--GLR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 550 DKYDTLVGSNASK--LSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLS 624
Cdd:TIGR00955 152 KCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQPS 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1311-1343 |
1.33e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.77 E-value: 1.33e-08
10 20 30
....*....|....*....|....*....|...
gi 124506379 1311 SLSGGQKQRIAIARALLREPKILLLDEATSSLD 1343
Cdd:PRK10419 151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1137-1396 |
1.55e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1137 SRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILKNDMTNFQDYQnnnnnslvlknvneFSNQ 1216
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK--------------LAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1217 SGsaedytvfnnngeillddinicdynlrdlrnlFSIVSQEPMLFN-MSIYENIKFGRE------DATLEDVKRVSKFAA 1289
Cdd:PRK09700 80 LG--------------------------------IGIIYQELSVIDeLTVLENLYIGRHltkkvcGVNIIDWREMRVRAA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1290 IDEFIESLPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIekTIVDIKDKADKTIITI 1368
Cdd:PRK09700 128 MMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLF--LIMNQLRKEGTAIVYI 201
|
250 260
....*....|....*....|....*....
gi 124506379 1369 AHRIASIKR-SDKIVVFnnpdRNGTFVQS 1396
Cdd:PRK09700 202 SHKLAEIRRiCDRYTVM----KDGSSVCS 226
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
792-1081 |
1.63e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 57.83 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 792 IFFSILVAgglypVFALLYARYVSTLFDFANLEYNSN---KYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLF 868
Cdd:cd18542 5 ILALLLAT-----ALNLLIPLLIRRIIDSVIGGGLREllwLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 869 ENILYQEMSFFdqDKNTPGVLSAHINRDV----HLLKTGL---VNNIVIFS-HFIMLFLVSMVMSFY---FCPIVaAVLT 937
Cdd:cd18542 80 DHLQRLSFSFH--DKARTGDLMSRCTSDVdtirRFLAFGLvelVRAVLLFIgALIIMFSINWKLTLIslaIIPFI-ALFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 938 FIYFINMR-VFavrarltksKEIEKKE-NMSSgvfafssddemfkdpsfLIQEAFYNMHTVINYGLEDY----FcnlIEK 1011
Cdd:cd18542 157 YVFFKKVRpAF---------EEIREQEgELNT-----------------VLQENLTGVRVVKAFAREDYeiekF---DKE 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1012 AIDYKNKgQKRRIIVNAALWGFSQSAQLFINSFAYWFGSFLIKRGTILVDDfmksLFTFIftgSYAGKLM 1081
Cdd:cd18542 208 NEEYRDL-NIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGE----LVAFI---SYLWMLI 269
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1311-1344 |
1.75e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.99 E-value: 1.75e-08
10 20 30
....*....|....*....|....*....|....
gi 124506379 1311 SLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1344
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
57-351 |
1.80e-08 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 57.44 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 57 LFISFVCAVLSGGT---LPFFIsvfGVILKNMNLGDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYLR 133
Cdd:cd18551 1 LILALLLSLLGTAAslaQPLLV---KNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 134 SVFYQDGQFHDNN-PG---SKLRSDldfyLEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVCG 209
Cdd:cd18551 78 RLLRLPVSFFDRRrSGdlvSRVTND----TTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 210 VICNKKVklnKKTSLLYNNNT---MSIIEEALMGIRTVASYCGEKTILNKFN--LSETFysKYILKANFVEALHIGLING 284
Cdd:cd18551 154 LPLGRRI---RKASKRAQDALgelSAALERALSAIRTVKASNAEERETKRGGeaAERLY--RAGLKAAKIEALIGPLMGL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 285 LILVSYAFGFWYGT-RIIINSATnqypnndfngasvisilLGVLIS--MFMLTIILP------NITEYMKALEATN 351
Cdd:cd18551 229 AVQLALLVVLGVGGaRVASGALT-----------------VGTLVAflLYLFQLITPlsqlssFFTQLQKALGALE 287
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1138-1354 |
1.96e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.04 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1138 RPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRfydlkndhIIlkndmtnfqdyqnnnnnSLVLKNVNefsnqs 1217
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTT----LLR--------LI-----------------AGLLPPAA------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1218 gsaedytvfnnnGEILLDDINICDYNLRDL------RNlfsivsqePMLFNMSIYENIKF-----GREDATLEdvkrvsk 1286
Cdd:PRK13539 57 ------------GTIKLDGGDIDDPDVAEAchylghRN--------AMKPALTVAENLEFwaaflGGEELDIA------- 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 1287 fAAIDEF----IESLPNKYdtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1354
Cdd:PRK13539 110 -AALEAVglapLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1145-1385 |
2.11e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1145 KNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILkndmtnfqdyqnnnnnslvlknvnefsnqsgsaedyt 1224
Cdd:PRK10261 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIF------------------------------------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1225 vfnnNGEiLLDdiNICDYNLRDLRNLFSIVSQEP-------MLFNMSIYENIkfgREDATLEDVKRVSKFAAIDEFIESL 1297
Cdd:PRK10261 384 ----NGQ-RID--TLSPGKLQALRRDIQFIFQDPyasldprQTVGDSIMEPL---RVHGLLPGKAAAARVAWLLERVGLL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1298 PNkydtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR 1377
Cdd:PRK10261 454 PE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVER 529
|
....*....
gi 124506379 1378 -SDKIVVFN 1385
Cdd:PRK10261 530 iSHRVAVMY 538
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
396-590 |
2.13e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.49 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 396 YKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDINLK----WWRSKIGVVSQD----PLLF 467
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG----KPVRIRsprdAIRAGIAYVPEDrkgeGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 468 SNSIKNNIkySLYSLKDLeamenyyeentndtyenKNFSLISNsmtsnellemKKEYQTIKDsdvvdvskkvLIHDF--- 544
Cdd:COG1129 344 DLSIRENI--TLASLDRL-----------------SRGGLLDR----------RRERALAEE----------YIKRLrik 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 124506379 545 VSSLpdkyDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEAT 590
Cdd:COG1129 385 TPSP----EQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1108-1388 |
2.24e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.66 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1108 DVRDDGGIRINKNLIKgkvdIKDVNFRYIS--RPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLL--------RF 1177
Cdd:TIGR03269 266 EVEKECEVEVGEPIIK----VRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAgvleptsgEV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1178 YDLKNDHIIlknDMTNfqdyqnnnnnslvlKNVNEfsnqSGSAEDYtvfnnngeillddinicdynlrdlrnlFSIVSQE 1257
Cdd:TIGR03269 342 NVRVGDEWV---DMTK--------------PGPDG----RGRAKRY---------------------------IGILHQE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1258 PMLF-NMSIYENIKfgrEDATLEDVKRVSKFAAI---------DEFIESLPNKYDTnvgpygkSLSGGQKQRIAIARALL 1327
Cdd:TIGR03269 374 YDLYpHRTVLDNLT---EAIGLELPDELARMKAVitlkmvgfdEEKAEEILDKYPD-------ELSEGERHRVALAQVLI 443
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1328 REPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI---------ASIKRSDKIVVFNNPD 1388
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMdfvldvcdrAALMRDGKIVKIGDPE 513
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
378-594 |
2.39e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 56.79 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYD-TRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDShnlkdinlkwwrsK 456
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-------------P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 I-------GVVSQ-DPLLFSNSIKNNIKYSLySLKDLEAMENYYEentndtyenknfslisnsmtSNELLemkkeyqtik 528
Cdd:COG4525 71 VtgpgadrGVVFQkDALLPWLNVLDNVAFGL-RLRGVPKAERRAR--------------------AEELL---------- 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 529 dsdvvdvsKKVLIHDFVsslpdkydtlvGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:COG4525 120 --------ALVGLADFA-----------RRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
829-1072 |
2.45e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 57.17 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 829 KYSIYILLIAIAMF-ISETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFDQdkNTPGVLSAHINRDVHLLKTGLVNN 907
Cdd:cd18572 36 YRAVLLLLLLSVLSgLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDA--TKTGELTSRLTSDCQKVSDPLSTN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 908 IVIFSHFIMLFLVSMVMSFYfcpiVAAVLTFIYFINMRVFAVrarLTK-----SKEIEKKENmssgvfafssddEMFKDP 982
Cdd:cd18572 114 LNVFLRNLVQLVGGLAFMFS----LSWRLTLLAFITVPVIAL---ITKvygryYRKLSKEIQ------------DALAEA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 983 SFLIQEAFYNMHTVINYGLEDYFCNLIEKAID-YKNKGqKRRIIVNAALWGFSQSAQLFINSFAYWFGSFLIKRGTILVD 1061
Cdd:cd18572 175 NQVAEEALSNIRTVRSFATEEREARRYERALDkALKLS-VRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAG 253
|
250
....*....|.
gi 124506379 1062 dfmkSLFTFIF 1072
Cdd:cd18572 254 ----QLVTFML 260
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
369-468 |
2.47e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.44 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 369 GETLPNIKKIEFKNVRFHYDTRK-DVeiyKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKD 447
Cdd:PRK10522 314 PQAFPDWQTLELRNVTFAYQDNGfSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGKPVTA 389
|
90 100
....*....|....*....|.
gi 124506379 448 INLKWWRSKIGVVSQDPLLFS 468
Cdd:PRK10522 390 EQPEDYRKLFSAVFTDFHLFD 410
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
789-1058 |
2.91e-08 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 57.07 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 789 VTIIFFSILVAgglypVFALLYARYVSTLFDF---ANLEYNSNKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKR 865
Cdd:cd18570 5 ILILLLSLLIT-----LLGIAGSFFFQILIDDiipSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 866 RLFENILYQEMSFFDQdKNTPGVLSahINRDVHLLKTGLVNNIV-IFSHFIMLFLVSMVMSFY------FCPIVAAVLTF 938
Cdd:cd18570 80 GYFKHLLKLPLSFFET-RKTGEIIS--RFNDANKIREAISSTTIsLFLDLLMVIISGIILFFYnwklflITLLIIPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 939 IYFINMRVFAVRARltksKEIEKKENMSsgvfafssddemfkdpSFLIqEAFYNMHTVINYGLEDYFCNLIEKA-IDYKN 1017
Cdd:cd18570 157 IILLFNKPFKKKNR----EVMESNAELN----------------SYLI-ESLKGIETIKSLNAEEQFLKKIEKKfSKLLK 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 124506379 1018 KGQKRRIIVNAALwGFSQSAQLFINSFAYWFGSFLIKRGTI 1058
Cdd:cd18570 216 KSFKLGKLSNLQS-SIKGLISLIGSLLILWIGSYLVIKGQL 255
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1126-1408 |
3.71e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.31 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFryiSRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTfmnlLLRFY--DLKNDHiilkndmtnfqdyqnnnnn 1203
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIggQIAPDH------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1204 slvlknvnefsnqsgsaedytvfnnnGEILLDDINI---CDYNLRDLRNLFSIVSQEPMLF-NMSIYENIKFG-REDATL 1278
Cdd:PRK11831 62 --------------------------GEILFDGENIpamSRSRLYTVRKRMSMLFQSGALFtDMNVFDNVAYPlREHTQL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1279 -EDVKRVSKFAAidefIESLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1357
Cdd:PRK11831 116 pAPLLHSTVMMK----LEAVGLRGAAKLMP--SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISEL 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 124506379 1358 KDKADKTIITIAH---RIASIKRSDKIVVfnnpdrnGTFVQSHGTHDELLSAQD 1408
Cdd:PRK11831 190 NSALGVTCVVVSHdvpEVLSIADHAYIVA-------DKKIVAHGSAQALQANPD 236
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
385-639 |
3.84e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.17 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 385 FHYdtrKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII-VNDSHNLKDINLKWWRSKIGVVSQD 463
Cdd:PRK13638 9 FRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwQGKPLDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 464 P--LLFSNSIKNNIKYSLYSLKDLEAmenyyeentndtyenknfslisnsmtsnellemkkeyqtikdsdvvDVSKKVli 541
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNLGVPEA----------------------------------------------EITRRV-- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 542 hdfvsslpDKYDTLVGSNASK------LSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 615
Cdd:PRK13638 118 --------DEALTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHV 189
|
250 260
....*....|....*....|....*
gi 124506379 616 tIIIAHRLSTI-RYANTIFVLSNRE 639
Cdd:PRK13638 190 -IISSHDIDLIyEISDAVYVLRQGQ 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1141-1390 |
4.37e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.81 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1141 VPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtNFQDYQNNNNNSLVLKNVNEFSNQSGSA 1220
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL------------------GCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1221 edytvfnnngeillddinicdynLRdlRNLFSIVSQE-PMLFNMSIYENIKFGREDATLEDVKRVSKFAAI------DEF 1293
Cdd:PRK10535 83 -----------------------LR--REHFGFIFQRyHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELlqrlglEDR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1294 IESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI----- 1368
Cdd:PRK10535 138 VEYQPSQ-----------LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVThdpqv 206
|
250 260
....*....|....*....|....*
gi 124506379 1369 ---AHRIASIKrsDKIVVFNNPDRN 1390
Cdd:PRK10535 207 aaqAERVIEIR--DGEIVRNPPAQE 229
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
792-1058 |
4.45e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 56.36 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 792 IFFSILVAGGLYPVFALLYARYVSTLFDFANLEYNSNKYSIYILLIAIAM---FISETLKNYYNNKIGEKVEKTMKRRLF 868
Cdd:cd18555 3 LLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFllyGLFSFLRGYIIIKLQTKLDKSLMSDFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 869 ENILYQEMSFFDQdkNTPGVLSAHINRDVHL-------LKTGLVNNIVIFSHFIMLFLVSMVMSFYFCpIVAAVLTFIYF 941
Cdd:cd18555 83 EHLLKLPYSFFEN--RSSGDLLFRANSNVYIrqilsnqVISLIIDLLLLVIYLIYMLYYSPLLTLIVL-LLGLLIVLLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 942 INMRvfavrarltKSKEIEKKENMSSGvfafssddemfKDPSFLIqEAFYNMHTVINYGLEDYFC----NLIEKAIDYkn 1017
Cdd:cd18555 160 LTRK---------KIKKLNQEEIVAQT-----------KVQSYLT-ETLYGIETIKSLGSEKNIYkkweNLFKKQLKA-- 216
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 124506379 1018 kgQKRRIIVNAALWGFSQSAQLFINSFAYWFGSFLIKRGTI 1058
Cdd:cd18555 217 --FKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGEL 255
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
381-608 |
4.76e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.84 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 381 KNVRFHYDTRkdvEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNdSHNLKDInlkwwRSKIGVV 460
Cdd:PRK11247 16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-TAPLAEA-----REDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 461 SQDP-LLFSNSIKNNIKYSL---YSLKDLEAMEnyyeentndtyenknfslisnsmtsnellemkkeyqtikdsdvvdvs 536
Cdd:PRK11247 87 FQDArLLPWKKVIDNVGLGLkgqWRDAALQALA----------------------------------------------- 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 537 kKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNL 608
Cdd:PRK11247 120 -AVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESL 179
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
395-635 |
5.64e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.76 E-value: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 395 IYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVnDSHNLKDINLKWWRSKIGVVSQDPllfsnSIKNN 474
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL-DGEHIQHYASKEVARRIGLLAQNA-----TTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 475 IkyslySLKDLEAMENYYEENTNDTYENKNFSLISNSMTSNELLEmkkeyqtikdsdvvdvskkvlihdfvsslpdkydt 554
Cdd:PRK10253 96 I-----TVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITH----------------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 555 LVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIF 633
Cdd:PRK10253 136 LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNqACRYASHLI 215
|
..
