|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
56-1369 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 1004.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 56 AEAGEMVLVLGYPT---STLFKTL------FH-GKTS-LSYSPPGSikfknNEFKSFSekcPHQIIYNNEQDVHFPFLTV 124
Cdd:TIGR00956 84 IKPGELTVVLGRPGsgcSTLLKTIasntdgFHiGVEGvITYDGITP-----EEIKKHY---RGDVVYNAETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 125 EQTIDFALSCKFDIPKGE-------RDQIRNELLREFGLSHVLKTIVGNDFFRGVSGGERKRISIIETFIANGSVYLWDN 197
Cdd:TIGR00956 156 GETLDFAARCKTPQNRPDgvsreeyAKHIADVYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 198 STKGLDSATALDFLEILRKMAKATRSVNLVRISQASDKIVDKFDKILMLSDSYQLFYGTVDECLTYFRDtLGIEKDPNDC 277
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEK-MGFKCPDRQT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 278 IIEYLTSILNFQFKNKNLGnlsnsSSASVLKTATgEVTKYTYNS--------DFDLYDQwKHSSYyrNIKQQIQGSSIDD 349
Cdd:TIGR00956 315 TADFLTSLTSPAERQIKPG-----YEKKVPRTPQ-EFETYWRNSpeyaqlmkEIDEYLD-RCSES--DTKEAYRESHVAK 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 350 SIKEVDPSdvSPiFNIPLKKQLLFCTKRAFQRSLGDKAYMTAQFISVVIQSLVIGSLFYEIPLTTIGSYSRGSLTFFSIL 429
Cdd:TIGR00956 386 QSKRTRPS--SP-YTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAIL 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 430 FFTFLSLADMPIAFQRQPVVKKQSQLHFYTNWVETLSTTVFDYCFKLCLVIVFSIILYFLAHLQYKAARFFIFLLFLSFY 509
Cdd:TIGR00956 463 FNAFSSLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFIC 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 510 NFCMVSLFALTTLVAPTISVANLFAGILLLAIAMYASYVIYLKNMHPWFVWIAYLNPAMYAMEAILSNELYNLKLDCSeT 589
Cdd:TIGR00956 543 TLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGRRFECS-Q 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 590 IVPRGPTYNDVPFSHKACAWQGATLGNDYVRGRDYLKQGLSYTYHHVWRNFGIIIGFLVFFIACTLFASQYIKPYFNKDE 669
Cdd:TIGR00956 622 YVPSGGGYDNLGVTNKVCTVVGAEPGQDYVDGDDYLKLSFQYYNSHKWRNFGIIIGFTVFFFFVYILLTEFNKGAKQKGE 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 670 IErnnSRLTRWLPFLNKKRGTRSSARNDSKYVGIPKSHsvsssssslsavPYQispSNKEMALNDYNEQpitetVETQKH 749
Cdd:TIGR00956 702 IL---VFRRGSLKRAKKAGETSASNKNDIEAGEVLGST------------DLT---DESDDVNDEKDME-----KESGED 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTVGTKK----LINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGVV-SGEILIDGHPLtdEDAFKR 823
Cdd:TIGR00956 759 IFHWRNLTYEVKIKKekrvILNNVDGWVKPGtLTALMGASGAGKTTLLNVLAERVTTGVItGGDRLVNGRPL--DSSFQR 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 824 SIGFVQQQDLHLDLLSVKESLEISCLLR-------GDGDRaYLDTVSNLLKLPS--DILVA----DLNPTQRKLLSIGVE 890
Cdd:TIGR00956 837 SIGYVQQQDLHLPTSTVRESLRFSAYLRqpksvskSEKME-YVEEVIKLLEMESyaDAVVGvpgeGLNVEQRKRLTIGVE 915
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 891 LVTKPSLLLFLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSKSVISHFDNIFLLKRGGECVFFGPMDDAC--- 967
Cdd:TIGR00956 916 LVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQTVYFGDLGENShti 995
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 968 -GYFMSHDntLVYDKEHDNPADFVIDAVGNSNSSAGKdtaeealtlnkeaIDWSALWESSVEKKLVKKETARLEDDARAS 1046
Cdd:TIGR00956 996 iNYFEKHG--APKCPEDANPAEWMLEVIGAAPGAHAN-------------QDYHEVWRNSSEYQAVKNELDRLEAELSKA 1060
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1047 GVDYTTSLWKQ--PSYLQQLALITRRQYICTKRDMTYVMAKYCLNGGAGLFIGFSFWHIKHNIIGLQDSIFFCFMALCVS 1124
Cdd:TIGR00956 1061 EDDNDPDALSKyaASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGTSLQGLQNQMFAVFMATVLF 1140
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1125 SPLINQIQDKALKTKEVYVAREARSNTYHWTVLLLSQSIIELPLALTSSTLFFVCAFFSCGF-------NNAGWSAGVFF 1197
Cdd:TIGR00956 1141 NPLIQQYLPPFVAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFywnasktGQVHERGVLFW 1220
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1198 LNYMLFAAYYSTLGLWLIYTAPNLQTAAVFVAFIYSFTASFCGVMQPYSLFPTFWKFMYRVSPYTYFVETFVSILLHNWE 1277
Cdd:TIGR00956 1221 LLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLADVP 1300
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1278 IKCDMSEMVPGQPLTGQSCGQFMEAFIEEYGGYLHNKNTFTVCAYCTYTVGDDFLKNENMSYDHVWRNFGIEWAFVGFNF 1357
Cdd:TIGR00956 1301 VTCKVKELLTFNPPSGQTCGEYMKPYLENAGGYLLNPNATDSCSFCQYSYTNDFLEPISSKYSGRWRNFGIFIAFIFFNI 1380
|
1370
....*....|..
gi 6324585 1358 FAMFAGYYLTYV 1369
Cdd:TIGR00956 1381 IATVFFYWLARV 1392
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
748-961 |
1.70e-91 |
|
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: 293.77 E-value: 1.70e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 748 KHIISWKNINYTV----GTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGVVSGEILIDGHPLTDEdaFK 822
Cdd:cd03232 1 GSVLTWKNLNYTVpvkgGKRQLLNNISGYVKPGtLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGRPLDKN--FQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 823 RSIGFVQQQDLHLDLLSVKESLEISCLLRGdgdrayldtvsnllklpsdilvadLNPTQRKLLSIGVELVTKPSLLlFLD 902
Cdd:cd03232 79 RSTGYVEQQDVHSPNLTVREALRFSALLRG------------------------LSVEQRKRLTIGVELAAKPSIL-FLD 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324585 903 EPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSKSVISHFDNIFLLKRGGECVFFG 961
Cdd:cd03232 134 EPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
49-1265 |
2.59e-82 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 297.91 E-value: 2.59e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGYPTS---TLFKTLfHGKTSLSYSPPGSIKFKNNEFKSFSEKCPHQIIYNNeqDVHFPFLTVE 125
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSgktTLLLAL-AGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYISQN--DVHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 126 QTIDFALSC-----KFDI--------------PKGERDQ--------------IRNELLREFGLSHVLKTIVGNDFFRGV 172
Cdd:PLN03140 258 ETLDFSARCqgvgtRYDLlselarrekdagifPEAEVDLfmkatamegvksslITDYTLKILGLDICKDTIVGDEMIRGI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 173 SGGERKRISIIETFIANGSVYLWDNSTKGLDSATALDFLEILRKMAKATRSVNLVRISQASDKIVDKFDKILMLSDSyQL 252
Cdd:PLN03140 338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDDIILLSEG-QI 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 253 FYgtvdecltyfrdtlgieKDPNDCIIEYLTSilnFQFKNKNlgnlsNSSSASVLKtatgEVTkytynSDFDLYDQWKHS 332
Cdd:PLN03140 417 VY-----------------QGPRDHILEFFES---CGFKCPE-----RKGTADFLQ----EVT-----SKKDQEQYWADR 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 333 SY-YRNI---------KQQIQGSSIDDSIKEvdPSDVSPIFNIPLKKQLLFCTKRAFQRSLGDKAYM---------TAQF 393
Cdd:PLN03140 463 NKpYRYIsvsefaerfKSFHVGMQLENELSV--PFDKSQSHKAALVFSKYSVPKMELLKACWDKEWLlmkrnafvyVFKT 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 394 ISVVIQSLVIGSLFYEIPLTTI----GSYSRGSLTFfSILFFTFLSLADMPIAFQRQPVVKKQSQLHFYTNWVETLSTTV 469
Cdd:PLN03140 541 VQIIIVAAIASTVFLRTEMHTRneedGALYIGALLF-SMIINMFNGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFL 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 470 FDYCFKLCLVIVFSIILYFLAHLQYKAARFFIFLLFLSFYNFCMVSLFALTTLVAPTISVANLFAGILLLAIAMYASYVI 549
Cdd:PLN03140 620 LGIPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFIL 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 550 YLKNMHPWFVWIAYLNPAMYAMEAILSNELYnlkldcsetiVPRgptyndvpFSHKACAWQGATLGNDYVRGRDYLKQGL 629
Cdd:PLN03140 700 PKGEIPNWWEWAYWVSPLSYGFNALAVNEMF----------APR--------WMNKMASDNSTRLGTAVLNIFDVFTDKN 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 630 SYtyhhvWRNFGIIIGFLVFFIACTLFASQYIKPYFNKDEIERNNSRLTRWLPFLNKKRGTRSSARNDSKYVGIPKSHSV 709
Cdd:PLN03140 762 WY-----WIGVGALLGFTILFNVLFTLALTYLNPLGKKQAIISEETAEEMEGEEDSIPRSLSSADGNNTREVAIQRMSNP 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 710 SSSSSSLSAvpyQISPSN-----KEMALndyneqPITETVetqkhiISWKNINYTVGTKK-------------LINNASG 771
Cdd:PLN03140 837 EGLSKNRDS---SLEAANgvapkRGMVL------PFTPLA------MSFDDVNYFVDMPAemkeqgvtedrlqLLREVTG 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 772 FISSG-LTALMGESGAGKTTLLNVLSQRVETGVVSGEILIDGHPlTDEDAFKRSIGFVQQQDLHLDLLSVKESLEISCLL 850
Cdd:PLN03140 902 AFRPGvLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFP-KKQETFARISGYCEQNDIHSPQVTVRESLIYSAFL 980
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 851 R------GDGDRAYLDTVSNLLKLPS--DILVA-----DLNPTQRKLLSIGVELVTKPSLLlFLDEPTSGLDAEAALTIV 917
Cdd:PLN03140 981 RlpkevsKEEKMMFVDEVMELVELDNlkDAIVGlpgvtGLSTEQRKRLTIAVELVANPSII-FMDEPTSGLDARAAAIVM 1059
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 918 KFLKQLSLQGQAIFCTIHQPSKSVISHFDNIFLLKRGGECVFFGPMDDAcgyfmSHDNTLVYD--------KEHDNPADF 989
Cdd:PLN03140 1060 RTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYSGPLGRN-----SHKIIEYFEaipgvpkiKEKYNPATW 1134
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 990 VIDAvgnsnSSAGkdtAEEALtlnkeAIDWSALWESSV----EKKLVKKETArleDDARASGV----DYTTSLWKQ-PSY 1060
Cdd:PLN03140 1135 MLEV-----SSLA---AEVKL-----GIDFAEHYKSSSlyqrNKALVKELST---PPPGASDLyfatQYSQSTWGQfKSC 1198
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1061 LQqlalitrRQYICTKRDMTYVMAKYCLNGGAGLFIGFSFWHIKHN---------IIG-LQDSIFFCFMALCVSsplinq 1130
Cdd:PLN03140 1199 LW-------KQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGTKrsnandltmVIGaMYAAVLFVGINNCST------ 1265
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1131 IQDKALKTKEVYVaREARSNTYHWTVLLLSQSIIELPLALTSSTLFFVCAFFSCGFNnagWSAGVF----FLNYMLFaAY 1206
Cdd:PLN03140 1266 VQPMVAVERTVFY-RERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFE---WTAAKFfwfyFISFFSF-LY 1340
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324585 1207 YSTLGLWLIYTAPNLQTAAVFVAFIYSFTASFCGVMQPYSLFPTFWKFMYRVSPYTYFV 1265
Cdd:PLN03140 1341 FTYYGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTV 1399
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
49-255 |
1.55e-75 |
|
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: 249.10 E-value: 1.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGYPTS---TLFKTLfHGKTSLSYSPPGSIKFKNNEFKSFSEKCPHQIIYNNEQDVHFPFLTVE 125
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSgcsTLLKAL-ANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 126 QTIDFALSCKfdipkgerdqirnellrefglshvlktivGNDFFRGVSGGERKRISIIETFIANGSVYLWDNSTKGLDSA 205
Cdd:cd03233 102 ETLDFALRCK-----------------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6324585 206 TALDFLEILRKMAKATRSVNLVRISQASDKIVDKFDKILMLSDSYQLFYG 255
Cdd:cd03233 153 TALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
751-961 |
3.41e-64 |
|
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: 216.26 E-value: 3.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTV------GTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGVVSGEILIDGHPLtDEDAFKR 823
Cdd:cd03213 4 LSFRNLTVTVksspskSGKQLLKNVSGKAKPGeLTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPL-DKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 824 SIGFVQQQDLHLDLLSVKESLEISCLLRGdgdrayldtvsnllklpsdilvadLNPTQRKLLSIGVELVTKPSlLLFLDE 903
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRG------------------------LSGGERKRVSIALELVSNPS-LLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6324585 904 PTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSKSVISHFDNIFLLKRgGECVFFG 961
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
761-1294 |
6.11e-60 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 217.99 E-value: 6.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 761 GTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGV-VSGEILIDGHPLtDEDAFKRSIGFVQQQDLHLDLL 838
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGeLLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 839 SVKESLEISCLLR------GDGDRAYLDTVSNLLKLPS--------DILVADLNPTQRKLLSIGVELVTKPSLLlFLDEP 904
Cdd:TIGR00955 115 TVREHLMFQAHLRmprrvtKKEKRERVDEVLQALGLRKcantrigvPGRVKGLSGGERKRLAFASELLTDPPLL-FCDEP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 905 TSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSKSVISHFDNIFLLKrGGECVFFGPMDDACGYFmshDNTLVYDKEHD 984
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMA-EGRVAYLGSPDQAVPFF---SDLGHPCPENY 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 985 NPADFVID--AVGNSNSSAGKDTAeEALTLNKEAIDWSALWESSVeKKLVKKETARLEDDARASGVDYTTSLWKqpsylq 1062
Cdd:TIGR00955 270 NPADFYVQvlAVIPGSENESRERI-EKICDSFAVSDIGRDMLVNT-NLWSGKAGGLVKDSENMEGIGYNASWWT------ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1063 QLALITRRQYICTKRDMTYVMAKYCLNGGAGLFIGFSFWHIKHNIIGLQD---SIFFC--FMALCVSSPLINQIqdkalk 1137
Cdd:TIGR00955 342 QFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNingALFLFltNMTFQNVFPVINVF------ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1138 TKEVYV-AREARSNTYHWTVLLLSQSIIELPLALTSSTLFFVCAFFSCGFnNAGWSAGVFFLNYMLFAAYYST-LGLWLI 1215
Cdd:TIGR00955 416 TAELPVfLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGL-RSGATHFLTFLFLVTLVANVATsFGYLIS 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1216 YTAPNLQTA-AVFVAFIYSFTAsFCGVMQPYSLFPTFWKFMYRVSpytYFVETFVSILLHNW----EIKCDMSEMVPGQP 1290
Cdd:TIGR00955 495 CAFSSTSMAlTVGPPFVIPFLL-FGGFFINSDSIPVYFKWLSYLS---WFRYGNEGLLINQWsdvdNIECTSANTTGPCP 570
|
....