gi 124506379 634 VL 635
Cdd:PRK10253 216 AL 217
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
838-1078 |
7.29e-08 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 55.60 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 838 AIAMFisetLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFdqDKNTPGVLsahINR---DVHLLKTGLVNNIVIFSH- 913
Cdd:cd18573 55 AAANF----GRVYLLRIAGERIVARLRKRLFKSILRQDAAFF--DKNKTGEL---VSRlssDTSVVGKSLTQNLSDGLRs 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 914 -------FIMLFLVSMVMSFYFCPIVAAVLTFIYF-------INMRVFAVRARLTKSKEiekkenmssgvfafssddemf 979
Cdd:cd18573 126 lvsgvggIGMMLYISPKLTLVMLLVVPPIAVGAVFygryvrkLSKQVQDALADATKVAE--------------------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 980 kdpsfliqEAFYNMHTVINYGLEDYFCNLIEKAIDYKNKGQKRRIIVNAALWGfsqSAQLFINSFAY---WFGSFLIKRG 1056
Cdd:cd18573 185 --------ERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFG---STGFSGNLSLLsvlYYGGSLVASG 253
|
250 260
....*....|....*....|..
gi 124506379 1057 TILVDDfmksLFTFIFTGSYAG 1078
Cdd:cd18573 254 ELTVGD----LTSFLMYAVYVG 271
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
789-947 |
7.96e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 55.59 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 789 VTIIFFSILVAGGLYpVFALLYARYVSTLFDFANLEYNSNKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLF 868
Cdd:cd18580 1 VLLLLLLLLLLAFLS-QFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 869 ENILYQEMSFFdqDKNTPGVLsahINR---DVHLLKTGLVNNIVIFSHFIMLFLVSMVMSFYFCP---IVAAVLTFIYFI 942
Cdd:cd18580 80 RSVLRAPMSFF--DTTPSGRI---LNRfskDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPyflIVLPPLLVVYYL 154
|
....*
gi 124506379 943 NMRVF 947
Cdd:cd18580 155 LQRYY 159
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
855-1064 |
8.02e-08 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 55.63 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 855 IGEKVEKTMKRRLFENILYQEMSFFDQdkNTPGVLSAHINRDVHLLKT--------GLVNNIVIFSHFIMLFLVSMVMSF 926
Cdd:cd18574 69 VGERVAARLRNDLFSSLLRQDIAFFDT--HRTGELVNRLTADVQEFKSsfkqcvsqGLRSVTQTVGCVVSLYLISPKLTL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 927 YF---CPIVAAVLTFIyfinmrvfavrARLTK--SKEIEKKENMSSGVfafssddemfkdpsflIQEAFYNMHTVINYGL 1001
Cdd:cd18574 147 LLlviVPVVVLVGTLY-----------GSFLRklSRRAQAQVAKATGV----------------ADEALGNIRTVRAFAM 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 1002 EDYFCNLIEKAIDyknKGQKRRIIVNAALWGFSQSAQLFINSFA---YWFGSFLIKRGTILVDDFM 1064
Cdd:cd18574 200 EDRELELYEEEVE---KAAKLNEKLGLGIGIFQGLSNLALNGIVlgvLYYGGSLVSRGELTAGDLM 262
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1126-1370 |
8.07e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.51 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisRPNVPIYKNLSFTCDSK----KTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnn 1201
Cdd:PRK13643 2 IKFEKVNYTY--QPNSPFASRALFDIDLEvkkgSYTALIGHTGSGKSTLLQHL--------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1202 nNSLVLKNvnefsnqsgsaedytvfnnNGEILLDDINICDYN----LRDLRNLFSIVSQEP--MLFNMSIYENIKFG--- 1272
Cdd:PRK13643 53 -NGLLQPT-------------------EGKVTVGDIVVSSTSkqkeIKPVRKKVGVVFQFPesQLFEETVLKDVAFGpqn 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1273 ----REDATLEDVKRVSKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1348
Cdd:PRK13643 113 fgipKEKAEKIAAEKLEMVGLADEFWEKSPFE-----------LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
250 260
....*....|....*....|..
gi 124506379 1349 LIEKTIVDIKdKADKTIITIAH 1370
Cdd:PRK13643 182 EMMQLFESIH-QSGQTVVLVTH 202
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
57-303 |
8.25e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 55.55 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 57 LFISFVCAVLSGGT---LPFFISV---FGVILKNMNLgddINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLE 130
Cdd:cd18545 2 LLLALLLMLLSTAAslaGPYLIKIaidEYIPNGDLSG---LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 131 YLRSVFYQDGQFHDNNP-G---SKLRSDLDFYLEQVSSGIgtkfITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIY 206
Cdd:cd18545 79 LFSHLQKLSFSFFDSRPvGkilSRVINDVNSLSDLLSNGL----INLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 207 VCGVICNKKV-----KLNKKTSLLYnnntmSIIEEALMGIRTVASYCGEKTILNKF-NLSETFYSKYiLKANFVEALH-- 278
Cdd:cd18545 155 LVVFLLRRRArkawqRVRKKISNLN-----AYLHESISGIRVIQSFAREDENEEIFdELNRENRKAN-MRAVRLNALFwp 228
|
250 260
....*....|....*....|....*.
gi 124506379 279 -IGLINGLilvSYAFGFWYGTRIIIN 303
Cdd:cd18545 229 lVELISAL---GTALVYWYGGKLVLG 251
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
322-608 |
1.32e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 322 ILLGVLISMFMLTIILpniTEYMKALEA--------TNSLYEIINRKPLVENN-DDGETLPNIKKI----EFKNVRFHYD 388
Cdd:TIGR00956 674 IIIGFTVFFFFVYILL---TEFNKGAKQkgeilvfrRGSLKRAKKAGETSASNkNDIEAGEVLGSTdltdESDDVNDEKD 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 389 TRKDVE----IYKDLSFTL-----------------KEGKTYAFVGESGCGKSTILK-LIERLYDP--TEGDIIVNDshn 444
Cdd:TIGR00956 751 MEKESGedifHWRNLTYEVkikkekrvilnnvdgwvKPGTLTALMGASGAGKTTLLNvLAERVTTGviTGGDRLVNG--- 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 445 lKDINLKWWRSkIGVVSQDPL-LFSNSIKNNIKYSLY-----SLKDLEAMEnYYEEntndtyenknfsLIsnsmtsnELL 518
Cdd:TIGR00956 828 -RPLDSSFQRS-IGYVQQQDLhLPTSTVRESLRFSAYlrqpkSVSKSEKME-YVEE------------VI-------KLL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 519 EMKkEYQtikdsdvvdvskkvlihdfvsslpdkyDTLVGSNASKLSGGQKQRISIARAIMRNPKILI-LDEATSSLDNKS 597
Cdd:TIGR00956 886 EME-SYA---------------------------DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
330
....*....|.
gi 124506379 598 EYLVQKTINNL 608
Cdd:TIGR00956 938 AWSICKLMRKL 948
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1288-1383 |
1.38e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.22 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1288 AAIDEFIE--SLPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTI 1365
Cdd:PRK13536 151 AVIPSLLEfaRLESKADARVS----DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARG-KTI 225
|
90
....*....|....*....
gi 124506379 1366 ITIAHRIASIKR-SDKIVV 1383
Cdd:PRK13536 226 LLTTHFMEEAERlCDRLCV 244
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
552-632 |
1.80e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.71 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 552 YDTLvGSNASKLSGGQKQRISIARAIMRNPK--ILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTIRYA 629
Cdd:cd03238 78 YLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTV-ILIEHNLDVLSSA 155
|
...
gi 124506379 630 NTI 632
Cdd:cd03238 156 DWI 158
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
403-597 |
1.86e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.63 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 403 LKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIV--NDSHNLKDINLKWWRSK-IGVVSQDPLLFSnsiknnikySL 479
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgQPLHQMDEEARAKLRAKhVGFVFQSFMLIP---------TL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 480 YSLKDLEAMENYYEENTNDTYENknfslisnsmtSNELLEMkkeyqtikdsdvVDVSKKvLIHdfvssLPdkydtlvgsn 559
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNG-----------AKALLEQ------------LGLGKR-LDH-----LP---------- 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 124506379 560 aSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKS 597
Cdd:PRK10584 145 -AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
392-635 |
2.16e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.22 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 392 DVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLY--DPTEGDIIVNDS----HNLKDINlkwwRSKIGVVSQDPL 465
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSplkaSNIRDTE----RAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 466 LfsnsiknnikyslysLKDLEAMENYYEENtndtyenkNFSLISNSMTSNELLEMKKEYQTIKDSDVVDVSKKVlihdfv 545
Cdd:TIGR02633 89 L---------------VPELSVAENIFLGN--------EITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPV------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 546 sslpdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNeNRITIIIAHRLST 625
Cdd:TIGR02633 140 ---------------GDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNE 203
|
250
....*....|.
gi 124506379 626 IR-YANTIFVL 635
Cdd:TIGR02633 204 VKaVCDTICVI 214
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1263-1406 |
2.27e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1263 MSIYENI------KFGREDATLedvKRVSKFAAIDEFIESLPNKYDTNVGPYGKsLSGGQKQRIAIARALLREPKILLLD 1336
Cdd:PRK10762 345 MSVKENMsltalrYFSRAGGSL---KHADEQQAVSDFIRLFNIKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILD 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124506379 1337 EATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASI-KRSDKIVVFNNPDRNGTFVQSHGTHDELLSA 1406
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFK-AEGLSIILVSSEMPEVlGMSDRILVMHEGRISGEFTREQATQEKLMAA 490
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
829-952 |
2.30e-07 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 54.32 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 829 KYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFDQdknTP-GVLSAHINRDVHLLKTGLVNN 907
Cdd:cd18544 42 LLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDR---TPvGRLVTRVTNDTEALNELFTSG 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 124506379 908 IV-IFSHFIMLFLVSMVMsFYFCP----IVAAVLTFIYFInMRVFAVRAR 952
Cdd:cd18544 119 LVtLIGDLLLLIGILIAM-FLLNWrlalISLLVLPLLLLA-TYLFRKKSR 166
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1312-1386 |
2.42e-07 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 52.43 E-value: 2.42e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 1312 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAHRIASIKR-SDKIVVFNN 1386
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGlCDRILVMYE 179
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
251-630 |
2.49e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.14 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 251 KTILNKF--NLSETFYSKYILKANfvealhiglinGLILVSYAFGFWYGTRIIINSatNQYPNNDF--NG------ASVI 320
Cdd:TIGR00954 317 LIIKFRFsyGFLDNIVAKYTWSAV-----------GLVAVSIPIFDKTHPAFLEMS--EEELMQEFynNGrlllkaADAL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 321 SILLGVLISMFMLTIILPNITEYMKALEATNSLYEiinRKPLVENNDDGET-------LPNIKKIEFKNVRFHYD----- 388
Cdd:TIGR00954 384 GRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNF---KRPRVEEIESGREggrnsnlVPGRGIVEYQDNGIKFEniplv 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 389 TRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYdPTEGDIIVNDShnlkdinlkwwRSKIGVVSQDPLLFS 468
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPA-----------KGKLFYVPQRPYMTL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 469 NSIKNNIKYSlyslkdleamenyyeentnDTYEnknfslisnsmtsnellEMKKeyQTIKDSDVVDVSKKVLIHDFV--- 545
Cdd:TIGR00954 529 GTLRDQIIYP-------------------DSSE-----------------DMKR--RGLSDKDLEQILDNVQLTHILere 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 546 ---SSLPDKYDTLvgsnasklSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEylvQKTINNLKgnENRITII-IAH 621
Cdd:TIGR00954 571 ggwSAVQDWMDVL--------SGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE---GYMYRLCR--EFGITLFsVSH 637
|
....*....
gi 124506379 622 RLSTIRYAN 630
Cdd:TIGR00954 638 RKSLWKYHE 646
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
399-635 |
2.65e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.36 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 399 LSFTLKEGKTYAFVGESGCGKS----TILKLIErlydpTEGDIIVN----DSHNLKDINLKWWRSKIG----VVSQDPLl 466
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLID-----YPGRVMAEklefNGQDLQRISEKERRNLVGaevaMIFQDPM- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 467 fsNSIknNIKYSLySLKDLEAMEnyyeentndTYENKNfslisnsmtsnellemKKEyqtiKDSDVVDVSKKVLIHDFVS 546
Cdd:PRK11022 100 --TSL--NPCYTV-GFQIMEAIK---------VHQGGN----------------KKT----RRQRAIDLLNQVGIPDPAS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 547 SLpDKYdtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI 626
Cdd:PRK11022 146 RL-DVY-------PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALV 217
|
250
....*....|
gi 124506379 627 -RYANTIFVL 635
Cdd:PRK11022 218 aEAAHKIIVM 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1142-1371 |
2.77e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.04 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1142 PIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiilkndmtnfqdyqnnnnnslvlknvnEFSNQSGSae 1221
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-----------------------------------ALKGTPVA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1222 dytvfnnnGEILLDDINicdynlrdlrnlfsivsqepmlfnmsiyenikFGREDATLEDVKRVSKFAAIDEFIeslpnky 1301
Cdd:COG2401 87 --------GCVDVPDNQ--------------------------------FGREASLIDAIGRKGDFKDAVELL------- 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 1302 dTNVG---------PYgKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR 1371
Cdd:COG2401 120 -NAVGlsdavlwlrRF-KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHH 196
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
378-588 |
2.88e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.62 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFhydTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSH--NLKDINLKWWRS 455
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipAMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 456 KIGVVSQDPLLFSnsiknnikyslyslkDLeamenyyeentnDTYENKNFSLISNSMTSNELLE----MKKEyqtikdsd 531
Cdd:PRK11831 85 RMSMLFQSGALFT---------------DM------------NVFDNVAYPLREHTQLPAPLLHstvmMKLE-------- 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 532 vvdvskKVLIHDFVSSLPdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDE 588
Cdd:PRK11831 130 ------AVGLRGAAKLMP-----------SELSGGMARRAALARAIALEPDLIMFDE 169
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
554-638 |
2.96e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.22 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 554 TLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTIN-----NLKGNENRITIIIAHRLSTIRY 628
Cdd:smart00382 52 IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEKNLTVILTTNDEKDLGP 131
|
90
....*....|
gi 124506379 629 ANTIFVLSNR 638
Cdd:smart00382 132 ALLRRRFDRR 141
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
397-594 |
3.12e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDINLK----WWRSKIGVVSQDP----LLFS 468
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG----HEVVTRspqdGLANGIVYISEDRkrdgLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 469 NSIKNNIkySLYSLKDLeamenyyeentndtyenknfsliSNSMTSnelLEMKKEYQTIKDsdvvdvskkvLIHDFVSSL 548
Cdd:PRK10762 345 MSVKENM--SLTALRYF-----------------------SRAGGS---LKHADEQQAVSD----------FIRLFNIKT 386
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 124506379 549 PDKyDTLVGsnasKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK10762 387 PSM-EQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1310-1385 |
3.41e-07 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 53.11 E-value: 3.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1310 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFN 1385
Cdd:cd03267 152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVID 228
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
54-288 |
3.64e-07 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 53.61 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 54 RKLLFISFVCAVLSGGT---LPFFISVF-GVILKNMNLGddinpIILSLVSIGLVQFILSMISSYCMD----VITSKIlk 125
Cdd:cd18549 1 KKLFFLDLFCAVLIAALdlvFPLIVRYIiDDLLPSKNLR-----LILIIGAILLALYILRTLLNYFVTywghVMGARI-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 126 tlklEY-LRSVFYQDGQ-----FHDNNP-G---SKLRSDLDFYLEQVSSGIGTKFITIFTYASSF-LGLYIwslikNARL 194
Cdd:cd18549 74 ----ETdMRRDLFEHLQklsfsFFDNNKtGqlmSRITNDLFDISELAHHGPEDLFISIITIIGSFiILLTI-----NVPL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 195 TLCITCVFPLIYVCGVICNKKVK-----LNKKTSLLYnnntmSIIEEALMGIRTVASYCGEKTILNKFNLSETFYSKYIL 269
Cdd:cd18549 145 TLIVFALLPLMIIFTIYFNKKMKkafrrVREKIGEIN-----AQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKK 219
|
250 260
....*....|....*....|....*.
gi 124506379 270 KANFVEA-------LHIGLINGLILV 288
Cdd:cd18549 220 KAYKAMAyffsgmnFFTNLLNLVVLV 245
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
402-628 |
4.51e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 52.80 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 402 TLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNdshnLKDINLKwwrskigvvsqdPLLFSNSIKNNIKYSLYS 481
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE----LDTVSYK------------PQYIKADYEGTVRDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 482 LKDLEAMENYYEentndtyenknfslisnsmtsnellemkkeyqtikdSDVVDvskkvlihdfvsslPDKYDTLVGSNAS 561
Cdd:cd03237 85 ITKDFYTHPYFK------------------------------------TEIAK--------------PLQIEQILDREVP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 562 KLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 628
Cdd:cd03237 115 ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDY 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1230-1404 |
5.33e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDDINICDYNLRD-LRNLFSIVSQE----------PMLFNmSIYENIKFGREDATLEDVKRVSKFA--AIDEFIES 1296
Cdd:PRK10982 303 GTITLHGKKINNHNANEaINHGFALVTEErrstgiyaylDIGFN-SLISNIRNYKNKVGLLDNSRMKSDTqwVIDSMRVK 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1297 LPNkYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIITIAHRIAS-I 1375
Cdd:PRK10982 382 TPG-HRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPElL 455
|
170 180
....*....|....*....|....*....
gi 124506379 1376 KRSDKIVVFNNPDRNGTFVQSHGTHDELL 1404
Cdd:PRK10982 456 GITDRILVMSNGLVAGIVDTKTTTQNEIL 484
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
393-626 |
5.47e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 393 VEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDINLKwwRSK------IGVVSQD-PL 465
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG----KEIDFK--SSKealengISMVHQElNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 466 LFSNSIKNNIKYSLYSLKDLEAMENyyeentndtyenknfslisnsmtsnellEMKKEYQTIKDSDVVDVSKKVLIhdfv 545
Cdd:PRK10982 85 VLQRSVMDNMWLGRYPTKGMFVDQD----------------------------KMYRDTKAIFDELDIDIDPRAKV---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 546 sslpdkydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLST 625
Cdd:PRK10982 133 ---------------ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGI-VYISHKMEE 196
|
.
gi 124506379 626 I 626
Cdd:PRK10982 197 I 197
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
381-594 |
5.64e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 52.62 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 381 KNVRFHYDTRKDVEiykDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII-------VNDSHNLKDINLKW- 452
Cdd:PRK11701 10 RGLTKLYGPRKGCR---DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqLRDLYALSEAERRRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 453 WRSKIGVVSQDP---LLFSNSIKNNIKYSLyslkdleamenyyeentndtyenknfslisnsMTSNEllemkKEYQTIKD 529
Cdd:PRK11701 87 LRTEWGFVHQHPrdgLRMQVSAGGNIGERL--------------------------------MAVGA-----RHYGDIRA 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 530 SdVVDVSKKVLIHdfvsslPDKYDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK11701 130 T-AGDWLERVEID------AARIDDLPTT----FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1230-1373 |
5.73e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDDINICDYNLRDLRNL-FSIVSQEPMLF----NMSIYENIKFGREDAtledvKRVSK-----FAAIDEFIESLPN 1299
Cdd:COG3845 313 GSIRLDGEDITGLSPRERRRLgVAYIPEDRLGRglvpDMSVAENLILGRYRR-----PPFSRggfldRKAIRAFAEELIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1300 KYD---TNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK--------AD-KTIIT 1367
Cdd:COG3845 388 EFDvrtPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgaavllisEDlDEILA 467
|
....*.
gi 124506379 1368 IAHRIA 1373
Cdd:COG3845 468 LSDRIA 473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1302-1370 |
5.82e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.79 E-value: 5.82e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 1302 DTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH 1370
Cdd:TIGR03719 156 DADVT----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTH 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
395-622 |
6.16e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.88 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 395 IYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLY--DPTEGDIIVNDshnlkdinLKWWRSKIGVvsqDpllfsnsik 472
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD--------NQFGREASLI---D--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 473 nnikySLYSLKD-LEAMEnyyeentndtyenknfsLISNSmtsnellemkkeyqtiKDSDVVDVSKKVlihdfvsslpdk 551
Cdd:COG2401 105 -----AIGRKGDfKDAVE-----------------LLNAV----------------GLSDAVLWLRRF------------ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 552 ydtlvgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIA-HR 622
Cdd:COG2401 135 ---------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKL-ARRAGITLVVAtHH 196
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
55-256 |
6.22e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 52.90 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 55 KLLFISFVCAVLSGGTlPFFIS-VFGVILKNMNLgDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYLR 133
Cdd:cd18555 6 SILLLSLLLQLLTLLI-PILTQyVIDNVIVPGNL-NLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 134 SVFYQDGQFHDNNPGSKL--RSDLDFYLEQVssgIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVCGVI 211
Cdd:cd18555 84 HLLKLPYSFFENRSSGDLlfRANSNVYIRQI---LSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 124506379 212 CNKKVK-LNKKtSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNK 256
Cdd:cd18555 161 TRKKIKkLNQE-EIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKK 205
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
406-636 |
6.23e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.12 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 406 GKTYAFVGESGCGKSTILKLIE-RLYDPT-EGDIIVNDSHNLKDInLKwwrsKIGVVSQDPLLFSN-SIKNNIKY-SLYS 481
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTKQI-LK----RTGFVTQDDILYPHlTVRETLVFcSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 482 LkdleamenyyeentndtyenknfsliSNSMTSNEllemkkeyqtikdsdvvdvskKVLIHDFVSS---LPDKYDTLVGS 558
Cdd:PLN03211 169 L--------------------------PKSLTKQE---------------------KILVAESVISelgLTKCENTIIGN 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 559 NASK-LSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIRYA--NTIFVL 635
Cdd:PLN03211 202 SFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMHQPSSRVYQmfDSVLVL 280
|
.
gi 124506379 636 S 636
Cdd:PLN03211 281 S 281
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
398-594 |
6.51e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.39 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 398 DLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIivndshNLKDINLKWWRSKIGVVSQ-DPLLFSNSIKNNIK 476
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI------TLDGKPVEGPGAERGVVFQnEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 477 YSLyslkdleamenyyeentndtyenknfslisnsmtsnELLEMKKEYQTIKDSDVVdvsKKVLIHDFVSSLPdkydtlv 556
Cdd:PRK11248 93 FGL------------------------------------QLAGVEKMQRLEIAHQML---KKVGLEGAEKRYI------- 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 124506379 557 gsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK11248 127 ----WQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1297-1370 |
7.05e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.89 E-value: 7.05e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 1297 LPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAH 1370
Cdd:PRK13537 128 LENKADAKVG----ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTH 196
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1310-1370 |
7.33e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 7.33e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124506379 1310 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdikdKADKTIITIAH 1370
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSH 399
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1293-1398 |
7.52e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.78 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1293 FIESLPNKYDTNVG--PYGK---SLSGGQKQRIAIARALLREPK--ILLLDEATSSLDSNS-EKLIE--KTIVDIKDkad 1362
Cdd:cd03238 64 FIDQLQFLIDVGLGylTLGQklsTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDiNQLLEviKGLIDLGN--- 140
|
90 100 110
....*....|....*....|....*....|....*..