gi 6324585 1291 LTGQ 1294
Cdd:TIGR00955 571 SSGE 574
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
762-961 |
6.30e-45 |
|
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: 162.44 E-value: 6.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 762 TKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVE-TGVVSGEILIDGHPLtDEDAFKRSIGFVQQQDLHLDLLS 839
Cdd:cd03234 19 YARILNDVSLHVESGqVMAILGSSGSGKTTLLDAISGRVEgGGTTSGQILFNGQPR-KPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 840 VKESLEISCLLRG-----DGDRAYLDTVSNLLKLP----SDILVADLNPTQRKLLSIGVELVTKPSLLlFLDEPTSGLDA 910
Cdd:cd03234 98 VRETLTYTAILRLprkssDAIRKKRVEDVLLRDLAltriGGNLVKGISGGERRRVSIAVQLLWDPKVL-ILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6324585 911 EAALTIVKFLKQLSLQGQAIFCTIHQPSKSVISHFDNIFLLKRgGECVFFG 961
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSS-GEIVYSG 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
750-961 |
8.97e-36 |
|
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: 135.08 E-value: 8.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTVG----TKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGV-VSGEILIDGHPLtDEDA--F 821
Cdd:cd03233 3 TLSWRNISFTTGkgrsKIPILKDFSGVVKPGeMVLVLGRPGSGCSTLLKALANRTEGNVsVEGDIHYNGIPY-KEFAekY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 822 KRSIGFVQQQDLHLDLLSVKESLEISCLLRGDgdrAYLDTVSNllklpsdilvadlnpTQRKLLSIGVELVTKPSLLLFl 901
Cdd:cd03233 82 PGEIIYVSEEDVHFPTLTVRETLDFALRCKGN---EFVRGISG---------------GERKRVSIAEALVSRASVLCW- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324585 902 DEPTSGLDAEAALTIVKFLKQLS-LQGQAIFCTIHQPSKSVISHFDNIFLLkRGGECVFFG 961
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMAdVLKTTTFVSLYQASDEIYDLFDKVLVL-YEGRQIYYG 202
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1067-1271 |
1.99e-34 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 131.24 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1067 ITRRQYICTKRDMTYVMAKYCLNGGAGLFIGFSFWHIKHNIIGLQDSIFFCFMALCVSSPLINQIQDKALKTKEVYVaRE 1146
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLY-RE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1147 ARSNTYHWTVLLLSQSIIELPLALTSSTLFFVCAFFSCGFNNAGWSAGVFFLNYMLFAAYYSTLGLWLIYTAPNLQTAAV 1226
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6324585 1227 FVAFIYSFTASFCGVMQPYSLFPTFWKFMYRVSPYTYFVETFVSI 1271
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
374-577 |
2.27e-34 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 131.24 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 374 CTKRAFQRSLGDKAYMTAQFISVVIQSLVIGSLFYEIPlTTIGSYSRGSLTFFSILFFTFLSLADM-PIAFQRQPVVKKQ 452
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG-NQQGGLNRPGLLFFSILFNAFSALSGIsPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 453 SQLHFYTNWVETLSTTVFDYCFKLCLVIVFSIILYFLAHLQYKAARFFIFLLFLSFYNFCMVSLFALTTLVAPTISVANL 532
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6324585 533 FAGILLLAIAMYASYVIYLKNMHPWFVWIAYLNPAMYAMEAILSN 577
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
49-578 |
1.57e-32 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 135.56 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGYP---TSTLFKTL-FHGKTSLSYSPPGSIKFKNNEFKSFSEKCPhqiiYNNEQDVHFPFLTV 124
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSgagKTTLMNALaFRSPKGVKGSGSVLLNGMPIDAKEMRAISA----YVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 125 EQTIDFA--LSCKFDIPKGERDQIRNELLREFGLSHVLKTIVGN-DFFRGVSGGERKRISIIETFIANGSVYLWDNSTKG 201
Cdd:TIGR00955 117 REHLMFQahLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 202 LDSATALDFLEILRKMAKATRSVnLVRISQASDKIVDKFDKILMLSDSYQLFYGTVDECLTYFRDtLGIEKDPN----DC 277
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTI-ICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSD-LGHPCPENynpaDF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 278 IIEYLTSILNFQfknknlgnlsNSSSASVLKtatgevtkytynsdfdLYDQWKHSSYYRNIKQQIQGSSiDDSIKEVDPS 357
Cdd:TIGR00955 275 YVQVLAVIPGSE----------NESRERIEK----------------ICDSFAVSDIGRDMLVNTNLWS-GKAGGLVKDS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 358 DVSPI--FNIPLKKQLLFCTKRAFQRSLGDKAYMTAQFISVVIQSLVIGSLFYEIPLTTIGSYSRGSLTFFSILFFTFL- 434
Cdd:TIGR00955 328 ENMEGigYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQn 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 435 SLADMPIAFQRQPVVKKQSQLHFYTNWVETLSTTVFDYCFKLCLVIVFSIILYFLAHLQYKAarffifllflsfYNFC-M 513
Cdd:TIGR00955 408 VFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGA------------THFLtF 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 514 VSLFALTTLVA-----------PTISVANLFAGILLLAIAMYASYVIYLKNMHPWFVWIAYLNPAMYAMEAILSNE 578
Cdd:TIGR00955 476 LFLVTLVANVAtsfgyliscafSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQ 551
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
759-992 |
3.71e-31 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 131.54 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 759 TVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGVVSGEILIDGHPLTDEdAFKRsIGFVQQQDLHLDL 837
Cdd:PLN03211 77 QIQERTILNGVTGMASPGeILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQ-ILKR-TGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 838 LSVKESLEISCLLR-------GDGDRAYLDTVSNL--LKLPSDIL----VADLNPTQRKLLSIGVELVTKPSLLLfLDEP 904
Cdd:PLN03211 155 LTVRETLVFCSLLRlpksltkQEKILVAESVISELglTKCENTIIgnsfIRGISGGERKRVSIAHEMLINPSLLI-LDEP 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 905 TSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSKSVISHFDNIFLLKRgGECVFFGPMDDACGYFMSHDNTLVYDKehd 984
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSE-GRCLFFGKGSDAMAYFESVGFSPSFPM--- 309
|
....*...
gi 6324585 985 NPADFVID 992
Cdd:PLN03211 310 NPADFLLD 317
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
751-967 |
3.82e-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: 123.04 E-value: 3.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLT-DEDAFKRSI 825
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGeITGLLGPNGAGKTTLLRMLA-----GLLkpdSGSILIDGEDVRkEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 826 GFVQQQD-LHlDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKL-----PSDILVADLNPTQRKLLSIGVELVTKPSLLL 899
Cdd:COG4555 77 GVLPDERgLY-DRLTVRENIRYFAELYGLFDEELKKRIEELIELlgleeFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324585 900 fLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPskSVISH-FDNIFLLKRgGECVFFGPMDDAC 967
Cdd:COG4555 156 -LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIM--QEVEAlCDRVVILHK-GKVVAQGSLDELR 220
|
|
| PDR_CDR |
pfam06422 |
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters ... |
591-670 |
4.01e-30 |
|
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters comprising extracellular loop 3, transmembrane segment 6 and linker region.
Pssm-ID: 461906 [Multi-domain] Cd Length: 92 Bit Score: 114.87 E-value: 4.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 591 VPRGPTYNDVPFSHKACAWQGATLGNDYVRGRDYLKQGLSYTYHHVWRNFGIIIGFLVFFIACTLFASQYIKPYFNKDEI 670
Cdd:pfam06422 1 VPSGPGYENVSGANQVCAVVGAVPGQTFVSGDDYLAASYGYSYSHLWRNFGILIAFWIFFLALYLIATEYNSAAKSKGEV 80
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
49-255 |
3.17e-29 |
|
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: 116.11 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLFHGKTSLSYSppGSIKFKNNEFKSFSEKCphQIIYNNEQDVHFPFLTV 124
Cdd:cd03213 25 LKNVSGKAKPGELTAIMG-PSgagkSTLLNALAGRRTGLGVS--GEVLINGRPLDKRSFRK--IIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 125 EQTIDFALSCkfdipkgerdqirnellrefglshvlktivgndffRGVSGGERKRISIIETFIANGSVYLWDNSTKGLDS 204
Cdd:cd03213 100 RETLMFAAKL-----------------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6324585 205 ATALDFLEILRKMAKATRSVnLVRISQASDKIVDKFDKILMLSDSYQLFYG 255
Cdd:cd03213 145 SSALQVMSLLRRLADTGRTI-ICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
751-965 |
4.28e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 117.09 E-value: 4.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDGHPL-TDEDAFKRSI 825
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGeIFGLLGPNGAGKTTTIRML-----LGLLrptSGEVRVLGEDVaRDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 826 GFVQQQDLHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKL-----PSDILVADLNPTQRKLLSIGVELVTKPSLLlF 900
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELfgltdAADRKVGTLSGGMKQRLGLALALLHDPELL-I 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324585 901 LDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSkSVISHFDNIFLLKRgGECVFFGPMDD 965
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLE-EAERLCDRVAIIDK-GRIVADGTPDE 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
754-954 |
1.09e-26 |
|
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: 107.87 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDGHPLTDE-DAFKRSIGFV 828
Cdd:cd03230 4 RNLSKRYGKKTALDDISLTVEKGeIYGLLGPNGAGKTTLIKII-----LGLLkpdSGEIKVLGKDIKKEpEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 829 QQQDLHLDLLSVKESLEIScllRGdgdrayldtvsnllklpsdilvadlnptQRKLLSIGVELVTKPSlLLFLDEPTSGL 908
Cdd:cd03230 79 PEEPSLYENLTVRENLKLS---GG----------------------------MKQRLALAQALLHDPE-LLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6324585 909 DAEAALTIVKFLKQLSLQGQAIFCTIHQPSkSVISHFDNIFLLKRG 954
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNG 171
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
49-247 |
2.82e-26 |
|
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: 108.51 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGYPTStlfktlfhGKTSL----------SYSPPGSIKFKNNEFKsfsekcPHQ----IIYNNE 114
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGS--------GKTTLldaisgrvegGGTTSGQILFNGQPRK------PDQfqkcVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 115 QDVHFPFLTVEQTIDFALSCKfdIPKGERDQIRNELLREFGLSHVLKTIVGNDFFRGVSGGERKRISIIETFIANGSVYL 194
Cdd:cd03234 89 DDILLPGLTVRETLTYTAILR--LPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6324585 195 WDNSTKGLDSATALDFLEILRKMAKATRSVnLVRISQASDKIVDKFDKILMLS 247
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIV-ILTIHQPRSDLFRLFDRILLLS 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
754-954 |
8.78e-26 |
|
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: 104.63 E-value: 8.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVEtgVVSGEILIDGHPLTDED--AFKRSIGFVQQ 830
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGeIVALVGPNGSGKSTLLRAIAGLLK--PTSGEILIDGKDIAKLPleELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 831 qdlhldlLSVkesleiscllrgdGdrayldtvsnllklpsdilvadlnptQRKLLSIGVELVTKPSLLLfLDEPTSGLDA 910
Cdd:cd00267 81 -------LSG-------------G--------------------------QRQRVALARALLLNPDLLL-LDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6324585 911 EAALTIVKFLKQLSLQGQAIFCTIHQPSkSVISHFDNIFLLKRG 954
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPE-LAELAADRVIVLKDG 156
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
751-954 |
7.26e-24 |
|
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: 101.41 E-value: 7.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKL----INNASGFISSG-LTALMGESGAGKTTLLNVLS--QRvetgVVSGEILIDGHPLT-----DE 818
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqaLKGVSLSIEKGeFVAIVGPSGSGKSTLLNILGglDR----PTSGEVRVDGTDISklsekEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 819 DAFKR-SIGFVQQQDLHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLLK---LPSdilVADLNPTQrklLSIGvE---- 890
Cdd:cd03255 77 AAFRRrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLErvgLGD---RLNHYPSE---LSGG-Qqqrv 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 891 -----LVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLS-LQGQAIFCTIHQPskSVISHFDNIFLLKRG 954
Cdd:cd03255 150 aiaraLANDPKIIL-ADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP--ELAEYADRIIELRDG 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
766-906 |
1.34e-23 |
|
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: 98.10 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 766 INNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETgvVSGEILIDGHPLTDED--AFKRSIGFVQQQDLHLDLLSVKE 842
Cdd:pfam00005 1 LKNVSLTLNPGeILALVGPNGAGKSTLLKLIAGLLSP--TEGTILLDGQDLTDDErkSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324585 843 SLEISCLLRGDGDRAYLDTVSNLLKL---------PSDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTS 906
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDARAEEALEKlglgdladrPVGERPGTLSGGQRQRVAIARALLTKPKLLL-LDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
754-954 |
1.88e-23 |
|
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: 99.85 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGT--KKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVetGVVSGEILIDGHPLTDEDAFKRS--IGFV 828
Cdd:cd03225 3 KNLSFSYPDgaRPALDDISLTIKKGeFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSLKELRrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 829 -QQQDLHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKLPSDILVADLNPT-----QRKLLSIGVELVTKPSLLLfLD 902
Cdd:cd03225 81 fQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFtlsggQKQRVAIAGVLAMDPDILL-LD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6324585 903 EPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSKsVISHFDNIFLLKRG 954
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDL-LLELADRVIVLEDG 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
49-264 |
6.75e-22 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 102.27 E-value: 6.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPTSTlfktlfhGKTSLSYSPPGSIKFKNNEFKSFSE--KCPHQII----YNNEQDVHFPFL 122
Cdd:PLN03211 84 LNGVTGMASPGEILAVLG-PSGS-------GKSTLLNALAGRIQGNNFTGTILANnrKPTKQILkrtgFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 123 TVEQTIDFA--LSCKFDIPKGERDQIRNELLREFGLSHVLKTIVGNDFFRGVSGGERKRISIIETFIANGSVYLWDNSTK 200
Cdd:PLN03211 156 TVRETLVFCslLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324585 201 GLDSATALDFLEILRKMAKATRSVnLVRISQASDKIVDKFDKILMLSDSYQLFYGTVDECLTYF 264
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTI-VTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYF 298
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
751-961 |
9.79e-22 |
|
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: 94.95 E-value: 9.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSGLTALMGESGAGKTTLLNVLSQRVETgvVSGEILIDGHPLT-DEDAFKRSIGFVQ 829
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPP--SSGTIRIDGQDVLkQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 830 QQDLHLDLLSVKESLEISCLLRG--DGD-RAYLDTVSNLLKLP--SDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEP 904
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGipSKEvKARVDEVLELVNLGdrAKKKIGSLSGGMRRRVGIAQALVGDPSILI-VDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6324585 905 TSGLDAEAALTIVKFLKQLSLQGQAIFCTiHQPSkSVISHFDNIFLLKrGGECVFFG 961
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGEDRIVILST-HIVE-DVESLCNQVAVLN-KGKLVFEG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
778-954 |
1.32e-21 |
|
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: 94.88 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 778 TALMGESGAGKTTLLNVLSQRVEtgVVSGEILIDGHPL-TDEDAFKRSIGFVQQQDLHLDLLSVKESLEISCLLRGDGDR 856
Cdd:cd03263 31 FGLLGHNGAGKTTTLKMLTGELR--PTSGTAYINGYSIrTDRKAARQSLGYCPQFDALFDELTVREHLRFYARLKGLPKS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 857 AYLDTVSNLLK---LPS--DILVADLNPTQRKLLSIGVELVTKPSlLLFLDEPTSGLDAEAALTIVKFLKQLslqgqaif 931
Cdd:cd03263 109 EIKEEVELLLRvlgLTDkaNKRARTLSGGMKRKLSLAIALIGGPS-VLLLDEPTSGLDPASRRAIWDLILEV-------- 179
|
170 180 190
....*....|....*....|....*....|...
gi 6324585 932 ctihQPSKSVI--SHF--------DNIFLLKRG 954
Cdd:cd03263 180 ----RKGRSIIltTHSmdeaealcDRIAIMSDG 208
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
750-954 |
1.62e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 94.73 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTVGTKKL----INNASGFISSG-LTALMGESGAGKTTLLNVLS--QRVEtgvvSGEILIDGHPLTDEDAFK 822
Cdd:COG1136 4 LLELRNLTKSYGTGEGevtaLRGVSLSIEAGeFVAIVGPSGSGKSTLLNILGglDRPT----SGEVLIDGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 823 RS------IGFVQQQdLHL-DLLSVKESLEISCLLRGDGDRAYLDTVSNLLKlpsdiLV-----ADLNPTQrklLSIGvE 890
Cdd:COG1136 80 LArlrrrhIGFVFQF-FNLlPELTALENVALPLLLAGVSRKERRERARELLE-----RVglgdrLDHRPSQ---LSGG-Q 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324585 891 ---------LVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQ-GQAIFCTIHQPskSVISHFDNIFLLKRG 954
Cdd:COG1136 150 qqrvaiaraLVNRPKLIL-ADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDP--ELAARADRVIRLRDG 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
749-975 |
4.90e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 94.00 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 749 HIISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDGHPLTDEdafKRS 824
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGeFVAIVGPNGAGKSTLLKAI-----LGLLpptSGTVRLFGKPPRRA---RRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 825 IGFV-QQQDLHLDL-LSVKESLEISCLLR-------GDGDRAY----LDTVsNLLKLpSDILVADLNPTQRKLLSIGVEL 891
Cdd:COG1121 77 IGYVpQRAEVDWDFpITVRDVVLMGRYGRrglfrrpSRADREAvdeaLERV-GLEDL-ADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 892 VTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSkSVISHFDNIFLLKRGgeCVFFGPMDDacgyFM 971
Cdd:COG1121 155 AQDPDLLL-LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLG-AVREYFDRVLLLNRG--LVAHGPPEE----VL 226
|
....
gi 6324585 972 SHDN 975
Cdd:COG1121 227 TPEN 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
754-952 |
4.28e-20 |
|
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: 90.01 E-value: 4.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVG-TKKLINNASGFISSG-LTALMGESGAGKTTLLNVLS--QRVEtgvvSGEILIDGHPLTDEDAFkRSIGFVQ 829
Cdd:cd03226 3 ENISFSYKkGTEILDDLSLDLYAGeIIALTGKNGAGKTTLAKILAglIKES----SGSILLNGKPIKAKERR-KSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 830 QQ-DLHLDLLSVKESLeiscLLRGDGDRAYLDTVSNLLKLPSDILVADLNPT-----QRKLLSIGVELVTKPSLLLFlDE 903
Cdd:cd03226 78 QDvDYQLFTDSVREEL----LLGLKELDAGNEQAETVLKDLDLYALKERHPLslsggQKQRLAIAAALLSGKDLLIF-DE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6324585 904 PTSGLDAEAALTIVKFLKQLSLQGQAIFctihqpsksVISHfDNIFLLK 952
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVI---------VITH-DYEFLAK 191
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
754-954 |
5.50e-20 |
|
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: 88.78 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETgvVSGEILIDGHPLTDED----AFKRSIGFV 828
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGeIVALLGPSGSGKSTLLRCIAGLEEP--DSGSILIDGEDLTDLEdelpPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 829 QQQDLHLDLLSVKESLEIscLLRGdGdrayldtvsnllklpsdilvadlnptQRKLLSIGVELVTKPSLLLfLDEPTSGL 908
Cdd:cd03229 82 FQDFALFPHLTVLENIAL--GLSG-G--------------------------QQQRVALARALAMDPDVLL-LDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6324585 909 DAEAALTIVKFLKQL-SLQGQAIFCTIHQPSkSVISHFDNIFLLKRG 954
Cdd:cd03229 132 DPITRREVRALLKSLqAQLGITVVLVTHDLD-EAARLADRVVVLRDG 177
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
751-954 |
6.10e-20 |
|
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: 88.59 E-value: 6.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNIN--YTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVEtgVVSGEILIDGHPLTDED--AFKRSI 825
Cdd:cd03228 1 IEFKNVSfsYPGRPKPVLKDVSLTIKPGeKVAIVGPSGSGKSTLLKLLLRLYD--PTSGEILIDGVDLRDLDleSLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 826 GFVqQQDLHLDLLSVKEsleiscllrgdgdrayldtvsNLLklpSDilvadlnpTQRKLLSIGVELVTKPSLLLfLDEPT 905
Cdd:cd03228 79 AYV-PQDPFLFSGTIRE---------------------NIL---SG--------GQRQRIAIARALLRDPPILI-LDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6324585 906 SGLDAEAALTIVKFLKQLSlQGQAIFCTIHQPskSVISHFDNIFLLKRG 954
Cdd:cd03228 125 SALDPETEALILEALRALA-KGKTVIVIAHRL--STIRDADRIIVLDDG 170
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
751-967 |
1.20e-19 |
|
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: 89.31 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTV-GTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTDED--AFKR 823
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGeFVAIIGPNGSGKSTLLRLLN-----GLLkptSGEVLVDGKDITKKNlrELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 824 SIGFV-QQQDLHLDLLSVKE----SLEISCLLRGDGDR---AYLDTVsNLLKLpsdilvADLNPT-----QRKLLSI-GV 889
Cdd:COG1122 76 KVGLVfQNPDDQLFAPTVEEdvafGPENLGLPREEIRErveEALELV-GLEHL------ADRPPHelsggQKQRVAIaGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324585 890 eLVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSKsVISHFDNIFLLKRgGECVFFGPMDDAC 967
Cdd:COG1122 149 -LAMEPEVLV-LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDD-GRIVADGTPREVF 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
49-199 |
1.63e-19 |
|
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: 86.55 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLfhgkTSLSYSPPGSIKFKNNEFKSFSEKCPHQII-YNNEQDVHFPFLT 123
Cdd:pfam00005 1 LKNVSLTLNPGEILALVG-PNgagkSTLLKLI----AGLLSPTEGTILLDGQDLTDDERKSLRKEIgYVFQDPQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 124 VEQTIDFALSCKFdIPKGERDQIRNELLREFGLSHVLKTIVGNdFFRGVSGGERKRISIIETFIANGSVYLWDNST 199
Cdd:pfam00005 76 VRENLRLGLLLKG-LSKREKDARAEEALEKLGLGDLADRPVGE-RPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
754-961 |
1.78e-19 |
|
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: 88.36 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLnvlsqRVETGVV---SGEILIDGHPLTDEDafkRSIGFVQ 829
Cdd:cd03235 3 EDLTVSYGGHPVLEDVSFEVKPGeFLAIVGPNGAGKSTLL-----KAILGLLkptSGSIRVFGKPLEKER---KRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 830 QQdLHLDL---LSVKESLEISCLLRGDGDRAY-----------LDTVsNLLKLpSDILVADLNPTQRKLLSIGVELVTKP 895
Cdd:cd03235 75 QR-RSIDRdfpISVRDVVLMGLYGHKGLFRRLskadkakvdeaLERV-GLSEL-ADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 896 SLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSkSVISHFDNIFLLKRGGecVFFG 961
Cdd:cd03235 152 DLLL-LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLLNRTV--VASG 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
751-954 |
2.24e-19 |
|
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: 94.52 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNIN--YTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLsQRVETgVVSGEILIDGHPLT--DEDAFKRSI 825
Cdd:COG2274 474 IELENVSfrYPGDSPPVLDNISLTIKPGeRVAIVGRSGSGKSTLLKLL-LGLYE-PTSGRILIDGIDLRqiDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 826 GFVQQQ---------------DLHLDLLSVKESLEISCLlrgdgdrayLDTVSnllKLPS--DILVAD----LNPTQRKL 884
Cdd:COG2274 552 GVVLQDvflfsgtirenitlgDPDATDEEIIEAARLAGL---------HDFIE---ALPMgyDTVVGEggsnLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 885 LSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLsLQGQAIFCTIHQPskSVISHFDNIFLLKRG 954
Cdd:COG2274 620 LAIARALLRNPRILI-LDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRL--STIRLADRIIVLDKG 685
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
754-961 |
5.66e-19 |
|
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: 85.95 E-value: 5.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGvvSGEILIDGHPLTDEDA--FKRSIGFVQQ 830
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGeIVGILGPNGAGKSTLLKTLAGLLKPS--SGEILLDGKDLASLSPkeLARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 831 qdlhldllsVKESLEISCLLrgdgDRaYLDTVSNllklpsdilvadlnpTQRKLLSIGVELVTKPSLLLfLDEPTSGLDA 910
Cdd:cd03214 81 ---------ALELLGLAHLA----DR-PFNELSG---------------GERQRVLLARALAQEPPILL-LDEPTSHLDI 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6324585 911 EAALTIVKFLKQLSLQ-GQAIFCTIHQPSkSVISHFDNIFLLKrGGECVFFG 961
Cdd:cd03214 131 AHQIELLELLRRLARErGKTVVMVLHDLN-LAARYADRVILLK-DGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
773-937 |
9.47e-19 |
|
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: 85.99 E-value: 9.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 773 ISSG-LTALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTD-EDAFKRSIGFVQQQDLHLDLLSVKESLEIS 847
Cdd:COG4133 25 LAAGeALALTGPNGSGKTTLLRILA-----GLLppsAGEVLWNGEPIRDaREDYRRRLAYLGHADGLKPELTVRENLRFW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 848 CLLRG-DGDRAYLDTVSNLLKLPS--DILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLS 924
Cdd:COG4133 100 AALYGlRADREAIDEALEAVGLAGlaDLPVRQLSAGQKRRVALARLLLSPAPLWL-LDEPFTALDAAGVALLAELIAAHL 178
|
170
....*....|...