gi 124506379 1363 kTIITIAHRIASIKRSDKIVVFN-NPDRNGTFVQSHG 1398
Cdd:cd03238 141 -TVILIEHNLDVLSSADWIIDFGpGSGKSGGKVVFSG 176
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1130-1410 |
8.33e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.32 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1130 DVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKST-FMNL--LLRfydlkndhiilkndmtnfqdyqnnNNNSLV 1206
Cdd:PRK13638 6 DLWFRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTlFMNLsgLLR------------------------PQKGAV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1207 LknvnefsnQSGSAEDYTvfnnngeillddinicDYNLRDLRNLFSIVSQEP--MLFNMSIYENIKFGRED---ATLEDV 1281
Cdd:PRK13638 59 L--------WQGKPLDYS----------------KRGLLALRQQVATVFQDPeqQIFYTDIDSDIAFSLRNlgvPEAEIT 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1282 KRVskfaaiDEFIeSLPNKYDTNVGPYgKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1361
Cdd:PRK13638 115 RRV------DEAL-TLVDAQHFRHQPI-QCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQG 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 124506379 1362 DKTIITiAHRIASIKR-SDKIVVFnnpdRNGTfVQSHGTHDELLSAQDGI 1410
Cdd:PRK13638 187 NHVIIS-SHDIDLIYEiSDAVYVL----RQGQ-ILTHGAPGEVFACTEAM 230
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
830-1060 |
8.48e-07 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 52.47 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 830 YSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFdqDKNTPG-VLSAHINrDVH----LLKTGL 904
Cdd:cd18545 42 IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFF--DSRPVGkILSRVIN-DVNslsdLLSNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 905 VNnivIFSHFIMLFLVSMVMsFYFCP----IVAAVLTFIYFInMRVFAVRARlTKSKEIEKKenmSSGVFAFssddemfk 980
Cdd:cd18545 119 IN---LIPDLLTLVGIVIIM-FSLNVrlalVTLAVLPLLVLV-VFLLRRRAR-KAWQRVRKK---ISNLNAY-------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 981 dpsflIQEAFYNMHTVINYGLEDYFCNLIEKAIDYKNKGQKRRIIVNAALWGFSQSAQLFINSFAYWFGSFLIKRGTILV 1060
Cdd:cd18545 182 -----LHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITV 256
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1248-1377 |
9.12e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.41 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1248 RNLFSIVSQEPMLFNMSIYENIKFGR--EDATLEDVKR-VSkfAAIDEFieSLPNKYDTnvgpYGKSLSGGQKQRIAIAR 1324
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLiiAGASGDDIRRrVS--AALDKV--GLLDKAKN----FPIQLSGGEQQRVGIAR 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 124506379 1325 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkDKADKTIITIAHRIASIKR 1377
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISR 202
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
389-637 |
9.30e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 52.92 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 389 TRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIV--NDSHNLKDINLKwwrSKIGVVSQDpll 466
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagDDVEALSARAAS---RRVASVPQD--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 467 fsnsiknnikyslyslkdleamenyyeentndtyenknfSLISNSMTSNELLEMKKEYQTIKDSDVVDVSKKVlihdfVS 546
Cdd:PRK09536 86 ---------------------------------------TSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAA-----VE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 547 SLPDKYDT--LVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDnkseylVQKTINNLK-----GNENRITIII 619
Cdd:PRK09536 122 RAMERTGVaqFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD------INHQVRTLElvrrlVDDGKTAVAA 195
|
250
....*....|....*....
gi 124506379 620 AHRLS-TIRYANTIFVLSN 637
Cdd:PRK09536 196 IHDLDlAARYCDELVLLAD 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1126-1402 |
9.65e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.14 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfyDLKNDHiilkndmtnfqdyqnnnnnsl 1205
Cdd:COG0488 316 LELEGLSKSY---GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG--ELEPDS--------------------- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 vlknvnefsnqsgsaedytvfnnnGEILLDDinicdyNLRdlrnlFSIVSQEPMLF--NMSIYENIKFGREDATLEDVKR 1283
Cdd:COG0488 370 ------------------------GTVKLGE------TVK-----IGYFDQHQEELdpDKTVLDELRDGAPGGTEQEVRG 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1284 vskfaaideFIESL---PNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdk 1360
Cdd:COG0488 415 ---------YLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--- 478
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 124506379 1361 aDKTIITIAH------RIAsikrsDKIVVFnnpdRNGTFVQSHGTHDE 1402
Cdd:COG0488 479 -PGTVLLVSHdryfldRVA-----TRILEF----EDGGVREYPGGYDD 516
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1302-1370 |
1.40e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 1.40e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 1302 DTNVGPygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH 1370
Cdd:PRK11819 158 DAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG----TVVAVTH 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1312-1343 |
1.63e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.97 E-value: 1.63e-06
10 20 30
....*....|....*....|....*....|..
gi 124506379 1312 LSGGQKQRIAIARALLREPKILLLDEATSSLD 1343
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
399-623 |
1.69e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.09 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 399 LSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDI--NLKWWRSKIGVVSQDPLLFSNsiknnik 476
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG----KDIetNLDAVRQSLGMCPQHNILFHH------- 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 477 yslyslkdLEAMEN--YYEENTNDTYENKNFSLisNSMTSNELLEMKKEYQtikdsdvvdvskkvlihdfvsslpdkydt 554
Cdd:TIGR01257 1018 --------LTVAEHilFYAQLKGRSWEEAQLEM--EAMLEDTGLHHKRNEE----------------------------- 1058
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 555 lvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRL 623
Cdd:TIGR01257 1059 -----AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
563-635 |
1.71e-06 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 49.92 E-value: 1.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124506379 563 LSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHRLSTIRYANTIFVL 635
Cdd:NF040873 120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1230-1405 |
1.84e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.28 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDDINICDYNLRDLRNLFSIVSQEPMLFnmsiyenikfgreDATLEDVKRVSKFAAIDEFIESLPNKYDTNVGPyG 1309
Cdd:PRK10522 378 GEILLDGKPVTAEQPEDYRKLFSAVFTDFHLF-------------DQLLGPEGKPANPALVEKWLERLKMAHKLELED-G 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1310 K----SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFn 1385
Cdd:PRK10522 444 RisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEM- 522
|
170 180
....*....|....*....|
gi 124506379 1386 npdRNGTFVQSHGTHDELLS 1405
Cdd:PRK10522 523 ---RNGQLSELTGEERDAAS 539
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
397-637 |
1.87e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII-----VNDSHNLKDIN-----LKWWRSKIGVVSQDPLL 466
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITlhgkkINNHNANEAINhgfalVTEERRSTGIYAYLDIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 467 FsNSIKNNIkyslyslkdleamenyyeentnDTYENKnFSLISNSmtsnellEMKKEYQTIKDSDVVDVSKkvlihdfvs 546
Cdd:PRK10982 345 F-NSLISNI----------------------RNYKNK-VGLLDNS-------RMKSDTQWVIDSMRVKTPG--------- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 547 slpdkYDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI 626
Cdd:PRK10982 385 -----HRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELL 455
|
250
....*....|.
gi 124506379 627 RYANTIFVLSN 637
Cdd:PRK10982 456 GITDRILVMSN 466
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1310-1374 |
2.02e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.19 E-value: 2.02e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 1310 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIAS 1374
Cdd:PLN03211 205 RGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKG-KTIVTSMHQPSS 268
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
389-618 |
2.21e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.24 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 389 TRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVN--DSHNLKDINLKwwrsKIGVV----SQ 462
Cdd:COG4586 31 EYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyVPFKRRKEFAR----RIGVVfgqrSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 463 dpLLFsnsiknnikyslyslkDLEAMENYyeentndtyenknfslisnsmtsnELLemKKEYqtikdsdvvDVSKKVL-- 540
Cdd:COG4586 107 --LWW----------------DLPAIDSF------------------------RLL--KAIY---------RIPDAEYkk 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 541 -IHDFVS--SLPDKYDTLVgsnaSKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITI 617
Cdd:COG4586 134 rLDELVEllDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYN-RERGTTI 208
|
.
gi 124506379 618 I 618
Cdd:COG4586 209 L 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1311-1377 |
2.45e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 2.45e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1311 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAHRIASIKR 1377
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRN 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1263-1406 |
2.79e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1263 MSIYENIkfgredaTLEDVKRVSKFAAID---------EFIESLPNKYDTNVGPYGkSLSGGQKQRIAIARALLREPKIL 1333
Cdd:PRK13549 356 MGVGKNI-------TLAALDRFTGGSRIDdaaelktilESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKIL 427
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 1334 LLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASI-KRSDKIVVFNNPDRNGTFVQSHGTHDELLSA 1406
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSELPEVlGLSDRVLVMHEGKLKGDLINHNLTQEQVMEA 500
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
57-303 |
2.93e-06 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 50.87 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 57 LFISFVCAVLSGGTLPFFISVFGVI---LKNMNL-GDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYL 132
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAidaLTAGTLtASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 133 RSVFYQDGQFHDNNP-G---SKLRSDLDFYLEQVSSGIGTKFITIFTYASSflgLYIWSLIkNARLTLCITCVFPLIYVC 208
Cdd:cd18541 81 AHLLTLSPSFYQKNRtGdlmARATNDLNAVRMALGPGILYLVDALFLGVLV---LVMMFTI-SPKLTLIALLPLPLLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 209 GVicnkkvKLNKKTSLLYNNN-----TMS-IIEEALMGIRTVASYCGEKTILNKF-NLSETFYSKYiLKANFVEALHIGL 281
Cdd:cd18541 157 VY------RLGKKIHKRFRKVqeafsDLSdRVQESFSGIRVIKAFVQEEAEIERFdKLNEEYVEKN-LRLARVDALFFPL 229
|
250 260
....*....|....*....|..
gi 124506379 282 INGLILVSYAFGFWYGTRIIIN 303
Cdd:cd18541 230 IGLLIGLSFLIVLWYGGRLVIR 251
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
789-953 |
3.30e-06 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 50.51 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 789 VTIIFFSILVAgglypVFALLYARYVSTLFDFANLEYNSNKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLF 868
Cdd:cd18551 2 ILALLLSLLGT-----AASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 869 ENILYQEMSFFdqDKNTPGVLSAHINRDVHLLKT-------GLVNNI--VIFShFIMLFLVSMVMSFYFCPIVAAVLTFI 939
Cdd:cd18551 77 RRLLRLPVSFF--DRRRSGDLVSRVTNDTTLLRElitsglpQLVTGVltVVGA-VVLMFLLDWVLTLVTLAVVPLAFLII 153
|
170
....*....|....
gi 124506379 940 YFINMRVFAVRARL 953
Cdd:cd18551 154 LPLGRRIRKASKRA 167
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1290-1386 |
3.48e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.86 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1290 IDEFIE--SLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1367
Cdd:COG4586 135 LDELVEllDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILL 210
|
90 100
....*....|....*....|
gi 124506379 1368 IAHRIASIKR-SDKIVVFNN 1386
Cdd:COG4586 211 TSHDMDDIEAlCDRVIVIDH 230
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
829-947 |
3.61e-06 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 50.47 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 829 KYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFENIlyQEMSFFDQDKNTPGVLsahINR---DVHLLKTGLV 905
Cdd:cd18548 40 RTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKI--QSFSFAEIDKFGTSSL---ITRltnDVTQVQNFVM 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 124506379 906 NNI---------VIFShFIMLFLVSMVMSFYFCPIVAAVLTFIYFINMRVF 947
Cdd:cd18548 115 MLLrmlvrapimLIGA-IIMAFRINPKLALILLVAIPILALVVFLIMKKAI 164
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1230-1351 |
4.66e-06 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 49.03 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDdiNICDYNLRDL--RNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVkrvskFAAIDEF----IESLPNKYdt 1303
Cdd:cd03231 55 GRVLLN--GGPLDFQRDSiaRGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQV-----EEALARVglngFEDRPVAQ-- 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 124506379 1304 nvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1351
Cdd:cd03231 126 --------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
563-637 |
4.77e-06 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 48.58 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 563 LSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIahrLST-----IRYANTIFVLSN 637
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELA--DAGKAVLL---ISSeldelLGLCDRILVMYE 179
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
832-953 |
4.90e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 50.20 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 832 IYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFdqDKNTPGVLSAHINRDVHLLKTGLVNNIV-I 910
Cdd:cd18563 47 LGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFF--DKRQTGSLMSRVTSDTDRLQDFLSDGLPdF 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 124506379 911 FSHFIMLFLVSMVMsFYFCPIVA-AVLTFIYFINMRVFAVRARL 953
Cdd:cd18563 125 LTNILMIIGIGVVL-FSLNWKLAlLVLIPVPLVVWGSYFFWKKI 167
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
56-303 |
5.34e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 49.87 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 56 LLFISFVCAVLsGGTLPFFIS-VFGVILKNMNLgDDINPIILSLVSIGLVQFILSMISSYCMDVITSKI----------- 123
Cdd:cd18568 7 ILLASLLLQLL-GLALPLFTQiILDRVLVHKNI-SLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIdlsllsdfykh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 124 LKTLKLEYLRSvfYQDG----QFHDNNpgsKLRSdldfYLEQVSSGIGTKFITIFTYASSFLgLYiwslikNARLTLCIT 199
Cdd:cd18568 85 LLSLPLSFFAS--RKVGdiitRFQENQ---KIRR----FLTRSALTTILDLLMVFIYLGLMF-YY------NLQLTLIVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 200 CVFPLIYVCGVICNKKVKLNKKTSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNKFnlsETFYSKYiLKANF-VEALH 278
Cdd:cd18568 149 AFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRW---ENKFAKA-LNTRFrGQKLS 224
|
250 260
....*....|....*....|....*...