gi 6324585 925 LQGQAIFCTIHQP 937
Cdd:COG4133 179 ARGGAVLLTTHQP 191
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
778-965 |
1.14e-18 |
|
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: 86.33 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 778 TALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTDEDAFKRS---IGFVQQQDLHLDLLSVKESLEISCLLR 851
Cdd:cd03224 29 VALLGRNGAGKTTLLKTIM-----GLLpprSGSIRFDGRDITGLPPHERAragIGYVPEGRRIFPELTVEENLLLGAYAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 852 GDGDRAY-LDTVSNL---LKLPSDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQG 927
Cdd:cd03224 104 RRAKRKArLERVYELfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL-LDEPSEGLAPKIVEEIFEAIRELRDEG 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 6324585 928 QAIFcTIHQPSKSVISHFDNIFLLKRgGECVFFGPMDD 965
Cdd:cd03224 183 VTIL-LVEQNARFALEIADRAYVLER-GRVVLEGTAAE 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
751-962 |
2.61e-18 |
|
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: 85.31 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLL---NVLSQRVETGVVSGEILIDGHPLTDED----AFK 822
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGeITALIGPSGCGKSTLLrllNRLNDLIPGAPDEGEVLLDGKDIYDLDvdvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 823 RSIGFVQQQDLHLDlLSVKESLEISCLLRGDGDRAYLDT-VSNLLK---LP---SDILVA-DLNPTQRKLLSIGVELVTK 894
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDErVEEALRkaaLWdevKDRLHAlGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324585 895 PSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCT--IHQPSKsvIShfDNI-FLLKrgGECVFFGP 962
Cdd:cd03260 160 PEVLL-LDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQAAR--VA--DRTaFLLN--GRLVEFGP 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
773-954 |
3.00e-18 |
|
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: 85.04 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 773 ISSGLTALMGESGAGKTTLLNVLS--QRVETG--VVSGEILIDGHPLTDEDAFKRSIGFVQQQDLHLDLLSVKESLEisC 848
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAglEKPDGGtiVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLA--F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 849 LLRGDGDRAYLDTVSNLLKL--PSDIL---VADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQL 923
Cdd:cd03297 99 GLKRKRNREDRISVDELLDLlgLDHLLnryPAQLSGGEKQRVALARALAAQPELLL-LDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|...
gi 6324585 924 --SLQGQAIFCTiHQPSKSVISHfDNIFLLKRG 954
Cdd:cd03297 178 kkNLNIPVIFVT-HDLSEAEYLA-DRIVVMEDG 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
750-954 |
9.76e-18 |
|
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: 83.71 E-value: 9.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTVGTK----KLINNASGFISSG-LTALMGESGAGKTTLLNVLsQRVETgVVSGEILIDGHPLTDEDA---- 820
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGeTLGLVGESGSGKSTLARAI-LGLLK-PTSGSIIFDGKDLLKLSRrlrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 821 -FKRSIGFV-QQQDLHLD-LLSVKESLE--ISCLLRGDGDRAYLDTVSNLL-KLPSDILVADLNPT-----QRKLLSIGV 889
Cdd:cd03257 79 iRRKEIQMVfQDPMSSLNpRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLvGVGLPEEVLNRYPHelsggQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324585 890 ELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQL--SLQGQAIFCTiHQPskSVISHF-DNIFLLKRG 954
Cdd:cd03257 159 ALALNPKLLI-ADEPTSALDVSVQAQILDLLKKLqeELGLTLLFIT-HDL--GVVAKIaDRVAVMYAG 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
735-938 |
1.58e-17 |
|
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: 87.73 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 735 YNEQPITETVETQkhiISWKNINYTV-GTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGvvSGEILIDG 812
Cdd:TIGR02857 309 AGKAPVTAAPASS---LEFSGVSVAYpGRRPALRPVSFTVPPGeRVALVGPSGAGKSTLLNLLLGFVDPT--EGSIAVNG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 813 HPLT--DEDAFKRSIGFVQQQDlHLDLLSVKESLEISC------LLRGDGDRAYLDTVSNLLKLPSDILVAD----LNPT 880
Cdd:TIGR02857 384 VPLAdaDADSWRDQIAWVPQHP-FLFAGTIAENIRLARpdasdaEIREALERAGLDEFVAALPQGLDTPIGEggagLSGG 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6324585 881 QRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSlQGQAIFCTIHQPS 938
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLL-LDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLA 518
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
754-936 |
1.58e-17 |
|
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: 82.95 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSqRVETgVVSGEILIDGHPLTDEDAFKRSIGFVQQQD 832
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGeFLALLGPSGCGKTTLLRLIA-GLER-PDSGEILIDGRDVTGVPPERRNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 833 LHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKLPSDILVADLNPT-----QRKLLSIGVELVTKPSLLLfLDEPTSG 907
Cdd:cd03259 82 ALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHelsggQQQRVALARALAREPSLLL-LDEPLSA 160
|
170 180 190
....*....|....*....|....*....|.
gi 6324585 908 LDAEAALTIVKFLKQLSLQGQ--AIFCTIHQ 936
Cdd:cd03259 161 LDAKLREELREELKELQRELGitTIYVTHDQ 191
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
779-945 |
3.10e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.61 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDG---HPLTDEDAFKRSIGFVqQQDLHL-DLLSVKESLEISCLLR 851
Cdd:COG1129 34 ALLGENGAGKSTLMKILS-----GVYqpdSGEILLDGepvRFRSPRDAQAAGIAII-HQELNLvPNLSVAENIFLGREPR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 852 GDG--D--------RAYLDTVSnlLKLPSDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGL-DAEAA--LTIVK 918
Cdd:COG1129 108 RGGliDwramrrraRELLARLG--LDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI-LDEPTASLtEREVErlFRIIR 184
|
170 180
....*....|....*....|....*...
gi 6324585 919 FLKQlslQGQAI-FctihqpsksvISHF 945
Cdd:COG1129 185 RLKA---QGVAIiY----------ISHR 199
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
756-972 |
3.99e-17 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 87.59 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 756 INYTVGTK-KLINNASGFIS-SGLTALMGESGAGKTTLLNVLSQRVETGV-VSGEILIDGHPLtDEDAFKRSIGFVQQQD 832
Cdd:PLN03140 170 INLAKKTKlTILKDASGIIKpSRMTLLLGPPSSGKTTLLLALAGKLDPSLkVSGEITYNGYRL-NEFVPRKTSAYISQND 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 833 LHLDLLSVKESLEISCLLRGDGDR-----------------------------AYLDTVSNL----------LKLPSDIL 873
Cdd:PLN03140 249 VHVGVMTVKETLDFSARCQGVGTRydllselarrekdagifpeaevdlfmkatAMEGVKSSLitdytlkilgLDICKDTI 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 874 VAD-----LNPTQRKLLSIGvELVTKPSLLLFLDEPTSGLDAEAALTIVKFLKQL-SLQGQAIFCTIHQPSKSVISHFDN 947
Cdd:PLN03140 329 VGDemirgISGGQKKRVTTG-EMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIvHLTEATVLMSLLQPAPETFDLFDD 407
|
250 260
....*....|....*....|....*
gi 6324585 948 IFLLKRgGECVFFGPMDDACGYFMS 972
Cdd:PLN03140 408 IILLSE-GQIVYQGPRDHILEFFES 431
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
751-954 |
5.66e-17 |
|
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: 85.97 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYT-VGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVEtgVVSGEILIDGHPLT--DEDAFKRSIG 826
Cdd:COG4988 337 IELEDVSFSyPGGRPALDGLSLTIPPGeRVALVGPSGAGKSTLLNLLLGFLP--PYSGSILINGVDLSdlDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 827 FVQQQDlHLDLLSVKESL----------EISCLLRgdgdRAYLDTVsnLLKLPS--DILVAD----LNPTQRKLLSIGVE 890
Cdd:COG4988 415 WVPQNP-YLFAGTIRENLrlgrpdasdeELEAALE----AAGLDEF--VAALPDglDTPLGEggrgLSGGQAQRLALARA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324585 891 LVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSlQGQA-IFCTiHQPskSVISHFDNIFLLKRG 954
Cdd:COG4988 488 LLRDAPLLL-LDEPTAHLDAETEAEILQALRRLA-KGRTvILIT-HRL--ALLAQADRILVLDDG 547
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
777-930 |
6.01e-17 |
|
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: 81.71 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 777 LTALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTDEDAFKRS---IG--FvqqQDLHL-DLLSVKESLEIS 847
Cdd:cd03219 28 IHGLIGPNGAGKTTLFNLIS-----GFLrptSGSVLFDGEDITGLPPHEIArlgIGrtF---QIPRLfPELTVLENVMVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 848 CLLRG----------DGDRAYLDTVSNLLK---LPS--DILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEA 912
Cdd:cd03219 100 AQARTgsglllararREEREARERAEELLErvgLADlaDRPAGELSYGQQRRLEIARALATDPKLLL-LDEPAAGLNPEE 178
|
170
....*....|....*...
gi 6324585 913 ALTIVKFLKQLSLQGQAI 930
Cdd:cd03219 179 TEELAELIRELRERGITV 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
779-923 |
6.05e-17 |
|
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: 85.73 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDGHPLTDED-----AFKRSIGFVQQQ-DLHLD-LLSVKESLEISC 848
Cdd:COG1123 295 GLVGESGSGKSTLARLL-----LGLLrptSGSILFDGKDLTKLSrrslrELRRRVQMVFQDpYSSLNpRMTVGDIIAEPL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 849 LLRGDGDRAYL-DTVSNLLK---LPSDilVADLNPT-----QRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKF 919
Cdd:COG1123 370 RLHGLLSRAERrERVAELLErvgLPPD--LADRYPHelsggQRQRVAIARALALEPKLLI-LDEPTSALDVSVQAQILNL 446
|
....
gi 6324585 920 LKQL 923
Cdd:COG1123 447 LRDL 450
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
771-923 |
1.54e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.44 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 771 GFIssgltalmGESGAGKTTLLNVLsqrveTGVV---SGEILIDGH-PLTDEDAFKRSIGFV--QQQDLHLDLlSVKESL 844
Cdd:COG4586 52 GFI--------GPNGAGKSTTIKML-----TGILvptSGEVRVLGYvPFKRRKEFARRIGVVfgQRSQLWWDL-PAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 845 EiscLLR---GDGDRAY---LDTVSNLLKLpSDILvadlnpTQ--RKLlSIG----VELVTkpSLL-----LFLDEPTSG 907
Cdd:COG4586 118 R---LLKaiyRIPDAEYkkrLDELVELLDL-GELL------DTpvRQL-SLGqrmrCELAA--ALLhrpkiLFLDEPTIG 184
|
170
....*....|....*.
gi 6324585 908 LDAEAALTIVKFLKQL 923
Cdd:COG4586 185 LDVVSKEAIREFLKEY 200
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
761-965 |
1.80e-16 |
|
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: 80.30 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 761 GTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVEtgVVSGEILIDGHPLT-----DEDAFKRSIGFVQQQdLH 834
Cdd:cd03256 12 NGKKALKDVSLSINPGeFVALIGPSGAGKSTLLRCLNGLVE--PTSGSVLIDGTDINklkgkALRQLRRQIGMIFQQ-FN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 835 L-DLLSVKESLEISCLlrgdgdrAYLDTVSNLLKL--PSDILVA------------------DLNPTQRKLLSIGVELVT 893
Cdd:cd03256 89 LiERLSVLENVLSGRL-------GRRSTWRSLFGLfpKEEKQRAlaalervglldkayqradQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324585 894 KPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQ-GQAIFCTIHQPSkSVISHFDNIFLLKRgGECVFFGPMDD 965
Cdd:cd03256 162 QPKLIL-ADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVD-LAREYADRIVGLKD-GRIVFDGPPAE 231
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
779-954 |
2.69e-16 |
|
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: 80.23 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTDED--AFKRSIGFVQQQ---DLHlDLLSVKESLE--ISC 848
Cdd:COG1124 35 GLVGESGSGKSTLLRALA-----GLErpwSGEVTFDGRPVTRRRrkAFRRRVQMVFQDpyaSLH-PRHTVDRILAepLRI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 849 LLRGDGDRayldTVSNLLK---LPSDIL---VADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLD----AEaaltIVK 918
Cdd:COG1124 109 HGLPDREE----RIAELLEqvgLPPSFLdryPHQLSGGQRQRVAIARALILEPELLL-LDEPTSALDvsvqAE----ILN 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 6324585 919 FLKQLSLQGQA--IFCTiHQPskSVISHF-DNIFLLKRG 954
Cdd:COG1124 180 LLKDLREERGLtyLFVS-HDL--AVVAHLcDRVAVMQNG 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
750-965 |
3.31e-16 |
|
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: 83.41 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKN--INYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRV-ETGVVSGEILIDGHPLTDEDAFKRS- 824
Cdd:COG1123 4 LLEVRDlsVRYPGGDVPAVDGVSLTIAPGeTVALVGESGSGKSTLALALMGLLpHGGRISGEVLLDGRDLLELSEALRGr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 825 -IGFV-QQQDLHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKLPSDILVADLNPT-----QRKLLSIGVELVTKPSL 897
Cdd:COG1123 84 rIGMVfQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHqlsggQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324585 898 LLfLDEPTSGLDAEAALTIVKFLKQLSLQ-GQAIFCTIHQPSKsVISHFDNIFLLKRgGECVFFGPMDD 965
Cdd:COG1123 164 LI-ADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGV-VAEIADRVVVMDD-GRIVEDGPPEE 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
754-935 |
3.52e-16 |
|
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: 79.68 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLInnasGFIssgltalmGESGAGKTTLLNVLSqrvetGVV---SGEILIDGH-PLTDEDAFKRSIGFV- 828
Cdd:cd03267 38 KGISFTIEKGEIV----GFI--------GPNGAGKTTTLKILS-----GLLqptSGEVRVAGLvPWKRRKKFLRRIGVVf 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 829 -QQQDLHLDLlSVKESLEISCLLRGDGDRAY---LDTVSNLLKLPS--DILVADLNPTQRKLLSIGVELVTKPSLLlFLD 902
Cdd:cd03267 101 gQKTQLWWDL-PVIDSFYLLAAIYDLPPARFkkrLDELSELLDLEEllDTPVRQLSLGQRMRAEIAAALLHEPEIL-FLD 178
|
170 180 190
....*....|....*....|....*....|....
gi 6324585 903 EPTSGLDAEAALTIVKFLKQLS-LQGQAIFCTIH 935
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNrERGTTVLLTSH 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
777-954 |
4.17e-16 |
|
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: 78.95 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 777 LTALMGESGAGKTTLLNVLSQRVETGvvSGEILIDG-HPLTDEDAFKRSIGFVQQQDLHLDLLSVKESLE-ISCL--LRG 852
Cdd:cd03266 33 VTGLLGPNGAGKTTTLRMLAGLLEPD--AGFATVDGfDVVKEPAEARRRLGFVSDSTGLYDRLTARENLEyFAGLygLKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 853 DGDRAYLDTVSNLLKLPS--DILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAI 930
Cdd:cd03266 111 DELTARLEELADRLGMEEllDRRVGGFSTGMRQKVAIARALVHDPPVLL-LDEPTTGLDVMATRALREFIRQLRALGKCI 189
|
170 180
....*....|....*....|....*.