gi 124506379 279 I--GLINGLI-LVSYAFGFWYGTRIIIN 303
Cdd:cd18568 225 IvlQLISSLInHLGTIAVLWYGAYLVIS 252
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1230-1342 |
5.38e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.49 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1230 GEILLDDINICDYNL-RDLRNLFSIVSQEPMLFN-MSIYENIK----FGREDATLEDVKRVskfaaidefIESLPNKYDT 1303
Cdd:PRK11614 60 GRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSrMTVEENLAmggfFAERDQFQERIKWV---------YELFPRLHER 130
|
90 100 110
....*....|....*....|....*....|....*....
gi 124506379 1304 NVGPYGkSLSGGQKQRIAIARALLREPKILLLDEATSSL 1342
Cdd:PRK11614 131 RIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
789-1017 |
5.53e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 49.78 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 789 VTIIFFSILVAGGLYpVFALLYARY-VSTLFDFANLEYnsnkYSIYILLiAIAMFISETLKNYYNNKIGEKVEKTMKRRL 867
Cdd:cd18606 1 LPLLLLLLILSQFAQ-VFTNLWLSFwTEDFFGLSQGFY----IGIYAGL-GVLQAIFLFLFGLLLAYLGIRASKRLHNKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 868 FENILYQEMSFFDQdknTPgvLSAHINR---DVHLLKTGLVNNIVIFSHFIMLFLVSMVMSFYFCP---IVAAVLTFIYF 941
Cdd:cd18606 75 LKRVLRAPMSFFDT---TP--LGRILNRfskDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPwfaIALPPLLVLYY 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 942 INMRVFavRArltKSKEIEKKENMS-SGVFA-FSsddemfkdpsfliqEAFYNMHTVINYGLEDYFCNLIEKAIDYKN 1017
Cdd:cd18606 150 FIANYY--RA---SSRELKRLESILrSFVYAnFS--------------ESLSGLSTIRAYGAQDRFIKKNEKLIDNMN 208
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
561-635 |
5.57e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.94 E-value: 5.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 561 SKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIRY-ANTIFVL 635
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1128-1407 |
5.85e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.40 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1128 IKDVNFRYisrPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRfydlkndhiilkndmtnfqdyqnnnnnslvl 1207
Cdd:PRK10575 14 LRNVSFRV---PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGR------------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1208 knvnefsNQSGSAedytvfnnnGEILLDDINICDYNLRDL-RNLFSIVSQEPMLFNMSIYENI------------KFGRE 1274
Cdd:PRK10575 60 -------HQPPSE---------GEILLDAQPLESWSSKAFaRKVAYLPQQLPAAEGMTVRELVaigrypwhgalgRFGAA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1275 DAtlEDVKRVSKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1354
Cdd:PRK10575 124 DR--EKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALV 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 124506379 1355 VDIKDKADKTIITIAHRIASIKR-SDKIVVFnnpdRNGTFVqSHGTHDELLSAQ 1407
Cdd:PRK10575 191 HRLSQERGLTVIAVLHDINMAARyCDYLVAL----RGGEMI-AQGTPAELMRGE 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
563-608 |
7.68e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 7.68e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124506379 563 LSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNL 608
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQL 451
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1289-1406 |
8.04e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.21 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1289 AIDEFIESLPNKYDTNVGPYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITI 1368
Cdd:TIGR02633 382 IIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEG-VAIIVV 459
|
90 100 110
....*....|....*....|....*....|....*....
gi 124506379 1369 AHRIASI-KRSDKIVVFNNPDRNGTFVQSHGTHDELLSA 1406
Cdd:TIGR02633 460 SSELAEVlGLSDRVLVIGEGKLKGDFVNHALTQEQVLAA 498
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1147-1343 |
8.61e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.78 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1147 LSFTCDSKKTTAIVGETGSGKSTfmnLLLRfydlkndhiilkndMTNFQDYQnnnnnslvlknvnefsnqsgsaedytvf 1226
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLAR--------------MAGLLPGS---------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1227 nnnGEILLDDINICDYNLRDL---RNLFSivSQEPMLFNMSIYENIKFGREDATLEDVKRvskfAAIDEFIES--LPNKY 1301
Cdd:PRK03695 50 ---GSIQFAGQPLEAWSAAELarhRAYLS--QQQTPPFAMPVFQYLTLHQPDKTRTEAVA----SALNEVAEAlgLDDKL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 124506379 1302 DTNVGpygkSLSGGQKQRIAIARALLR-------EPKILLLDEATSSLD 1343
Cdd:PRK03695 121 GRSVN----QLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1312-1370 |
8.70e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.96 E-value: 8.70e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 1312 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1370
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1312-1370 |
9.20e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.62 E-value: 9.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 1312 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1370
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTH 205
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1308-1383 |
9.46e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.35 E-value: 9.46e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1308 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRS-DKIVV 1383
Cdd:PRK11022 150 YPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAaHKIIV 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1282-1373 |
9.53e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.17 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1282 KRVSKFAAIDEFIE--SLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLD----SNSEKLIEKTIv 1355
Cdd:COG1245 185 EKVDERGKLDELAEklGLENILDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELA- 259
|
90
....*....|....*...
gi 124506379 1356 dikdKADKTIITIAHRIA 1373
Cdd:COG1245 260 ----EEGKYVLVVEHDLA 273
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1312-1392 |
1.16e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.45 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1312 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR---IASIkrSDKIVVFNN-- 1386
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDmklVMGI--SDRIYVVNQgt 231
|
....*.
gi 124506379 1387 PDRNGT 1392
Cdd:PRK11300 232 PLANGT 237
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
563-637 |
1.35e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 48.23 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 563 LSGGQKQRISIARAIMR------NPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 635
Cdd:PRK13548 135 LSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNlAARYADRIVLL 214
|
..
gi 124506379 636 SN 637
Cdd:PRK13548 215 HQ 216
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
404-628 |
1.36e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.52 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 404 KEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDShnlkdinlkwWRskiGVVSQdpllFSNSiknnikyslyslk 483
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPD----------WD---EILDE----FRGS------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 484 dleAMENYYEENTND----TYENKNFSLISNSMTSNELLEMKKEYQTIKDSDVVDVSKkvlihdfvsslpdkYDTLVGSN 559
Cdd:cd03236 74 ---ELQNYFTKLLEGdvkvIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLE--------------LRHVLDRN 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124506379 560 ASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTIRY 628
Cdd:cd03236 137 IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV-LVVEHDLAVLDY 204
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
378-637 |
1.38e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.95 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrkDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDINlKW----- 452
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG----KDIT-DWqtaki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 453 WRSKIGVVSQDPLLFSN-SIKNNIkyslyslkdleAMENYYEEntndtyenknfslisnsmtsnellemKKEYQTikdsd 531
Cdd:PRK11614 78 MREAVAIVPEGRRVFSRmTVEENL-----------AMGGFFAE--------------------------RDQFQE----- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 532 vvdvsKKVLIHDFVSSLPDKYDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSLdnkSEYLVQK---TINNL 608
Cdd:PRK11614 116 -----RIKWVYELFPRLHERRIQRAGT----MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---APIIIQQifdTIEQL 183
|
250 260
....*....|....*....|....*....
gi 124506379 609 KGNENRITIIIAHRLSTIRYANTIFVLSN 637
Cdd:PRK11614 184 REQGMTIFLVEQNANQALKLADRGYVLEN 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
398-594 |
1.72e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 398 DLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-----IVNDshnlKDINLkwwRSKIGVVSQdpllfsnsik 472
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDA----GDIAT---RRRVGYMSQ---------- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 473 nniKYSLYS-------LkDLEAmenyyeentndtyenknfslisnsmtsnELLEMKKEyqtikdsdvvDVSKKV--LIHD 543
Cdd:NF033858 347 ---AFSLYGeltvrqnL-ELHA----------------------------RLFHLPAA----------EIAARVaeMLER 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 124506379 544 FvsSLPDKYDTLvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:NF033858 385 F--DLADVADAL----PDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
563-640 |
1.82e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.22 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 563 LSGGQKQ------RISIARAIMRNPKILILDEATSSLD--NKSEYLVQkTINNLKGNENRITIIIAHRLSTIRYANTIFV 634
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeeNIEESLAE-IIEERKSQKNFQLIVITHDEELVDAADHIYR 194
|
....*.
gi 124506379 635 LSNRER 640
Cdd:cd03240 195 VEKDGR 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
390-594 |
2.16e-05 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 46.97 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 390 RKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNlkdinlkwwrSKIGVVSQDPLLF-- 467
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL----------AEQRDEPHENILYlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 468 -SNSIKNnikyslyslkDLEAMENyyeentndtyenknfslisnsmtsnelLEMKKEYQTIKDSDVVDVSKKVLIHDFvS 546
Cdd:TIGR01189 80 hLPGLKP----------ELSALEN---------------------------LHFWAAIHGGAQRTIEDALAAVGLTGF-E 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 124506379 547 SLPdkydtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:TIGR01189 122 DLP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
378-635 |
2.84e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 47.67 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDtrKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDINLKWWRSKI 457
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 458 GVVSQDPllfsnsiknnikyslyslkDLEAMENYYEENTNDTYENKNFSLIS-NSMTSNELLEMKKEyqtikdsdvvdvs 536
Cdd:PRK13644 80 GIVFQNP-------------------ETQFVGRTVEEDLAFGPENLCLPPIEiRKRVDRALAEIGLE------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 537 kkvlihdfvsslpdKYDTlvgSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRIT 616
Cdd:PRK13644 128 --------------KYRH---RSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTI 189
|
250
....*....|....*....
gi 124506379 617 IIIAHRLSTIRYANTIFVL 635
Cdd:PRK13644 190 VYITHNLEELHDADRIIVM 208
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
369-625 |
3.04e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.39 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 369 GETLPNiKKIEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDShnlkdi 448
Cdd:TIGR03719 315 GPRLGD-KVIEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET------ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 449 nlkwwrSKIGVVSQdpllfsnsiknnikyslySLKDLEAMENYYEEntndtyenknfslISNsmtSNELLEMKKeyqtik 528
Cdd:TIGR03719 385 ------VKLAYVDQ------------------SRDALDPNKTVWEE-------------ISG---GLDIIKLGK------ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 529 dsdvVDVSKKVLIHDFVSSLPDKyDTLVGSnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDnkseylvqktINNL 608
Cdd:TIGR03719 419 ----REIPSRAYVGRFNFKGSDQ-QKKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD----------VETL 479
|
250 260
....*....|....*....|....*....