gi 6324585 931 -FCT-IHQPSKSVIshfDNIFLLKRG 954
Cdd:cd03266 190 lFSThIMQEVERLC---DRVVVLHRG 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
777-923 |
6.68e-16 |
|
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: 79.31 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 777 LTALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDGHPLTDEDAFKRS---IG--FvqqQDLHL-DLLSVKESLEIS 847
Cdd:COG0411 32 IVGLIGPNGAGKTTLFNLI-----TGFYrptSGRILFDGRDITGLPPHRIArlgIArtF---QNPRLfPELTVLENVLVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 848 CLLRG---------------DGDRAYLDTVSNLLKLP-----SDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSG 907
Cdd:COG0411 104 AHARLgrgllaallrlprarREEREARERAEELLERVgladrADEPAGNLSYGQQRRLEIARALATEPKLLL-LDEPAAG 182
|
170
....*....|....*.
gi 6324585 908 LDAEAALTIVKFLKQL 923
Cdd:COG0411 183 LNPEETEELAELIRRL 198
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
49-259 |
1.08e-15 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 78.18 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLfhgktsLSYSPP--GSIKFKNNEFKSFSEKCPHQIIYNNEQDVHFPFL 122
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLG-PNgagkTTTIRML------LGLLRPtsGEVRVLGEDVARDPAEVRRRIGYVPQEPALYPDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 123 TVEQTIDFALSCkFDIPKGERDQIRNELLREFGLSHVLKTIVGNdffrgVSGGERKRISIIETFIANGSVYLWDNSTKGL 202
Cdd:COG1131 89 TVRENLRFFARL-YGLPRKEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 203 DSATALDFLEILRKMAKATRSVnLV---RISQAsDKIvdkFDKILMLSDSYQLFYGTVDE 259
Cdd:COG1131 163 DPEARRELWELLRELAAEGKTV-LLsthYLEEA-ERL---CDRVAIIDKGRIVADGTPDE 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
774-924 |
2.33e-15 |
|
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: 79.37 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 774 SSGLTALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTDEDAF------KRSIGFVQQQDL---HldlLSVK 841
Cdd:COG4148 24 GRGVTALFGPSGSGKTTLLRAIA-----GLErpdSGRIRLGGEVLQDSARGiflpphRRRIGYVFQEARlfpH---LSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 842 ESLEISC-LLRGDGDRAYLDTVSNLLKLpSDILvaDLNPTQrklLS--------IGVELVTKPSLLLfLDEPTSGLDAEA 912
Cdd:COG4148 96 GNLLYGRkRAPRAERRISFDEVVELLGI-GHLL--DRRPAT---LSggerqrvaIGRALLSSPRLLL-MDEPLAALDLAR 168
|
170
....*....|..
gi 6324585 913 ALTIVKFLKQLS 924
Cdd:COG4148 169 KAEILPYLERLR 180
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
754-962 |
3.09e-15 |
|
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: 77.01 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTDEDA--FKRSIGF 827
Cdd:COG1120 5 ENLSVGYGGRPVLDDVSLSLPPGeVTALLGPNGSGKSTLLRALA-----GLLkpsSGEVLLDGRDLASLSRreLARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 828 VQQQDLHLDLLSVKESLEISC-----LLRGDGD------RAYLDTVsNLLKLpSDILVADLNPTQRKLLSIGVELVTKPS 896
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRyphlgLFGRPSAedreavEEALERT-GLEHL-ADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324585 897 LLLfLDEPTSGLDAEAALTIVKFLKQLS-LQGQAIFCTIHQPSkSVISHFDNIFLLKrGGECVFFGP 962
Cdd:COG1120 158 LLL-LDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLN-LAARYADRLVLLK-DGRIVAQGP 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
751-935 |
5.70e-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: 75.48 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSGLT-ALMGESGAGKTTLLNVLSQRVEtgVVSGEILIDGHPLTDE-DAFKRSIGFV 828
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIfGLLGPNGAGKTTTIKMLTTLLK--PTSGRATVAGHDVVREpREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 829 QQQDLHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKL-----PSDILVADLNPTQRKLLSIGVELVTKPSLLlFLDE 903
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFvglleAADRLVKTYSGGMRRRLEIARSLVHRPEVL-FLDE 157
|
170 180 190
....*....|....*....|....*....|...
gi 6324585 904 PTSGLDAEAALTIVKFLKQL-SLQGQAIFCTIH 935
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTH 190
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
751-935 |
1.47e-14 |
|
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: 74.37 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNIN--YTVGTKKLiNNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETgvVSGEILIDGHPLTDEDA-----FK 822
Cdd:cd03292 1 IEFINVTktYPNGTAAL-DGINISISAGeFVFLVGPSGAGKSTLLKLIYKEELP--TSGTIRVNGQDVSDLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 823 RSIGFVQQQDLHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKL-----PSDILVADLNPTQRKLLSIGVELVTKPSL 897
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELvglshKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 6324585 898 LLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIH 935
Cdd:cd03292 158 LI-ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
49-248 |
2.89e-14 |
|
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: 73.27 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTL--FHGKTSlsysppGSIKFKNNEFKS-----FSEKC------P-HQII 110
Cdd:cd03225 17 LDDISLTIKKGEFVLIVG-PNgsgkSTLLRLLngLLGPTS------GEVLVDGKDLTKlslkeLRRKVglvfqnPdDQFF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 111 ynneqdvhfpFLTVEQTIDFALsCKFDIPKGERDQIRNELLREFGLSHVLKTIVGNdffrgVSGGERKRISIIETFIANG 190
Cdd:cd03225 90 ----------GPTVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 191 SVYLWDNSTKGLDSATALDFLEILRKMAKATRSVNLV--RIsqasDKIVDKFDKILMLSD 248
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVthDL----DLLLELADRVIVLED 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
779-938 |
4.39e-14 |
|
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: 73.01 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLS-QRVETgvvSGEILIDGHPLTDEDAF--KRSIGFVQQqDLHLDLLSVKESLEISCLLRGDGD 855
Cdd:cd03245 34 AIIGRVGSGKSTLLKLLAgLYKPT---SGSVLLDGTDIRQLDPAdlRRNIGYVPQ-DVTLFYGTLRDNITLGAPLADDER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 856 ------RAYLDTVSNLLKLPSDILVAD----LNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLsL 925
Cdd:cd03245 110 ilraaeLAGVTDFVNKHPNGLDLQIGErgrgLSGGQRQAVALARALLNDPPILL-LDEPTSAMDMNSEERLKERLRQL-L 187
|
170
....*....|...
gi 6324585 926 QGQAIFCTIHQPS 938
Cdd:cd03245 188 GDKTLIIITHRPS 200
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
751-978 |
5.21e-14 |
|
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: 72.92 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLnvlsqRVETGVV---SGEILIDGHPLT-----DEDAF 821
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGeILAIIGPSGSGKSTLL-----RLIVGLLrpdSGEVLIDGEDISglseaELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 822 KRSIGFVQQQDLHLDLLSVKESleISCLLRGDGD----------RAYLDTVSnllkLPSDilvADLNPTQ-----RKLLS 886
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFEN--VAFPLREHTRlseeeireivLEKLEAVG----LRGA---EDLYPAElsggmKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 887 IGVELVTKPSlLLFLDEPTSGLDAEAALTIVKFLkqLSLQGQAIFCTIhqpsksVISH--------FDNIFLLKRgGECV 958
Cdd:cd03261 147 LARALALDPE-LLLYDEPTAGLDPIASGVIDDLI--RSLKKELGLTSI------MVTHdldtafaiADRIAVLYD-GKIV 216
|
250 260
....*....|....*....|
gi 6324585 959 FFGPMDDacgyFMSHDNTLV 978
Cdd:cd03261 217 AEGTPEE----LRASDDPLV 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
755-935 |
7.06e-14 |
|
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: 72.58 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 755 NINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDGHPLTDEDAFKRS---IGF 827
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGeIVGLLGPNGAGKTTTFYMI-----VGLVkpdSGKILLDGQDITKLPMHKRArlgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 828 VQQQDLHLDLLSVKESLEISCLLRGDgDRAY----LDTVSNLLKLPS--DILVADLNPTQRKLLSIGVELVTKPSLLLfL 901
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGL-SKKEreekLEELLEEFHITHlrKSKASSLSGGERRRVEIARALATNPKFLL-L 157
|
170 180 190
....*....|....*....|....*....|....
gi 6324585 902 DEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIH 935
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
750-980 |
7.26e-14 |
|
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: 72.70 E-value: 7.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDGHPLTDED-----A 820
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGeILAIIGGSGSGKSVLLKLI-----IGLLrpdSGEILVDGQDITGLSekelyE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 821 FKRSIGFVQQQDLHLDLLSVKESLEISCLLRGDGDRAYL-DTVSNLLK---LPSdilVADLNPTQrklLSIG----VEL- 891
Cdd:COG1127 80 LRRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIrELVLEKLElvgLPG---AADKMPSE---LSGGmrkrVALa 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 892 ---VTKPSLLlFLDEPTSGLDAEAALTIVKFLKQL--SLQGQAIfctihqpsksVISH-----F---DNIFLLKRgGECV 958
Cdd:COG1127 154 ralALDPEIL-LYDEPTAGLDPITSAVIDELIRELrdELGLTSV----------VVTHdldsaFaiaDRVAVLAD-GKII 221
|
250 260
....*....|....*....|..
gi 6324585 959 FFGPMDDacgyFMSHDNTLVYD 980
Cdd:COG1127 222 AEGTPEE----LLASDDPWVRQ 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
751-936 |
7.32e-14 |
|
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: 71.86 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDGHPLTDEDAFKRSIG 826
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGeIYGFLGPNGAGKTTTMKII-----LGLIkpdSGEITFDGKSYQKNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 827 -FVQQQDLHlDLLSVKESLEISCLLRGDGDRAY---LDTVsnLLKLPSDILVADLNPTQRKLLSIGVELVTKPSLLLfLD 902
Cdd:cd03268 76 aLIEAPGFY-PNLTARENLRLLARLLGIRKKRIdevLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI-LD 151
|
170 180 190
....*....|....*....|....*....|....
gi 6324585 903 EPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQ 936
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHL 185
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
49-248 |
1.16e-13 |
|
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: 71.75 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLfhgkTSLSYSPPGSIKFKNNEFKSFSEKcpHQIIYNNE------QDVH 118
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVG-PSgsgkSTLLNIL----GGLDRPTSGEVRVDGTDISKLSEK--ELAAFRRRhigfvfQSFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 119 F-PFLTVEQTIdfALSCKFD-IPKGERDQIRNELLREFGLSHVLKTIVGNdffrgVSGGERKRISIIETFIANGSVYLWD 196
Cdd:cd03255 93 LlPDLTALENV--ELPLLLAgVPKKERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARALANDPKIILAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6324585 197 NSTKGLDSATALDFLEILRKMAKAtRSVNLVRISQaSDKIVDKFDKILMLSD 248
Cdd:cd03255 166 EPTGNLDSETGKEVMELLRELNKE-AGTTIVVVTH-DPELAEYADRIIELRD 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
780-935 |
1.66e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 71.24 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 780 LMGESGAGKTTLLNVL--SQRVEtgvvSGEILIDGHPLTDEDA-----FKRSIGFVqQQDLHL-DLLSVKESLEISCLLR 851
Cdd:COG2884 33 LTGPSGAGKSTLLKLLygEERPT----SGQVLVNGQDLSRLKRreipyLRRRIGVV-FQDFRLlPDRTVYENVALPLRVT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 852 GDGDRAYLDTVSNLLKlpsdiLV-----ADLNPTQrklLSIGvE---------LVTKPSLLLfLDEPTSGLDAEAALTIV 917
Cdd:COG2884 108 GKSRKEIRRRVREVLD-----LVglsdkAKALPHE---LSGG-EqqrvaiaraLVNRPELLL-ADEPTGNLDPETSWEIM 177
|
170
....*....|....*...
gi 6324585 918 KFLKQLSLQGQAIFCTIH 935
Cdd:COG2884 178 ELLEEINRRGTTVLIATH 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
750-962 |
2.00e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTVGTKKLINNAS-GFISSGLTALMGESGAGKTTLL---NVLSQRVETGVVSGEILIDGH----PLTDEDAF 821
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSlDFYPNEITALIGPSGSGKSTLLrsiNRMNDLNPEVTITGSIVYNGHniysPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 822 KRSIGFVQQQDLHLDlLSVKESLEISCLLRGDGDRAYLD-TVSNLLKLPS------DILVAD---LNPTQRKLLSIGVEL 891
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDeAVEKSLKGASiwdevkDRLHDSalgLSGGQQQRVCIARVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324585 892 VTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSKSVISHFDNIFLlkrGGECVFFGP 962
Cdd:PRK14239 164 ATSPKIIL-LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFL---DGDLIEYND 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
737-954 |
2.26e-13 |
|
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: 74.80 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 737 EQPITETVETQKHIISWKNIN--YTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTG---VVSGEILI 810
Cdd:COG4987 320 TEPAEPAPAPGGPSLELEDVSfrYPGAGRPVLDGLSLTLPPGeRVAIVGPSGSGKSTLLALL-----LRfldPQSGSITL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 811 DGHPLT--DEDAFKRSIGFVQQqDLHLDLLSVKESLeiscLL-RGDGD----RAYLDTVsNLLKLpsdilVADLnPT--- 880
Cdd:COG4987 395 GGVDLRdlDEDDLRRRIAVVPQ-RPHLFDTTLRENL----RLaRPDATdeelWAALERV-GLGDW-----LAAL-PDgld 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 881 -------------QRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLsLQGQAIFCTIHQPskSVISHFDN 947
Cdd:COG4987 463 twlgeggrrlsggERRRLALARALLRDAPILL-LDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRL--AGLERMDR 538
|
....*..