gi 124506379 609 KGNENRI------TIIIAH------RLST 625
Cdd:TIGR03719 480 RALEEALlnfagcAVVISHdrwfldRIAT 508
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
406-626 |
3.14e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.46 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 406 GKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDINLKWWRSK----IGVVSQDPLLFSN-SIKNNIKYSly 480
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG----KEVTFNGPKSSqeagIGIIHQELNLIPQlTIAENIFLG-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 481 slkdleamenyyEENTNdtyenkNFSLIsnsmtsnellEMKKEYQtikDSDvvdvskKVLIHdfvSSLPDKYDTLVGsna 560
Cdd:PRK10762 104 ------------REFVN------RFGRI----------DWKKMYA---EAD------KLLAR---LNLRFSSDKLVG--- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 561 sKLSGGQKQRISIARAIMRNPKILILDEATSSL-DNKSEYLVqKTINNLKgNENRITIIIAHRLSTI 626
Cdd:PRK10762 141 -ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRELK-SQGRGIVYISHRLKEI 204
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
789-955 |
3.26e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 47.48 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 789 VTIIFFSILVAGGLYPVFALLYARYVSTLF---DFANLeynsNKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKR 865
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALpqgDLGLL----VLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 866 RLFENILYQEMSFFDQDKntPGVLSAHINRDVHLLKTGLVNNIV-IFSHFIMLFLVSMVMsFYFCPIVA----AVLTFIY 940
Cdd:cd18550 77 QLYAHLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGTLTsVVSNVVTLVATLVAM-LALDWRLAllslVLLPLFV 153
|
170
....*....|....*
gi 124506379 941 FINMRVFAVRARLTK 955
Cdd:cd18550 154 LPTRRVGRRRRKLTR 168
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
399-637 |
3.52e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.85 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 399 LSFTLKEGKTYAFVGESGCGKSTILKLIERLYdPTEGDIIVNDShnlkdinlkwwrskigvvsqdPLlfsnsiknnikyS 478
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQ---------------------PL------------E 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 479 LYSLKDLEAMENYYEENTNDTYenknfslisnSMTSNELLEMkkeYQTikDSDVVDVSKKVLiHDFVSSLpdKYDTLVGS 558
Cdd:PRK03695 61 AWSAAELARHRAYLSQQQTPPF----------AMPVFQYLTL---HQP--DKTRTEAVASAL-NEVAEAL--GLDDKLGR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 559 NASKLSGGQKQRISIARAIMR-----NP--KILILDEATSSLDNKSEYLVQKTINNL--KGnenrITIIIA-HRLS-TIR 627
Cdd:PRK03695 123 SVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLDVAQQAALDRLLSELcqQG----IAVVMSsHDLNhTLR 198
|
250
....*....|
gi 124506379 628 YANTIFVLSN 637
Cdd:PRK03695 199 HADRVWLLKQ 208
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
824-1058 |
3.67e-05 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 47.33 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 824 EYNSNKYSIYILLIAIAMFISET---LKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFDqdKNTPGVLSAHINRDVHLL 900
Cdd:cd18590 29 EYQHNAFTSAIGLMCLFSLGSSLsagLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDTTLM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 901 KTGLVNNIVIFshfiMLFLVSMVMSFYFCPIVAAVLTFIYFINMRVFAVrarltkskeIEKKENMSSGVFAFSSDDEMFK 980
Cdd:cd18590 107 SRSVALNANVL----LRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAI---------AQKVYNTYHQKLSQAVQDSIAK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 981 DPSfLIQEAFYNMHTVINYGLEDYFCNLIEKAIDYKNKGQKRRIIVNAALWGFSQSAQLFINSFAYWFGSFLIKRGTI 1058
Cdd:cd18590 174 AGE-LAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1281-1373 |
3.73e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1281 VKRVSKFAAIDEFIE--SLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1358
Cdd:PRK13409 184 LKKVDERGKLDEVVErlGLENILDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA 259
|
90
....*....|....*
gi 124506379 1359 DkaDKTIITIAHRIA 1373
Cdd:PRK13409 260 E--GKYVLVVEHDLA 272
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1312-1375 |
3.98e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.18 E-value: 3.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 1312 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI 1375
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEG-KTMLVSTHNLGSV 205
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
375-519 |
4.68e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 47.30 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 375 IKKIEFKNVRfhydtrkdveIYKDLSFTLKEGKTyAFVGESGCGKSTILKLIERLYDPTEGDII-VNDSHNLKDINLK-- 451
Cdd:COG3593 3 LEKIKIKNFR----------SIKDLSIELSDDLT-VLVGENNSGKSSILEALRLLLGPSSSRKFdEEDFYLGDDPDLPei 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 452 ----WWRSKIGVVSQDplLFSNSIKNNIKYSLYSLKD-----LEAMENYYEENTNDTYENKNFSLISNSMTSNELLE 519
Cdd:COG3593 72 eielTFGSLLSRLLRL--LLKEEDKEELEEALEELNEelkeaLKALNELLSEYLKELLDGLDLELELSLDELEDLLK 146
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
562-628 |
4.76e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 4.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 562 KLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 628
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDY 137
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1312-1376 |
4.95e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 47.82 E-value: 4.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 1312 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHRIASIK 1376
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD----VEGYMYRLCREFGITLFSVSHRKSLWK 643
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1126-1357 |
5.10e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1126 VDIKDVNFRYISRPnvpIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlKNDHIilkndmtnfQDYqnnnNNSL 1205
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------TGDHP---------QGY----SNDL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1206 VLknvneFSNQSGSAEdyTVFnnngeilldDI--NI--------CDY----NLRD--LRNLF-SIvsqepmlfnmSIYEN 1268
Cdd:PRK10938 319 TL-----FGRRRGSGE--TIW---------DIkkHIgyvssslhLDYrvstSVRNviLSGFFdSI----------GIYQA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1269 IKfgredatledvKRVSKFAaiDEFIESLPNKYDTNVGPYgKSLSGGQkQRIA-IARALLREPKILLLDEATSSLDSNSE 1347
Cdd:PRK10938 373 VS-----------DRQQKLA--QQWLDILGIDKRTADAPF-HSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNR 437
|
250
....*....|
gi 124506379 1348 KLIeKTIVDI 1357
Cdd:PRK10938 438 QLV-RRFVDV 446
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
561-608 |
5.50e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.51 E-value: 5.50e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 124506379 561 SKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNL 608
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL 449
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1146-1343 |
5.54e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.46 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1146 NLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnSLVLKNvnefsnQSGSAEdytv 1225
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNAL-----------------------------SARLAP------DAGEVH---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1226 FNNNGEILLDDINICDYNLRDL-RNLFSIVSQEPML-FNMSI-----------------YENIkfgREDAT--LEDVKrv 1284
Cdd:PRK11701 65 YRMRDGQLRDLYALSEAERRRLlRTEWGFVHQHPRDgLRMQVsaggnigerlmavgarhYGDI---RATAGdwLERVE-- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1285 skfaaID-EFIESLPNKYdtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLD 1343
Cdd:PRK11701 140 -----IDaARIDDLPTTF-----------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
401-594 |
6.46e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 401 FTLKEGKTYAFVGESGCGKSTILKLI--ERLYDptEGDIIVNdshnlKDInlkwwrskigVVS---QDPllfsnsiKNNI 475
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILngEVLLD--DGRIIYE-----QDL----------IVArlqQDP-------PRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 476 KYSLYS-----LKDL-EAMENYYE--ENTNDTYENKNFSLISNSMtsnELLEMKKEYQTikDSDVVDVSKKVLIHdfvss 547
Cdd:PRK11147 80 EGTVYDfvaegIEEQaEYLKRYHDisHLVETDPSEKNLNELAKLQ---EQLDHHNLWQL--ENRINEVLAQLGLD----- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 124506379 548 lPDKydtlvgsNASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK11147 150 -PDA-------ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
516-632 |
6.81e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.70 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 516 ELLEMKKEYQTIkdSDVVDVSKKVlIHDFVSSLPD---KYDTLV---------GSNASKLSGGQKQRISIARAIMR---N 580
Cdd:TIGR00630 774 ETLEVKYKGKNI--ADVLDMTVEE-AYEFFEAVPSisrKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstG 850
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 581 PKILILDEATSSLD----NKSEYLVQKTINnlKGNEnriTIIIAHRLSTIRYANTI 632
Cdd:TIGR00630 851 RTLYILDEPTTGLHfddiKKLLEVLQRLVD--KGNT---VVVIEHNLDVIKTADYI 901
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
412-597 |
7.57e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 412 VGESGCGKSTILKLIERLYDPTEGDIIVNDSHnlkdinlkwwrsKIGVVSQDPLL-FSNSIKNNIKYSLYSLKDL----- 485
Cdd:PRK11819 39 LGLNGAGKSTLLRIMAGVDKEFEGEARPAPGI------------KVGYLPQEPQLdPEKTVRENVEEGVAEVKAAldrfn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 486 EAMENYYEENTNdtyenknfslisnsmtSNELLEMKKEYQTIKDS-DVVDVSKKVLIHDFVSSLPDKyDTLVgsnaSKLS 564
Cdd:PRK11819 107 EIYAAYAEPDAD----------------FDALAAEQGELQEIIDAaDAWDLDSQLEIAMDALRCPPW-DAKV----TKLS 165
|
170 180 190
....*....|....*....|....*....|...
gi 124506379 565 GGQKQRISIARAIMRNPKILILDEATSSLDNKS 597
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1132-1384 |
8.25e-05 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 45.60 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1132 NFRYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILKNDMtnfqdyqnnnnnSLVLknvn 1211
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV------------SSLL---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1212 EFsnQSGsaedytvFNNNgeillddinicdynlrdlrnlfsivsqepmlfnMSIYENIKFgreDATLEDVKRVSKFAAID 1291
Cdd:cd03220 90 GL--GGG-------FNPE---------------------------------LTGRENIYL---NGRLLGLSRKEIDEKID 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1292 EFIE--SLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKtIVDIKDKAdKTIITI 1368
Cdd:cd03220 125 EIIEfsELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRR-LRELLKQG-KTVILV 198
|
250
....*....|....*..
gi 124506379 1369 AHRIASIKR-SDKIVVF 1384
Cdd:cd03220 199 SHDPSSIKRlCDRALVL 215
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
562-626 |
8.45e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 8.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 562 KLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTI 626
Cdd:PRK15056 142 ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELR-DEGKTMLVSTHNLGSV 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
543-638 |
8.54e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 543 DFVSSLPDKYDT---------------LVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINN 607
Cdd:PRK13409 419 DLLRSITDDLGSsyykseiikplqlerLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 498
|
90 100 110
....*....|....*....|....*....|.
gi 124506379 608 LKGNENRITIIIAHRLSTIRYantifvLSNR 638
Cdd:PRK13409 499 IAEEREATALVVDHDIYMIDY------ISDR 523
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1132-1372 |
8.64e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.39 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1132 NFRYISRPNVpiyknLSFTcdsKKTTAIVGETGSGKSTFMN-LLLRFYDLKNDHIILKNDMTNfqdyQNNNNNSLVLknv 1210
Cdd:COG0419 9 NFRSYRDTET-----IDFD---DGLNLIVGPNGAGKSTILEaIRYALYGKARSRSKLRSDLIN----VGSEEASVEL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1211 nEFSNQSGSaedYTVFNNNGEIllddINICDYNLRDLRNLFSIvsqepmLFNMSIYENIKFGREDATLEDVKRVSKFAAI 1290
Cdd:COG0419 74 -EFEHGGKR---YRIERRQGEF----AEFLEAKPSERKEALKR------LLGLEIYEELKERLKELEEALESALEELAEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1291 DEFIESLPNKYdTNVGPYgKSLSGGQKQRIAIARALLrepkiLLLDeaTSSLDSNSEKLIEKTIVDIKdkadktIITiaH 1370
Cdd:COG0419 140 QKLKQEILAQL-SGLDPI-ETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA------IIT--H 202
|
..
gi 124506379 1371 RI 1372
Cdd:COG0419 203 VI 204
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1137-1394 |
9.72e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1137 SRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILKNDMTNFqdyqnnnnnslvlKNVNEfsnq 1216
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF-------------KSSKE---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1217 sgsaedytvfnnngeillddinicdynlrDLRNLFSIVSQE-PMLFNMSIYENIKFGR---------EDATLEDVKRVsk 1286
Cdd:PRK10982 70 -----------------------------ALENGISMVHQElNLVLQRSVMDNMWLGRyptkgmfvdQDKMYRDTKAI-- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1287 faaIDEFieslpnkyDTNVGPYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSLdsnSEKLIE---KTIVDIKDKA 1361
Cdd:PRK10982 119 ---FDEL--------DIDIDPRAKvaTLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKEVNhlfTIIRKLKERG 184
|
250 260 270
....*....|....*....|....*....|....
gi 124506379 1362 dKTIITIAHRIASIKR-SDKIVVFnnpdRNGTFV 1394
Cdd:PRK10982 185 -CGIVYISHKMEEIFQlCDEITIL----RDGQWI 213
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
378-597 |
1.04e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 378 IEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIivndshnlkdinlKWW-RSK 456
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------------KWSeNAN 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 457 IGVVSQDpllfsnsiknnikyslyslkdleamenYYEENTNDtyenknfslisnsMTsneLLEMKKEYQTIKDSDVV--- 533
Cdd:PRK15064 384 IGYYAQD---------------------------HAYDFEND-------------LT---LFDWMSQWRQEGDDEQAvrg 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 534 ----------DVSKKVLIhdfvsslpdkydtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKS 597
Cdd:PRK15064 421 tlgrllfsqdDIKKSVKV---------------------LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES 473
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
400-626 |
1.06e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 45.75 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 400 SFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSH--NLKDINLkwwrSKIGVVS--QDPLLFsnsiknni 475
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieGLPGHQI----ARMGVVRtfQHVRLF-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 476 kyslyslKDLEAMEN-----YYEENTNdtyenknfsLISNsmtsneLLEMKKEYQtiKDSDVVDVSKKVLihDFVSSLPd 550
Cdd:PRK11300 93 -------REMTVIENllvaqHQQLKTG---------LFSG------LLKTPAFRR--AESEALDRAATWL--ERVGLLE- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 551 kydtLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI 626
Cdd:PRK11300 146 ----HANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLV 217
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
789-1072 |
1.07e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 45.99 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 789 VTIIFFSILVAGGLYPVFALLYARYVSTLFDFANLEYNSNKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLF 868
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 869 ENILYQEMSFFDqDKNTpGVLSAHINRDVHLLKTGLVNNIVIFSHFIMLFLVSMVMSFYFCPIVAAV----LTFIYFINM 944
Cdd:cd18778 81 DKLQRLSLRYFD-DRQT-GDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLtlipIPFLALGAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 945 RvFAVRARltkskEIEKKENMSSGvfafssddEMfkdpSFLIQEAFYNMHTVINYGLEDYfcnliEKAiDYKNKGQK-RR 1023
Cdd:cd18778 159 L-YSKKVR-----PRYRKVREALG--------EL----NALLQDNLSGIREIQAFGREEE-----EAK-RFEALSRRyRK 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 124506379 1024 IIVNAA-LWGFSQSAQLFINSFAY----WFGSFLIKRGTILVDDfmksLFTFIF 1072
Cdd:cd18778 215 AQLRAMkLWAIFHPLMEFLTSLGTvlvlGFGGRLVLAGELTIGD----LVAFLL 264
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
553-635 |
1.23e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.34 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 553 DTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIRY-ANT 631
Cdd:PRK13409 203 ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL--AEGKYVLVVEHDLAVLDYlADN 280
|
....