gi 6324585 948 IFLLKRG 954
Cdd:COG4987 539 ILVLEDG 545
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
777-910 |
2.57e-13 |
|
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: 70.58 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 777 LTALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTDEDafkRSIGFVQQQDLHLDLLSVKESLEISCLLRGD 853
Cdd:cd03293 32 FVALVGPSGCGKSTLLRIIA-----GLErptSGEVLVDGEPVTGPG---PDRGYVFQQDALLPWLTVLDNVALGLELQGV 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324585 854 GDRAYLDTVSNLLKlpsdiLV-----ADLNPTQ-----RKLLSIGVELVTKPSLLLfLDEPTSGLDA 910
Cdd:cd03293 104 PKAEARERAEELLE-----LVglsgfENAYPHQlsggmRQRVALARALAVDPDVLL-LDEPFSALDA 164
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
777-908 |
4.24e-13 |
|
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: 70.40 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 777 LTALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTDEDAFKRS---IGFVQQ-----QDlhldlLSVKESLE 845
Cdd:COG0410 31 IVALLGRNGAGKTTLLKAIS-----GLLpprSGSIRFDGEDITGLPPHRIArlgIGYVPEgrrifPS-----LTVEENLL 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324585 846 ISCLLRGDGD--RAYLDTVSNL---LKLPSDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGL 908
Cdd:COG0410 101 LGAYARRDRAevRADLERVYELfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL-LDEPSLGL 167
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
750-965 |
4.46e-13 |
|
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: 70.50 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTG----VVSGEILIDGHPLTDEDAF--K 822
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGeHWAILGPNGAGKSTLLSLI-----TGdlppTYGNDVRLFGERRGGEDVWelR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 823 RSIGFVQQqDLHLDL---LSVKE--------SL----EIScllrgDGDRAYLDTVSNLLKLPS--DILVADLNPTQRKLL 885
Cdd:COG1119 78 KRIGLVSP-ALQLRFprdETVLDvvlsgffdSIglyrEPT-----DEQRERARELLELLGLAHlaDRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 886 SIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQG--QAIFCTiHQPSKsVISHFDNIFLLKRgGECVFFGPM 963
Cdd:COG1119 152 LIARALVKDPELLI-LDEPTAGLDLGARELLLALLDKLAAEGapTLVLVT-HHVEE-IPPGITHVLLLKD-GRVVAAGPK 227
|
..
gi 6324585 964 DD 965
Cdd:COG1119 228 EE 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
745-910 |
1.26e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.90 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 745 ETQKHIISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLnvlsqRVETGV---VSGEILIDGhpltdEDA 820
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGtMVTLLGPSGCGKTTVL-----RLVAGLekpTEGQIFIDG-----EDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 821 FKRSIgfvQQQDL-----------HLDL-------------------LSVKESLEIsCLLRGDGDRaYLDTVSNllklps 870
Cdd:PRK11432 71 THRSI---QQRDIcmvfqsyalfpHMSLgenvgyglkmlgvpkeerkQRVKEALEL-VDLAGFEDR-YVDQISG------ 139
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6324585 871 dilvadlnpTQRKLLSIGVELVTKPSLLLFlDEPTSGLDA 910
Cdd:PRK11432 140 ---------GQQQRVALARALILKPKVLLF-DEPLSNLDA 169
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
49-254 |
1.51e-12 |
|
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: 67.65 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGYP---TSTLFKTLFHGKTSLSYSppGSI----KFKNNEFKSFSEKCPHQiiynneqDVHFPF 121
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESgagKTTLLDVLAGRKTAGVIT--GEIlingRPLDKNFQRSTGYVEQQ-------DVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 122 LTVEQTIDFalSCKfdipkgerdqirnellrefglshvlktivgndfFRGVSGGERKRISIIETFIANGSVYLWDNSTKG 201
Cdd:cd03232 94 LTVREALRF--SAL---------------------------------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6324585 202 LDSATALDFLEILRKMAKATRSVnLVRISQASDKIVDKFDKILMLSDSYQLFY 254
Cdd:cd03232 139 LDSQAAYNIVRFLKKLADSGQAI-LCTIHQPSASIFEKFDRLLLLKRGGKTVY 190
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
779-935 |
1.73e-12 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 69.73 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDGHPLTDE-DAFKRSIGFVQQQDLHLDLLSVKESLEISCLLRGDG 854
Cdd:TIGR01188 23 GFLGPNGAGKTTTIRML-----TTLLrptSGTARVAGYDVVREpRKVRRSIGIVPQYASVDEDLTGRENLEMMGRLYGLP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 855 DRAYLDTVSNLLKLPS-----DILVADLNPTQRKLLSIGVELVTKPSLLlFLDEPTSGLDAEAALTIVKFLKQLSLQGQA 929
Cdd:TIGR01188 98 KDEAEERAEELLELFElgeaaDRPVGTYSGGMRRRLDIAASLIHQPDVL-FLDEPTTGLDPRTRRAIWDYIRALKEEGVT 176
|
....*.
gi 6324585 930 IFCTIH 935
Cdd:TIGR01188 177 ILLTTH 182
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
751-936 |
2.10e-12 |
|
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: 67.94 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSqRVETgVVSGEILIDGHPLTDE----DAFKRSI 825
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGeVVVIIGPSGSGKSTLLRCIN-LLEE-PDSGTIIIDGLKLTDDkkniNELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 826 GFV-QQQDL--HLDLL-------------SVKESLEIScllrgdgdRAYLDTVSnlLKLPSDILVADLNPTQRKLLSIGV 889
Cdd:cd03262 79 GMVfQQFNLfpHLTVLenitlapikvkgmSKAEAEERA--------LELLEKVG--LADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6324585 890 ELVTKPSLLLFlDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQ 936
Cdd:cd03262 149 ALAMNPKVMLF-DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
754-923 |
2.68e-12 |
|
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: 67.67 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLnvlsqRVETGVV---SGEILIDGHPLTDEDAFKRSIGFVQ 829
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGeFVVLLGPSGCGKTTTL-----RMIAGLEeptSGRIYIGGRDVTDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 830 QQDLHLDLLSVKESLEISCLLRGdGDRAYLD----TVSNLLKLPS--DILVADLNPTQRKLLSIGVELVTKPSLLLfLDE 903
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRK-VPKDEIDervrEVAELLQIEHllDRKPKQLSGGQRQRVALGRAIVREPKVFL-MDE 156
|
170 180
....*....|....*....|....
gi 6324585 904 PTSGLDA----EAALTIVKFLKQL 923
Cdd:cd03301 157 PLSNLDAklrvQMRAELKRLQQRL 180
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
778-954 |
2.82e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.96 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 778 TALMGESGAGKTTLLNVLSQRVEtgVVSGEILIDGHPLTD--EDAFKRSIGFVqQQDLHLDLLSVKESLEISCLLRGDGD 855
Cdd:COG1132 369 VALVGPSGSGKSTLVNLLLRFYD--PTSGRILIDGVDIRDltLESLRRQIGVV-PQDTFLFSGTIRENIRYGRPDATDEE 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 856 ------RAYLDTVsnLLKLPS--DILVAD----LNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQL 923
Cdd:COG1132 446 veeaakAAQAHEF--IEALPDgyDTVVGErgvnLSGGQRQRIAIARALLKDPPILI-LDEATSALDTETEALIQEALERL 522
|
170 180 190
....*....|....*....|....*....|....*...
gi 6324585 924 sLQGQAIFctihqpsksVISH-------FDNIFLLKRG 954
Cdd:COG1132 523 -MKGRTTI---------VIAHrlstirnADRILVLDDG 550
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
751-935 |
2.84e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.86 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLlnvlsQRVETGVVS---GEILIDGHPLTDEDAFKRS-I 825
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGeCFGLLGPNGAGKSTI-----ARMILGMTSpdaGKITVLGVPVPARARLARArI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 826 GFVQQQDlHLDL-LSVKESLEISCLLRGDGDRAYLDTVSNLLKLP-----SDILVADLNPTQRKLLSIGVELVTKPSLLL 899
Cdd:PRK13536 117 GVVPQFD-NLDLeFTVRENLLVFGRYFGMSTREIEAVIPSLLEFArleskADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190
....*....|....*....|....*....|....*.
gi 6324585 900 fLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIH 935
Cdd:PRK13536 196 -LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
779-944 |
2.87e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTDE---DAFKRSIGFVQQqdlHLDL---LSVKE----SLE 845
Cdd:COG3845 35 ALLGENGAGKSTLMKILY-----GLYqpdSGEILIDGKPVRIRsprDAIALGIGMVHQ---HFMLvpnLTVAEnivlGLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 846 ISCLLRGDGD--RAYLDTVSNL--LKLPSDILVADlnptqrklLSIG----VE----LVTKPSLLLfLDEPTSGLDAEAA 913
Cdd:COG3845 107 PTKGGRLDRKaaRARIRELSERygLDVDPDAKVED--------LSVGeqqrVEilkaLYRGARILI-LDEPTAVLTPQEA 177
|
170 180 190
....*....|....*....|....*....|...
gi 6324585 914 LTIVKFLKQLSLQGqaifctihqpsKSV--ISH 944
Cdd:COG3845 178 DELFEILRRLAAEG-----------KSIifITH 199
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
779-923 |
3.19e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.88 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSQRVETGvvSGEILIDGHPLTDEDAFKRS------IGFVQQQDLHLDLLSVKESLEISCLLRG 852
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDDGS--SGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLIPTLNALENVELPALLRG 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 853 DGDRAYLDTVSNLLKLPS-----DILVADLNPTQRKLLSIGVELVTKPSlLLFLDEPTSGLDAEAALTIVKFLKQL 923
Cdd:PRK10584 118 ESSRQSRNGAKALLEQLGlgkrlDHLPAQLSGGEQQRVALARAFNGRPD-VLFADEPTGNLDRQTGDKIADLLFSL 192
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
754-949 |
3.60e-12 |
|
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: 66.78 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSGLT-ALMGESGAGKTTLLNVLSQRVETGVVSGEILIDGHPLTD---EDAFKRSIGfvq 829
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVhALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDITDlppEERARLGIF--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 830 qqdlhldlLSVKESLEISCLlrgdgdrayldTVSNLLKlpsdilvaDLNPT----QRK---LLSIgveLVTKPSLLLfLD 902
Cdd:cd03217 81 --------LAFQYPPEIPGV-----------KNADFLR--------YVNEGfsggEKKrneILQL---LLLEPDLAI-LD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6324585 903 EPTSGLDAEAALTIVKFLKQLSLQGQAIFctihqpsksVISHFDNIF 949
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLREEGKSVL---------IITHYQRLL 167
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
779-923 |
4.70e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 69.36 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTDEDAFKRSIGFVQQqdlHLDL---LSVKE----SLEIsc 848
Cdd:COG3842 35 ALLGPSGCGKTTLLRMIA-----GFEtpdSGRILLDGRDVTGLPPEKRNVGMVFQ---DYALfphLTVAEnvafGLRM-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 849 llRGDGDRAYLDTVSNLLKlpsdiLV-----ADLNPTQrklLSIG----VE----LVTKPSLLLfLDEPTSGLDAEAALT 915
Cdd:COG3842 105 --RGVPKAEIRARVAELLE-----LVgleglADRYPHQ---LSGGqqqrVAlaraLAPEPRVLL-LDEPLSALDAKLREE 173
|
....*...
gi 6324585 916 IVKFLKQL 923
Cdd:COG3842 174 MREELRRL 181
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
778-910 |
5.98e-12 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 67.42 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 778 TALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTDEDafkRSIGFVQQQDLHLDLLSVKESLEISCLLRGDG 854
Cdd:COG1116 40 VALVGPSGCGKSTLLRLIA-----GLEkptSGEVLVDGKPVTGPG---PDRGVVFQEPALLPWLTVLDNVALGLELRGVP 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324585 855 DRAYLDTVSNLLKlpsdiLV-----ADLNPTQrklLSIG----VE----LVTKPSLLLfLDEPTSGLDA 910
Cdd:COG1116 112 KAERRERARELLE-----LVglagfEDAYPHQ---LSGGmrqrVAiaraLANDPEVLL-MDEPFGALDA 171
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
778-944 |
6.38e-12 |
|
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: 65.14 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 778 TALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDG---HPLTDEDAFKRSIGFVQQqdlhldllsvkesleiscllr 851
Cdd:cd03216 29 HALLGENGAGKSTLMKILS-----GLYkpdSGEILVDGkevSFASPRDARRAGIAMVYQ--------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 852 gdgdrayldtvsnllklpsdilvadLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQA-I 930
Cdd:cd03216 83 -------------------------LSVGERQMVEIARALARNARLLI-LDEPTAALTPAEVERLFKVIRRLRAQGVAvI 136
|
170
....*....|....
gi 6324585 931 FctihqpsksvISH 944
Cdd:cd03216 137 F----------ISH 140
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
751-954 |
7.23e-12 |
|
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: 66.48 E-value: 7.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKL-INNASGFISSGLT-ALMGESGAGKTTLLNVLSQRVEtgVVSGEILIDGHPLTD--EDAFKRSIG 826
Cdd:cd03254 3 IEFENVNFSYDEKKPvLKDINFSIKPGETvAIVGPTGAGKTTLINLLMRFYD--PQKGQILIDGIDIRDisRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 827 FVqQQDLHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLL----KLPSDILV------ADLNPTQRKLLSIGVELVTKPS 896
Cdd:cd03254 81 VV-LQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHdfimKLPNGYDTvlgengGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6324585 897 LLLfLDEPTSGLDAEAALTIVKFLKQLsLQGQAIFCTIHQPskSVISHFDNIFLLKRG 954
Cdd:cd03254 160 ILI-LDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRL--STIKNADKILVLDDG 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
751-936 |
1.27e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETgvVSGEILIDGHP---LTDEDAFKRSIG 826
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGeIHALLGENGAGKSTLMKVLSGIHEP--TKGTITINNINynkLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 827 FVQQQDLHLDLLSVKESLEISCLL------------RGDGDRAYLDTVSNLLKLPSDILVADLNPTQRKLLSIGVELVTK 894
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGRHLtkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6324585 895 PSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQ 936
Cdd:PRK09700 164 AKVII-MDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
754-922 |
1.39e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGVVSGEILIDGHPL---TDEDAFKRSIGFVQ 829
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGeIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEELqasNIRDTERAGIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 830 QQDLHLDLLSVKESL----EISCLLRGDGDRAYLDTVSNLLKLPSDILVA----DLNPTQRKLLSIGVELvTKPSLLLFL 901
Cdd:PRK13549 89 QELALVKELSVLENIflgnEITPGGIMDYDAMYLRAQKLLAQLKLDINPAtpvgNLGLGQQQLVEIAKAL-NKQARLLIL 167
|
170 180
....*....|....*....|....