gi 124506379 632 IFVL 635
Cdd:PRK13409 281 VHIA 284
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1277-1399 |
1.24e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.44 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1277 TLEDVKRVSKFAAIDEFIE--SLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS----NSEKLI 1350
Cdd:cd03236 107 VGELLKKKDERGKLDELVDqlELRHVLDRNI----DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrlNAARLI 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 124506379 1351 EKTIVDikdkaDKTIITIAHRIASIKR-SDKI-VVFNNPDRNGTFVQSHGT 1399
Cdd:cd03236 183 RELAED-----DNYVLVVEHDLAVLDYlSDYIhCLYGEPGAYGVVTLPKSV 228
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
344-602 |
1.65e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 344 MKALEATNSLYEIINRKPLVENNDDGETLPNIKKIEFKNVRFHYDTRKdvEIYKDLSFTLKEGKTYAFVGESGCGKSTIL 423
Cdd:PLN03073 475 IKALDRLGHVDAVVNDPDYKFEFPTPDDRPGPPIISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTIL 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 424 KLIERLYDPTEGDIivndshnlkdinlkwWRSKigvvsqdpllfsnsiknNIKYSLYSLKDLEAMEnyyeentndtyenk 503
Cdd:PLN03073 553 KLISGELQPSSGTV---------------FRSA-----------------KVRMAVFSQHHVDGLD-------------- 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 504 nfslisnsMTSNELLEMKKEYQTIKDsdvvdvsKKVLIHdfVSSLpdkydTLVGSNASK----LSGGQKQRISIARAIMR 579
Cdd:PLN03073 587 --------LSSNPLLYMMRCFPGVPE-------QKLRAH--LGSF-----GVTGNLALQpmytLSGGQKSRVAFAKITFK 644
|
250 260
....*....|....*....|....
gi 124506379 580 NPKILILDEATSSLD-NKSEYLVQ 602
Cdd:PLN03073 645 KPHILLLDEPSNHLDlDAVEALIQ 668
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
54-305 |
1.76e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 45.16 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 54 RKLLFISFVCAVLSGG---TLPFF----ISVFgVILKNMnlgDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILKT 126
Cdd:cd18540 1 KKLLILLIILMLLVALldaVFPLLtkyaIDHF-ITPGTL---DGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 127 LKleylRSVFY--QDGQF--HDNNPG----SKLRSDLDFYLEQVSSGigtkFITIFTYASSFLGLYIWSLIKNARLTLCI 198
Cdd:cd18540 77 LR----KKAFEhlQTLSFsyFDKTPVgwimARVTSDTQRLGEIISWG----LVDLVWGITYMIGILIVMLILNWKLALIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 199 TCVFPLIYVCGVICNKKV--------KLNKKTSLLYNnntmsiieEALMGIRTVASYCGEKTILNKF-NLSETFYSKYIl 269
Cdd:cd18540 149 LAVVPVLAVVSIYFQKKIlkayrkvrKINSRITGAFN--------EGITGAKTTKTLVREEKNLREFkELTEEMRRASV- 219
|
250 260 270
....*....|....*....|....*....|....*.
gi 124506379 270 KANFVEALHIGLINGLILVSYAFGFWYGTRIIINSA 305
Cdd:cd18540 220 RAARLSALFLPIVLFLGSIATALVLWYGGILVLAGA 255
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
553-637 |
1.83e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.20 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 553 DTLVGSNASKLSGGQKQRISIARAI---------MRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 623
Cdd:PRK13547 136 TALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDP 215
|
90
....*....|....*
gi 124506379 624 S-TIRYANTIFVLSN 637
Cdd:PRK13547 216 NlAARHADRIAMLAD 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
370-621 |
1.85e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 370 ETLP-NIKKIEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIErlydpteGDiivndsHnlkdi 448
Cdd:PRK10938 252 HALPaNEPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT-------GD------H----- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 449 nlkwwrskigvvsqdPLLFSNS----------------IKNNIKYSLYSLKdleaMEnyYEENTNdtyeNKNFsLISNSM 512
Cdd:PRK10938 311 ---------------PQGYSNDltlfgrrrgsgetiwdIKKHIGYVSSSLH----LD--YRVSTS----VRNV-ILSGFF 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 513 TSNELlemkkeYQTIKDSDvvdvskkvlihdfvSSLPDKYDTLVGSNASK-------LSGGQKQRISIARAIMRNPKILI 585
Cdd:PRK10938 365 DSIGI------YQAVSDRQ--------------QKLAQQWLDILGIDKRTadapfhsLSWGQQRLALIVRALVKHPTLLI 424
|
250 260 270
....*....|....*....|....*....|....*.
gi 124506379 586 LDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 621
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
558-619 |
2.02e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 44.63 E-value: 2.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 558 SNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIII 619
Cdd:COG1137 132 SKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLK--ERGIGVLI 191
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1311-1351 |
2.13e-04 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 43.89 E-value: 2.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 124506379 1311 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1351
Cdd:TIGR01189 127 QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1143-1351 |
2.15e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.59 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1143 IYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILknDMTNFQDYQNNNnnslVLKNVNEFSNQSGSAED 1222
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL--DGEHIQHYASKE----VARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1223 YTVfnnnGEILLddinicdynlrdlRNLFSivsQEPMLfnmsiyenIKFGREDAtlEDVKRVSKFAAIDEFIEslpNKYD 1302
Cdd:PRK10253 96 ITV----QELVA-------------RGRYP---HQPLF--------TRWRKEDE--EAVTKAMQATGITHLAD---QSVD 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 124506379 1303 TnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIE 1351
Cdd:PRK10253 143 T--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQIDLLE 184
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
377-437 |
2.24e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 2.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 377 KI--EFKNVRFHYDTRKDVeiyKDLSFTLKEGKTYAFVGESGCGKSTILKL-IERLyDPTEGDI 437
Cdd:PRK11147 317 KIvfEMENVNYQIDGKQLV---KDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQL-QADSGRI 376
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
397-594 |
2.31e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.40 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 397 KDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDshnlKDI-NL---KWWRSKIGVVSQDPLLF----S 468
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG----EDItGLsprERRRLGVAYIPEDRLGRglvpD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 469 NSIKNNIkyslyslkdleAMENYYeentndtyeNKNFSlisnsmtSNELLEMKKeyqtikdsdvvdvskkvlIHDFVSSL 548
Cdd:COG3845 351 MSVAENL-----------ILGRYR---------RPPFS-------RGGFLDRKA------------------IRAFAEEL 385
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 124506379 549 PDKYDTLVGS---NASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:COG3845 386 IEEFDVRTPGpdtPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
830-1095 |
2.43e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 44.89 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 830 YSIYILLIAIAMF--ISETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFdqDKNTPGVLSAHINrDVHLLKTGLVNN 907
Cdd:cd18782 42 YVIGVVMLVAALLeaVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFF--DKRPVGELSTRIS-ELDTIRGFLTGT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 908 I------VIFS--HFIMLFLVSMVMSFyfcpIVAAVLTfIYFINMRVFAVRARltksKEIEKKENMSSgvfafssddemf 979
Cdd:cd18782 119 AlttlldVLFSviYIAVLFSYSPLLTL----VVLATVP-LQLLLTFLFGPILR----RQIRRRAEASA------------ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 980 KDPSFLIqEAFYNMHTVINYGLEDYF-CNLIEKAIDYKNKGQKRRIIvNAALWGFSQSAQLFINSFAYWFGSFLIKRGTI 1058
Cdd:cd18782 178 KTQSYLV-ESLTGIQTVKAQNAELKArWRWQNRYARSLGEGFKLTVL-GTTSGSLSQFLNKLSSLLVLWVGAYLVLRGEL 255
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 124506379 1059 LVDDfmksLFTF-IFTGSYAGKLMSLKGDSE---NAKLSFE 1095
Cdd:cd18782 256 TLGQ----LIAFrILSGYVTGPILRLSTLWQqfqELRVSLE 292
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
558-634 |
2.55e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.55 E-value: 2.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 558 SNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFV 634
Cdd:COG1245 451 KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYiSDRLMV 528
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1311-1351 |
2.73e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 2.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 124506379 1311 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-EKLIE 1351
Cdd:PLN03073 627 TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
1153-1187 |
3.32e-04 |
|
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.
Pssm-ID: 410874 [Multi-domain] Cd Length: 177 Bit Score: 42.91 E-value: 3.32e-04
10 20 30
....*....|....*....|....*....|....*
gi 124506379 1153 SKKTTAIVGETGSGKSTFMNLLLRFYDlKNDHIIL 1187
Cdd:cd01130 11 ARKNILISGGTGSGKTTLLNALLSFIP-PDERIVT 44
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
563-608 |
3.32e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 43.39 E-value: 3.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124506379 563 LSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNL 608
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
836-963 |
3.81e-04 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 44.00 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 836 LIAIAMFISETLKN-YYNNKIGeKVEKTMKRRLFENILYQEMSFFDQDKntPGVLSAHINRDVHLLKTGLVNNI------ 908
Cdd:cd18589 44 LLTIASAVSEFVCDlIYNITMS-RIHSRLQGLVFAAVLRQEIAFFDSNQ--TGDIVSRVTTDTEDMSESLSENLsllmwy 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 909 ---VIFSHFIMLFL-VSMVMSFYFC-PIV---------------------------AAVLTFIYFINMRVFA-------- 948
Cdd:cd18589 121 larGLFLFIFMLWLsPKLALLTALGlPLLllvpkfvgkfqqslavqvqkslaranqVAVETFSAMKTVRSFAneegeaqr 200
|
170
....*....|....*
gi 124506379 949 VRARLTKSKEIEKKE 963
Cdd:cd18589 201 YRQRLQKTYRLNKKE 215
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1140-1370 |
4.66e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.48 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1140 NVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfydlkndhiilkndmtnfqdyqnnnnnslvlknvnefsnqsGS 1219
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI-------------------------------------------AG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1220 AEDYTVfnNNGEILLDDINICDYN--LRDLRNLFsIVSQEPmlFNMSIYENIKFGRedATLEDVKRVSKFAAID--EFIE 1295
Cdd:CHL00131 56 HPAYKI--LEGDILFKGESILDLEpeERAHLGIF-LAFQYP--IEIPGVSNADFLR--LAYNSKRKFQGLPELDplEFLE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1296 SLPNKYDT----------NVGpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTI 1365
Cdd:CHL00131 129 IINEKLKLvgmdpsflsrNVN---EGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSI 204
|
....*
gi 124506379 1366 ITIAH 1370
Cdd:CHL00131 205 ILITH 209
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1280-1368 |
4.93e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1280 DVKRVSKFAAIDEFIE--SLPNKYDTNVG-PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1356
Cdd:PLN03140 985 EVSKEEKMMFVDEVMElvELDNLKDAIVGlPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064
|
90
....*....|..
gi 124506379 1357 IKDKADKTIITI 1368
Cdd:PLN03140 1065 TVDTGRTVVCTI 1076
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1143-1368 |
5.11e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1143 IYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLlrfYDLKNDHIILKNDMTnfqdyqnnnnnslvlknVNefsnqsGSAED 1222
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVL---AERVTTGVITGGDRL-----------------VN------GRPLD 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1223 YTVFNNNGEILLDDINICDYNLRD-LRnlFSIVSQEPMlfNMSIYENIKFgredatledVKRVSKFAAIDEFIESLpnky 1301
Cdd:TIGR00956 832 SSFQRSIGYVQQQDLHLPTSTVREsLR--FSAYLRQPK--SVSKSEKMEY---------VEEVIKLLEMESYADAV---- 894
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 1302 dtnVGPYGKSLSGGQKQRIAIARALLREPKILL-LDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1368
Cdd:TIGR00956 895 ---VGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTI 959
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1310-1356 |
5.53e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 5.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 124506379 1310 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1356
Cdd:PRK11147 439 KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS 485
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
562-635 |
6.80e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.64 E-value: 6.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 562 KLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 635
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLsQWADKINVL 232
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
553-607 |
7.03e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 7.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 553 DTLVG-SNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINN 607
Cdd:PLN03140 1009 DAIVGlPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1315-1370 |
8.18e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 8.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 1315 GQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKDKADKTIITIAH 1370
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLE----DVLNERNSTMIIISH 210
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1262-1403 |
9.09e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.85 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1262 NMSIYENIKFgredatledvkrVSKFAAIDEFIESLpnkYDTNVG--PYGKS---LSGGQKQRIAIARALLRE---PKIL 1333
Cdd:TIGR00630 790 DMTVEEAYEF------------FEAVPSISRKLQTL---CDVGLGyiRLGQPattLSGGEAQRIKLAKELSKRstgRTLY 854
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 1334 LLDEATSSL---DSNseKLIEkTIVDIKDKADkTIITIAHRIASIKRSDKIVVFnNP---DRNGTFVQShGTHDEL 1403
Cdd:TIGR00630 855 ILDEPTTGLhfdDIK--KLLE-VLQRLVDKGN-TVVVIEHNLDVIKTADYIIDL-GPeggDGGGTVVAS-GTPEEV 924
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
516-632 |
9.24e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.60 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 516 ELLEMKKEYQTIkdSDVVDVSKKVlIHDFVSSLP---DKYDTLV---------GSNASKLSGGQKQRISIARAIMR---N 580
Cdd:cd03271 114 ETLEVRYKGKSI--ADVLDMTVEE-ALEFFENIPkiaRKLQTLCdvglgyiklGQPATTLSGGEAQRIKLAKELSKrstG 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 581 PKILILDEATSSL---DnkseylVQKTINNL-----KGNEnriTIIIAHRLSTIRYANTI 632
Cdd:cd03271 191 KTLYILDEPTTGLhfhD------VKKLLEVLqrlvdKGNT---VVVIEHNLDVIKCADWI 241
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
382-597 |
9.35e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 42.24 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 382 NVRFHYdtrKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIivndshnlkdinlkwwrskigvvs 461
Cdd:PRK13540 6 ELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 462 qdpLLFSNSIKnnikyslyslKDLEAMENYYEENTNDTYENKNFSLISNSmtsneLLEMKKEYQTIKDSDVVDVSKKVLI 541
Cdd:PRK13540 59 ---LFERQSIK----------KDLCTYQKQLCFVGHRSGINPYLTLRENC-----LYDIHFSPGAVGITELCRLFSLEHL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 124506379 542 HDFVSSLpdkydtlvgsnaskLSGGQKQRISIARAIMRNPKILILDEATSSLDNKS 597
Cdd:PRK13540 121 IDYPCGL--------------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
538-632 |
9.46e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 538 KVLIHDFVSSLPdkydtlVGSNASKLSGGQKQRISIARAIMRNPK---ILILDEATSSLDNKSEYLVQKTINNLKgNENR 614
Cdd:PRK00635 1681 QALIDNGLGYLP------LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLV-SLGH 1753
|
90
....*....|....*...
gi 124506379 615 ITIIIAHRLSTIRYANTI 632
Cdd:PRK00635 1754 SVIYIDHDPALLKQADYL 1771
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
369-442 |
1.02e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124506379 369 GETLPNiKKIEFKNVRFHYDTRKdveIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDS 442
Cdd:PRK11819 317 GPRLGD-KVIEAENLSKSFGDRL---LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET 386
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1297-1344 |
1.07e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 1.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124506379 1297 LPNKYDTNVG-PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1344
Cdd:TIGR00956 194 LSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
395-598 |
1.13e-03 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 41.71 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 395 IYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDShnlkdinlkwwrskiGVVSQDPLLFSNSI--- 471
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---------------PLDFQRDSIARGLLylg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 472 -KNNIKYSLYSLKDLEAmenYYEENTNDTYEnknfslisnsmtsnELLemkkeyqtikdsDVVDVSKkvlihdfVSSLPd 550
Cdd:cd03231 80 hAPGIKTTLSVLENLRF---WHADHSDEQVE--------------EAL------------ARVGLNG-------FEDRP- 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 124506379 551 kydtlvgsnASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSE 598
Cdd:cd03231 123 ---------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1307-1406 |
1.30e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1307 PYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRSDKIVVFn 1385
Cdd:PRK15093 156 PY--ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLsQWADKINVL- 232
|
90 100
....*....|....*....|.
gi 124506379 1386 npdRNGTFVQShGTHDELLSA 1406
Cdd:PRK15093 233 ---YCGQTVET-APSKELVTT 249
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1312-1346 |
1.36e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 41.48 E-value: 1.36e-03
10 20 30
....*....|....*....|....*....|....*
gi 124506379 1312 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1346
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1290-1382 |
1.41e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 41.30 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1290 IDEFIESlPNKYDTNVgpygKSLSGGQKQRIAIAR--ALLRE---PkILLLDEATSSLD-SNSEKLIEKtivdIKDKADK 1363
Cdd:cd03278 97 VSEIIEA-PGKKVQRL----SLLSGGEKALTALALlfAIFRVrpsP-FCVLDEVDAALDdANVERFARL----LKEFSKE 166
|
90 100
....*....|....*....|
gi 124506379 1364 T-IITIAHRIASIKRSDKIV 1382
Cdd:cd03278 167 TqFIVITHRKGTMEAADRLY 186
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
508-634 |
1.69e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 508 ISNSMTSNELLEMKKEYQTIKDSDVVDVSKkvLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILD 587
Cdd:PRK09580 93 VSNQFFLQTALNAVRSYRGQEPLDRFDFQD--LMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILD 170
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 124506379 588 EATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIRYANTIFV 634
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNSLR-DGKRSFIIVTHYQRILDYIKPDYV 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1229-1372 |
2.35e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 42.69 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1229 NGEILLDDINIcDYNLRDLRNLFSIVSQEPMLFN-MSIYENIKF-----GR--EDATLEdvkrvskfaaIDEFIESLPNK 1300
Cdd:TIGR01257 984 SGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAEHILFyaqlkGRswEEAQLE----------MEAMLEDTGLH 1052
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124506379 1301 YDTNvgPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRI 1372
Cdd:TIGR01257 1053 HKRN--EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
367-599 |
2.39e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.40 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 367 DDGETLPNIK-KI--EFKNVRFHYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIErlyDPTEGdiivndsh 443
Cdd:TIGR00956 45 DYQPTFPNALlKIltRGFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIA---SNTDG-------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 444 nlkdinlkwwrSKIGVVSQdpllfsnsiknnIKYSLYSLKDleaMENYYEENTNDTYENKN-FSlisnSMTSNELLEMKK 522
Cdd:TIGR00956 114 -----------FHIGVEGV------------ITYDGITPEE---IKKHYRGDVVYNAETDVhFP----HLTVGETLDFAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 523 EYQTIKDSdVVDVSKKVLIHDFVS------SLPDKYDTLVGSNASK-LSGGQKQRISIARAIMRNPKILILDEATSSLDN 595
Cdd:TIGR00956 164 RCKTPQNR-PDGVSREEYAKHIADvymatyGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
....
gi 124506379 596 KSEY 599
Cdd:TIGR00956 243 ATAL 246
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1310-1354 |
2.42e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 40.94 E-value: 2.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 124506379 1310 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1354
Cdd:PRK13538 128 RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
1157-1187 |
2.55e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 42.24 E-value: 2.55e-03
10 20 30
....*....|....*....|....*....|.
gi 124506379 1157 TAIVGETGSGKSTFMNLLLRFYDLKNDHIIL 1187
Cdd:COG3451 207 TLILGPSGSGKSFLLKLLLLQLLRYGARIVI 237
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
84-293 |
2.62e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 41.38 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 84 NMNLGDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYLRSVFYQDGQFHDNNPGSKLRSDL-----DF- 157
Cdd:cd18574 34 NGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLtadvqEFk 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 158 -YLEQVSSgIGTKFITIFtyASSFLGLYIWSliknARLTLCITCVFPLIYVCGVICNKKVKLNKKTSLLYNNNTMSIIEE 236
Cdd:cd18574 114 sSFKQCVS-QGLRSVTQT--VGCVVSLYLIS----PKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124506379 237 ALMGIRTVASYCGEKTILNKFNlSETFYSKyilKANFVEALHIGL--------INGLILVSYAFG 293
Cdd:cd18574 187 ALGNIRTVRAFAMEDRELELYE-EEVEKAA---KLNEKLGLGIGIfqglsnlaLNGIVLGVLYYG 247
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1311-1367 |
2.67e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 42.31 E-value: 2.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1311 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1367
Cdd:TIGR01257 2070 TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLT 2126
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
556-608 |
2.98e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 2.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 124506379 556 VGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNL 608
Cdd:NF040905 398 VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL 450
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
560-594 |
4.28e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 4.28e-03
10 20 30
....*....|....*....|....*....|....*
gi 124506379 560 ASKLSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:NF033858 134 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1261-1377 |
5.15e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 40.45 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1261 FNMSI--YENIKFG--------RE-DATLEDVKrvsKFAAIDEFIeslpnkyDTNVgpygKSLSGGQKQRIAIARALLRE 1329
Cdd:COG1134 99 FHPELtgRENIYLNgrllglsrKEiDEKFDEIV---EFAELGDFI-------DQPV----KTYSSGMRARLAFAVATAVD 164
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 124506379 1330 PKILLLDEATSSLDSN-SEKLIEKtIVDIKDKAdKTIITIAHRIASIKR 1377
Cdd:COG1134 165 PDILLVDEVLAVGDAAfQKKCLAR-IRELRESG-RTVIFVSHSMGAVRR 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
563-594 |
5.24e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.19 E-value: 5.24e-03
10 20 30
....*....|....*....|....*....|..
gi 124506379 563 LSGGQKQRISIARAIMRNPKILILDEATSSLD 594
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1262-1414 |
5.38e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1262 NMSIYENIKFgREDATLEDVKRVSKFAAIDEFIESLpnKYDTNVG-PY------GKSLSGGQKQRIAIARAL-------- 1326
Cdd:TIGR00630 435 ELSIREAHEF-FNQLTLTPEEKKIAEEVLKEIRERL--GFLIDVGlDYlslsraAGTLSGGEAQRIRLATQIgsgltgvl 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1327 --LREPKILLLDEATssldsnsEKLIEkTIVDIKDKADkTIITIAHRIASIKRSDKIVvfnnpD------RNGTFVQSHG 1398
Cdd:TIGR00630 512 yvLDEPSIGLHQRDN-------RRLIN-TLKRLRDLGN-TLIVVEHDEDTIRAADYVI-----DigpgagEHGGEVVASG 577
|
170
....*....|....*.
gi 124506379 1399 THDELLSAQDGIYKKY 1414
Cdd:TIGR00630 578 TPEEILANPDSLTGQY 593
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1310-1407 |
5.60e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1310 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSeklIEkTIVDIKDKADKTIITIAH----------RIASIKrSD 1379
Cdd:PRK15064 437 KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES---IE-SLNMALEKYEGTLIFVSHdrefvsslatRIIEIT-PD 511
|
90 100
....*....|....*....|....*...
gi 124506379 1380 KIVVFnnpdrngtfvqsHGTHDELLSAQ 1407
Cdd:PRK15064 512 GVVDF------------SGTYEEYLRSQ 527
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
819-966 |
6.34e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 40.24 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 819 DFANLEYNSNKYsiyiLLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFDQdknTPgvlSAHI-NR-- 895
Cdd:cd18599 53 DNPDLNFYQLVY----GGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDT---TP---TGRIlNRfs 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124506379 896 ------DVHLlkTGLVNNIVIFSHFIMLFLVSMVMSF-YFCpIVAAVLTFIYFINMRVFAVRARltkskEIEKKENMS 966
Cdd:cd18599 123 kdldevDVRL--PFTLENFLQNVLLVVFSLIIIAIVFpWFL-IALIPLAIIFVFLSKIFRRAIR-----ELKRLENIS 192
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1269-1343 |
7.97e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 7.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124506379 1269 IKFGREDATLEDVKRVS--KFAAIDEFIeslpnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1343
Cdd:PRK15439 374 IKPARENAVLERYRRALniKFNHAEQAA---------------RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
1157-1187 |
9.31e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 37.71 E-value: 9.31e-03
10 20 30
....*....|....*....|....*....|.
gi 124506379 1157 TAIVGETGSGKSTFMNLLLRFYDLKNDHIIL 1187
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLPEVRDSVVF 38
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1292-1382 |
9.55e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.52 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 1292 EFIESLP---NKYDT--NVG----PYGKS---LSGGQKQRIAIARALLRE---PKILLLDEATSSLD-SNSEKLIE--KT 1353
Cdd:cd03271 138 EFFENIPkiaRKLQTlcDVGlgyiKLGQPattLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHfHDVKKLLEvlQR 217
|
90 100
....*....|....*....|....*....
gi 124506379 1354 IVDikdkADKTIITIAHRIASIKRSDKIV 1382
Cdd:cd03271 218 LVD----KGNTVVVIEHNLDVIKCADWII 242
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
185-341 |
9.84e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 39.69 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 185 IWSLIK----NARLTLCITCVFPLIYVCGVICNKKV-KLNKKTSLLYNN-NTmsIIEEALMGIRTVASYCGEKTILNKFN 258
Cdd:cd18548 128 IGAIIMafriNPKLALILLVAIPILALVVFLIMKKAiPLFKKVQKKLDRlNR--VVRENLTGIRVIRAFNREDYEEERFD 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124506379 259 LSETFYSKYILKANFVEALHIGLINGLILVSYAFGFWYGTRIIINSATNQypnndfnGA--SVISILLGVLISMFMLTII 336
Cdd:cd18548 206 KANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQV-------GDlvAFINYLMQILMSLMMLSMV 278
|
....*
gi 124506379 337 LPNIT 341
Cdd:cd18548 279 FVMLP 283
|
|
| |