gi 6324585 902 DEPTSGL-DAEAA--LTIVKFLKQ 922
Cdd:PRK13549 168 DEPTASLtESETAvlLDIIRDLKA 191
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
751-955 |
2.20e-11 |
|
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: 65.33 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKK--LINNASGFISSGLT-ALMGESGAGKTTLLNVLSQRVEtgVVSGEILIDGHPLTDEDA--FKRSI 825
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETvALVGPSGSGKSTLVNLIPRFYD--VDSGRILIDGHDVRDYTLasLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 826 GFVqQQDLHLDLLSVKESLEIScllRGDGDRAYLDTVSNL-------LKLPS--DILVAD----LNPTQRKLLSIGVELV 892
Cdd:cd03251 79 GLV-SQDVFLFNDTVAENIAYG---RPGATREEVEEAARAanahefiMELPEgyDTVIGErgvkLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324585 893 TKPSLLLfLDEPTSGLDAEAALTIVKFLKQLsLQGQAIFCTIHQpsKSVISHFDNIFLLKRGG 955
Cdd:cd03251 155 KDPPILI-LDEATSALDTESERLVQAALERL-MKNRTTFVIAHR--LSTIENADRIVVLEDGK 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
754-923 |
2.57e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 67.02 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSqrvetG---VVSGEILIDGHPLTDEDAFKRSIGFV- 828
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGeFLVLLGPSGCGKSTLLRMIA-----GledPTSGEILIGGRDVTDLPPKDRNIAMVf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 829 QQQDL--HldlLSVKESLEISCLLRGDgDRAYLDT----VSNLLKLpSDIL---VADLNPTQRKLLSIGVELVTKPSLLL 899
Cdd:COG3839 82 QSYALypH---MTVYENIAFPLKLRKV-PKAEIDRrvreAAELLGL-EDLLdrkPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180
....*....|....*....|....*...
gi 6324585 900 FlDEPTSGLDA----EAALTIVKFLKQL 923
Cdd:COG3839 157 L-DEPLSNLDAklrvEMRAEIKRLHRRL 183
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
751-954 |
2.94e-11 |
|
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: 64.61 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSGLT-ALMGESGAGKTTLLnvlsqRVETGVV---SGEILIDGHPLTDEDafKRSIG 826
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIfGLLGPNGAGKTTTI-----RMILGIIlpdSGEVLFDGKPLDIAA--RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 827 FV-QQQDLHLDLlSVKESLEISCLLRGDGDRAYLDTVSNLLKL-----PSDILVADLNPTQRKLLSIGVELVTKPSLLLf 900
Cdd:cd03269 74 YLpEERGLYPKM-KVIDQLVYLAQLKGLKKEEARRRIDEWLERlelseYANKRVEELSKGNQQKVQFIAAVIHDPELLI- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6324585 901 LDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQpSKSVISHFDNIFLLKRG 954
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKG 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
49-246 |
3.07e-11 |
|
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: 64.48 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLfhgktsLSYSPP--GSIKFknneFKSFSEKCPHQIIY---NNEQDVHF 119
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVG-PNgagkSTLLKAI------LGLLKPtsGSIRV----FGKPLEKERKRIGYvpqRRSIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 120 PfLTVEQTIDFAL---SCKFDIPKGERDQIRNELLREFGLSHVLKTIVGNdffrgVSGGERKRIsiietFIA-----NGS 191
Cdd:cd03235 84 P-ISVRDVVLMGLyghKGLFRRLSKADKAKVDEALERVGLSELADRQIGE-----LSGGQQQRV-----LLAralvqDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6324585 192 VYLWDNSTKGLDSATALDFLEILRKMAKATRSVnLVrISQASDKIVDKFDKILML 246
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTI-LV-VTHDLGLVLEYFDRVLLL 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
761-909 |
3.17e-11 |
|
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: 65.01 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 761 GTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETgvVSGEILIDGHPLTDEDAFK--RSIGFVQQQDLHLDL 837
Cdd:cd03295 12 GGKKAVNNLNLEIAKGeFLVLIGPSGSGKTTTMKMINRLIEP--TSGEIFIDGEDIREQDPVElrRKIGYVIQQIGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 838 LSVKESLEISCLLRGDGDRAYLDTVSNLLKLpsdilvADLNPT---------------QRkllsIGV--ELVTKPSLLLf 900
Cdd:cd03295 90 MTVEENIALVPKLLKWPKEKIRERADELLAL------VGLDPAefadryphelsggqqQR----VGVarALAADPPLLL- 158
|
....*....
gi 6324585 901 LDEPTSGLD 909
Cdd:cd03295 159 MDEPFGALD 167
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
779-937 |
3.26e-11 |
|
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: 63.92 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLS--QRVEtgvvSGEILIDGHPL-TDEDAFKRSIGFVQQQDLHLDLLSVKESLEISCLLRGDGD 855
Cdd:TIGR01189 30 QVTGPNGIGKTTLLRILAglLRPD----SGEVRWNGTPLaEQRDEPHENILYLGHLPGLKPELSALENLHFWAAIHGGAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 856 RAYLDTVS--NLLKLpSDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCT 933
Cdd:TIGR01189 106 RTIEDALAavGLTGF-EDLPAAQLSAGQQRRLALARLWLSRRPLWI-LDEPTTALDKAGVALLAGLLRAHLARGGIVLLT 183
|
....
gi 6324585 934 IHQP 937
Cdd:TIGR01189 184 THQD 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
780-937 |
3.36e-11 |
|
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: 64.05 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 780 LMGESGAGKTTLLNVLS--QRVEtgvvSGEILIDGHPLTDE-DAFKRSIGFVQQQDLHLDLLSVKESLEISCLLRGD-GD 855
Cdd:cd03231 31 VTGPNGSGKTTLLRILAglSPPL----AGRVLLNGGPLDFQrDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHSDeQV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 856 RAYLDTVSnlLKLPSDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIH 935
Cdd:cd03231 107 EEALARVG--LNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI-LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
..
gi 6324585 936 QP 937
Cdd:cd03231 184 QD 185
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
751-923 |
5.67e-11 |
|
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: 64.28 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLnvlsqRVETGV---VSGEILIDGHPLTDEDAFKRSIG 826
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGeLVALLGPSGSGKTTLL-----RLIAGLerpDSGTILFGGEDATDVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 827 FVQQqdlHLDL---LSVKESLEISCLLRGDGDRAYLDT----VSNLLKLP-----SDILVADLNPTQRKLLSIGVELVTK 894
Cdd:cd03296 78 FVFQ---HYALfrhMTVFDNVAFGLRVKPRSERPPEAEirakVHELLKLVqldwlADRYPAQLSGGQRQRVALARALAVE 154
|
170 180
....*....|....*....|....*....
gi 6324585 895 PSLLLfLDEPTSGLDAEAALTIVKFLKQL 923
Cdd:cd03296 155 PKVLL-LDEPFGALDAKVRKELRRWLRRL 182
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
779-930 |
6.50e-11 |
|
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: 62.83 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSqrvetGV---VSGEILIDGHPLTD---EDAFKRSIGFV----QQQDLHLDLlSVKESLEISC 848
Cdd:cd03215 30 GIAGLVGNGQTELAEALF-----GLrppASGEITLDGKPVTRrspRDAIRAGIAYVpedrKREGLVLDL-SVAENIALSS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 849 LLRGdGdrayldtvsnllklpsdilvadlnpTQRKLLsIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQ 928
Cdd:cd03215 104 LLSG-G-------------------------NQQKVV-LARWLARDPRVLI-LDEPTRGVDVGAKAEIYRLIRELADAGK 155
|
..
gi 6324585 929 AI 930
Cdd:cd03215 156 AV 157
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
750-922 |
7.56e-11 |
|
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: 66.39 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGVVSGEILIDGHPLTDE---DAFKRSI 825
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGeCVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASnirDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 826 GFVQQQDLHLDLLSVKESLEISCLLRGDGDRAYLDTV----SNLLK------LPSDILVADLNPTQRKLLSIGVELvTKP 895
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMylraKNLLRelqldaDNVTRPVGDYGGGQQQLVEIAKAL-NKQ 159
|
170 180 190
....*....|....*....|....*....|
gi 6324585 896 SLLLFLDEPTSGL---DAEAALTIVKFLKQ 922
Cdd:TIGR02633 160 ARLLILDEPSSSLtekETEILLDIIRDLKA 189
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
49-248 |
9.43e-11 |
|
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: 61.49 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLfhgktSLSYSPP-GSIKFKNNefksfsekcphqiiynneqdvhfpflt 123
Cdd:cd00267 15 LDNVSLTLKAGEIVALVG-PNgsgkSTLLRAI-----AGLLKPTsGEILIDGK--------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 124 veqtidfalsckfDIPKGERDQIRNELLREFGLShvlktivgndffrgvsGGERKRISIIETFIANGSVYLWDNSTKGLD 203
Cdd:cd00267 62 -------------DIAKLPLEELRRRIGYVPQLS----------------GGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6324585 204 SATALDFLEILRKMAKATRSVnlVRISQASDKIVDKFDKILMLSD 248
Cdd:cd00267 113 PASRERLLELLRELAEEGRTV--IIVTHDPELAELAADRVIVLKD 155
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
754-935 |
1.08e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.04 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNAS-GFISSGLTALMGESGAGKTTLLNVLSQRVETGvvSGEILIDGHPLT--DEDAFKRSIGFVQQ 830
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSlTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS--EGEILLDAQPLEswSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 831 QDLHLDLLSVKESLEIS------CLLR-GDGDRAYLDTVSNL--LKLPSDILVADLNPTQRKLLSIGVeLVTKPSLLLFL 901
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGrypwhgALGRfGAADREKVEEAISLvgLKPLAHRLVDSLSGGERQRAWIAM-LVAQDSRCLLL 171
|
170 180 190
....*....|....*....|....*....|....*
gi 6324585 902 DEPTSGLDAEAALTIVKFLKQLSLQ-GQAIFCTIH 935
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLH 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
750-935 |
1.51e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.06 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDGHPLTDEDAFKRS- 824
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGeCFGLLGPNGAGKTTTLRML-----LGLThpdAGSISLCGEPVPSRARHARQr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 825 IGFVQQQDlHLDL-LSVKESLEISCLLRGDGDRAYLDTVSNLL---KLPS--DILVADLNPTQRKLLSIGVELVTKPSLL 898
Cdd:PRK13537 82 VGVVPQFD-NLDPdFTVRENLLVFGRYFGLSAAAARALVPPLLefaKLENkaDAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 6324585 899 LfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIH 935
Cdd:PRK13537 161 V-LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
751-954 |
1.92e-10 |
|
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: 61.08 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVG--TKKLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTGV---VSGEILIDGHPLT--DEDAFK 822
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGeSLAIIGPSGSGKSTLARLI-----LGLlrpTSGRVRLDGADISqwDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 823 RSIGFVQQQDLhldllsvkesleiscLLRGDgdrayldtvsnllklpsdilVAD--LNPTQRKLLSIGVELVTKPSlLLF 900
Cdd:cd03246 76 DHVGYLPQDDE---------------LFSGS--------------------IAEniLSGGQRQRLGLARALYGNPR-ILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 901 LDEPTSGLD--AEAALTIVkfLKQLSLQGQAIFCTIHQPskSVISHFDNIFLLKRG 954
Cdd:cd03246 120 LDEPNSHLDveGERALNQA--IAALKAAGATRIVIAHRP--ETLASADRILVLEDG 171
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
778-937 |
1.96e-10 |
|
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: 65.07 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 778 TALMGESGAGKTTLLNVLSQRVETgvVSGEILIDGHPLT--DEDAFKRSIGFVqQQDLHLDLLSVKESLEIScllRGDGD 855
Cdd:TIGR02868 364 VAILGPSGSGKSTLLATLAGLLDP--LQGEVTLDGVPVSslDQDEVRRRVSVC-AQDAHLFDTTVRENLRLA---RPDAT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 856 RAYLDTVSNLLKLPSDI------LVADLNPT-------QRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQ 922
Cdd:TIGR02868 438 DEELWAALERVGLADWLralpdgLDTVLGEGgarlsggERQRLALARALLADAPILL-LDEPTEHLDAETADELLEDLLA 516
|
170
....*....|....*
gi 6324585 923 lSLQGQAIFCTIHQP 937
Cdd:TIGR02868 517 -ALSGRTVVLITHHL 530
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
779-935 |
2.24e-10 |
|
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: 65.81 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSQrvETGVVSGEILIDGHP-LTDEDAFKRSIGFVQQQDLHLDLLSVKESLEISCLLRGDGDRA 857
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTG--DTTVTSGDATVAGKSiLTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEE 2046
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 858 yLDTVSNL------LKLPSDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIF 931
Cdd:TIGR01257 2047 -IEKVANWsiqslgLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL-LDEPTTGMDPQARRMLWNTIVSIIREGRAVV 2124
|
....
gi 6324585 932 CTIH 935
Cdd:TIGR01257 2125 LTSH 2128
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
770-965 |
2.55e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.55 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 770 SGFISSG-LTALMGESGAGKTTLLNVLSqrvetGVVS--GEILIDGHPLTDEDAFK--RSIGFVQQQDLHLDLLSVKE-- 842
Cdd:COG4138 16 SAQVNAGeLIHLIGPNGAGKSTLLARMA-----GLLPgqGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 843 SLEISCLLRGDGDRAYLDTVSNLLKLpSDILVADLNPT-----QRKLLsIGVELVTKPSL-----LLFLDEPTSGLDA-- 910
Cdd:COG4138 91 ALHQPAGASSEAVEQLLAQLAEALGL-EDKLSRPLTQLsggewQRVRL-AAVLLQVWPTInpegqLLLLDEPMNSLDVaq 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6324585 911 EAALTivKFLKQLSLQGQAIFCTIHQPSKSViSHFDNIFLLKRgGECVFFGPMDD 965
Cdd:COG4138 169 QAALD--RLLRELCQQGITVVMSSHDLNHTL-RHADRVWLLKQ-GKLVASGETAE 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
43-224 |
2.75e-10 |
|
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: 61.75 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 43 PNPAnqLNDITFQAEAGEMVLVLGYPT---STLFKTL--FHGKTSlsysppGSIKFKNNEFKSFSEKCPHQIIYNNEQDV 117
Cdd:cd03263 14 TKPA--VDDLSLNVYKGEIFGLLGHNGagkTTTLKMLtgELRPTS------GTAYINGYSIRTDRKAARQSLGYCPQFDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 118 HFPFLTVEQTIDFalSCKFD-IPKGERDQIRNELLREFGLSHVLKTIVGNdffrgVSGGERKRISIIETFIANGSVYLWD 196
Cdd:cd03263 86 LFDELTVREHLRF--YARLKgLPKSEIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180
....*....|....*....|....*...
gi 6324585 197 NSTKGLDSATALDFLEILRKMAKAtRSV 224
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRKG-RSI 185
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
774-909 |
2.92e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.74 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 774 SSGLTALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTDED------AFKRSIGFV-QQQDL--HldlLSVK 841
Cdd:PRK11144 23 AQGITAIFGRSGAGKTSLINAIS-----GLTrpqKGRIVLNGRVLFDAEkgiclpPEKRRIGYVfQDARLfpH---YKVR 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 842 ESLEISCllrGDGDRAYLDTVSNLLKLPS--DILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLD 909
Cdd:PRK11144 95 GNLRYGM---AKSMVAQFDKIVALLGIEPllDRYPGSLSGGEKQRVAIGRALLTAPELLL-MDEPLASLD 160
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
777-965 |
3.45e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 62.24 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 777 LTALMGESGAGKTTLLNVLSQRVE---TGVVSGEILIDGHPLTDEDA--FKRSIGFVQQQDLHLDLLSVKESL------- 844
Cdd:PRK14247 31 ITALMGPSGSGKSTLLRVFNRLIElypEARVSGEVYLDGQDIFKMDVieLRRRVQMVFQIPNPIPNLSIFENValglkln 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 845 -------EISCLLRGDGDRAYL-DTVSNLLKLPSdilvADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTI 916
Cdd:PRK14247 111 rlvkskkELQERVRWALEKAQLwDEVKDRLDAPA----GKLSGGQQQRLCIARALAFQPEVLL-ADEPTANLDPENTAKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6324585 917 VKFLKQLSLQGQAIFCTIHQPSKSVISHFdNIFLLKrgGECVFFGPMDD 965
Cdd:PRK14247 186 ESLFLELKKDMTIVLVTHFPQQAARISDY-VAFLYK--GQIVEWGPTRE 231
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
1157-1276 |
3.56e-10 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 60.98 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1157 LLLSQSIIELPLALTSSTLFFVCAFFSCGFNNAGWSAGVFFLNYMLFAAYYSTLGLWLIYTAPNLQTAAVFVAFIYSFTA 1236
Cdd:COG0842 48 ILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLT 127
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 6324585 1237 SFCGVMQPYSLFPTFWKFMYRVSPYTYFVETFVSILLHNW 1276
Cdd:COG0842 128 FLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALFLGGA 167
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
754-965 |
4.53e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 62.43 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASgF-ISSG-LTALMGESGAGKTTLLnvlsqRVETGVV---SGEILIDGHPLTDEDafKRSIGF- 827
Cdd:COG4152 5 KGLTKRFGDKTAVDDVS-FtVPKGeIFGLLGPNGAGKTTTI-----RIILGILapdSGEVLWDGEPLDPED--RRRIGYl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 828 -----------VQQQ-----DLH-LDLLSVKES-------LEIscllrgdGDRAYlDTVSNLLKlpsdilvadLNptQRK 883
Cdd:COG4152 77 peerglypkmkVGEQlvylaRLKgLSKAEAKRRadewlerLGL-------GDRAN-KKVEELSK---------GN--QQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 884 lLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQA-IFCTiHQPSkSVISHFDNIFLLKRgGECVFFGP 962
Cdd:COG4152 138 -VQLIAALLHDPELLI-LDEPFSGLDPVNVELLKDVIRELAAKGTTvIFSS-HQME-LVEELCDRIVIINK-GRKVLSGS 212
|
...
gi 6324585 963 MDD 965
Cdd:COG4152 213 VDE 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
761-955 |
4.58e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.95 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 761 GTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSqRVETGvVSGEILIDGHPLTDEDA--FKRSIGFVQQQDLHLDL 837
Cdd:PRK11231 13 GTKRILNDLSLSLPTGkITALIGPNGCGKSTLLKCFA-RLLTP-QSGTVFLGDKPISMLSSrqLARRLALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 838 LSVKESLE------ISCLLR-GDGDRAYLDTVSNLLKLP--SDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGL 908
Cdd:PRK11231 91 ITVRELVAygrspwLSLWGRlSAEDNARVNQAMEQTRINhlADRRLTDLSGGQRQRAFLAMVLAQDTPVVL-LDEPTTYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6324585 909 DAEAALTIVKFLKQLSLQGQAIFCTIH---QPSKsvisHFDNIFLLKRGG 955
Cdd:PRK11231 170 DINHQVELMRLMRELNTQGKTVVTVLHdlnQASR----YCDHLVVLANGH 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
751-927 |
4.58e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.57 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSGLTA-LMGESGAGKTTLLNVLSQrVETGvVSGEILIDGHPL-----TDEDA---F 821
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLvLLGPSGAGKSSLLRVLNL-LEMP-RSGTLNIAGNHFdfsktPSDKAireL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 822 KRSIGFVQQQdLHL-DLLSVKESL-EISCLLRG-DGDRAYLDTVSNLLKLP----SDILVADLNPTQRKLLSIGVELVTK 894
Cdd:PRK11124 81 RRNVGMVFQQ-YNLwPHLTVQQNLiEAPCRVLGlSKDQALARAEKLLERLRlkpyADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190
....*....|....*....|....*....|...
gi 6324585 895 PSLLLFlDEPTSGLDAEAALTIVKFLKQLSLQG 927
Cdd:PRK11124 160 PQVLLF-DEPTAALDPEITAQIVSIIRELAETG 191
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
751-954 |
7.14e-10 |
|
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: 59.63 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVG--TKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGvvSGEILIDGHPLTD-EDAFKRSIG 826
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGeKIALLGRSGSGKSTLLQLLTGDLKPQ--QGEITLDGVPVSDlEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 827 FVQQqdlhldllsvkesleiscllrgdgdRAYL--DTVSNLLKLPsdilvadLNPTQRKLLSIGVELVTKPSLLLfLDEP 904
Cdd:cd03247 79 VLNQ-------------------------RPYLfdTTLRNNLGRR-------FSGGERQRLALARILLQDAPIVL-LDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6324585 905 TSGLDA--EAAL--TIVKFLKQLSLqgqaIFCTIHQPSksvISHFDNIFLLKRG 954
Cdd:cd03247 126 TVGLDPitERQLlsLIFEVLKDKTL----IWITHHLTG---IEHMDKILFLENG 172
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
751-955 |
7.18e-10 |
|
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: 61.02 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTK---KLINNASGFISSGLT-ALMGESGAGKTTLLNVLsQRVeTGVVSGEILIDGHPLTDED--AFKRS 824
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTvALVGSSGCGKSTVVSLL-ERF-YDPTSGEILLDGVDIRDLNlrWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 825 IGFVqQQDLHLDLLSVKESleiscLLRGDGDRAYLDTV---------SNLLKLPS--DILVAD----LNPTQRKLLSIGV 889
Cdd:cd03249 79 IGLV-SQEPVLFDGTIAEN-----IRYGKPDATDEEVEeaakkanihDFIMSLPDgyDTLVGErgsqLSGGQKQRIAIAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324585 890 ELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIfcTI-HQpsKSVISHFDNIFLLKRGG 955
Cdd:cd03249 153 ALLRNPKILL-LDEATSALDAESEKLVQEALDRAMKGRTTI--VIaHR--LSTIRNADLIAVLQNGQ 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
34-221 |
7.25e-10 |
|
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: 60.56 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 34 KSYDAEDSmPNPAnqLNDITFQAEAGEMVLVLGyPT----STLFKTL--FHGKTSlsysppGSIKFknnEFKSFSEkCPH 107
Cdd:cd03293 8 KTYGGGGG-AVTA--LEDISLSVEEGEFVALVG-PSgcgkSTLLRIIagLERPTS------GEVLV---DGEPVTG-PGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 108 QIIYNNEQDVHFPFLTVEQTIDFALSCKFdIPKGERDQIRNELLREFGLSHVLktivgNDFFRGVSGGERKRISIIETFI 187
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQG-VPKAEARERAEELLELVGLSGFE-----NAYPHQLSGGMRQRVALARALA 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 6324585 188 ANGSVYLWDNSTKGLDSATAL----DFLEILRKMAKAT 221
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREqlqeELLDIWRETGKTV 185
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
755-954 |
8.17e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.40 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 755 NINYTVGTKKLiNNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETgvVSGEILIDGHPLtDEDA-----FKRSIGFV 828
Cdd:PRK13636 12 NYNYSDGTHAL-KGININIKKGeVTAILGGNGAGKSTLFQNLNGILKP--SSGRILFDGKPI-DYSRkglmkLRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 829 -QQQDLHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKLPSdilVADL--NPT------QRKLLSIGVELVTKPSLLL 899
Cdd:PRK13636 88 fQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTG---IEHLkdKPThclsfgQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 900 fLDEPTSGLDAEAALTIVKFLKQLSLQ-GQAIFCTIHQpSKSVISHFDNIFLLKRG 954
Cdd:PRK13636 165 -LDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHD-IDIVPLYCDNVFVMKEG 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
751-910 |
1.13e-09 |
|
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: 60.33 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQrVETgVVSGEILIDGHPLTDEDAFKRSIGFVQ 829
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGeFFTLLGPSGCGKTTLLRLIAG-FET-PTSGEILLDGKDITNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 830 QQDLHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKLP-----SDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEP 904
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVqlegyANRKPSQLSGGQQQRVAIARALVNEPKVLL-LDEP 157
|
....*.
gi 6324585 905 TSGLDA 910
Cdd:cd03300 158 LGALDL 163
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
750-936 |
1.16e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.49 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLL---NVLSQrvetgVVSGEILIDGHPLTDEDAFKRSI 825
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGeVVVIIGPSGSGKSTLLrciNKLEE-----ITSGDLIVDGLKVNDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 826 ----GFVQQQDLHLDLLSVKESLEISCL-LRGDGDRAYLDTVSNLLK----------LPSdilvaDLNPTQRKLLSIGVE 890
Cdd:PRK09493 76 rqeaGMVFQQFYLFPHLTALENVMFGPLrVRGASKEEAEKQARELLAkvglaerahhYPS-----ELSGGQQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6324585 891 LVTKPSLLLFlDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQ 936
Cdd:PRK09493 151 LAVKPKLMLF-DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
778-935 |
1.20e-09 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 59.36 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 778 TALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLtDED-----AFKRSIGFV-QQQDLHLDLLSVKESLEISC 848
Cdd:TIGR01166 21 LALLGANGAGKSTLLLHLN-----GLLrpqSGAVLIDGEPL-DYSrkgllERRQRVGLVfQDPDDQLFAADVDQDVAFGP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 849 L---LRGDGDRAYLDTVSNLLKLP--SDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQL 923
Cdd:TIGR01166 95 LnlgLSEAEVERRVREALTAVGASglRERPTHCLSGGEKKRVAIAGAVAMRPDVLL-LDEPTAGLDPAGREQMLAILRRL 173
|
170
....*....|..
gi 6324585 924 SLQGQAIFCTIH 935
Cdd:TIGR01166 174 RAEGMTVVISTH 185
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
49-237 |
1.91e-09 |
|
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: 58.18 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLfhgktsLSYSPP--GSIKFKNNEFKSFSEKCPHQIIYNNEQDVHFPFL 122
Cdd:cd03230 16 LDDISLTVEKGEIYGLLG-PNgagkTTLIKII------LGLLKPdsGEIKVLGKDIKKEPEEVKRRIGYLPEEPSLYENL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 123 TVEQTIDFalsckfdipkgerdqirnellrefglshvlktivgndffrgvSGGERKRISIIETFIANGSVYLWDNSTKGL 202
Cdd:cd03230 89 TVRENLKL------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6324585 203 DSATALDFLEILRKMAKATRSV-----NLVRISQASDKIV 237
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTIllsshILEEAERLCDRVA 166
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
772-954 |
2.11e-09 |
|
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: 62.72 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 772 FISSGLTALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDGHPL-TDEDAFKRSIGFVQQQDLHLDLLSVKESLEIS 847
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSIL-----TGLLpptSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 848 CLLRGDG-DRAYLDTVSNL----LKLPSDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQ 922
Cdd:TIGR01257 1028 AQLKGRSwEEAQLEMEAMLedtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV-LDEPTSGVDPYSRRSIWDLLLK 1106
|
170 180 190
....*....|....*....|....*....|..
gi 6324585 923 LSLQGQAIFCTIHQPSKSVIShfDNIFLLKRG 954
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADLLG--DRIAIISQG 1136
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
782-921 |
2.26e-09 |
|
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: 59.04 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 782 GESGAGKTTLLNVLSQRVEtgVVSGEILIDGHPLTDEDAFK--RSIGFVQQQDL--------HLDLLSVKESLEI-SCLl 850
Cdd:cd03244 37 GRTGSGKSSLLLALFRLVE--LSSGSILIDGVDISKIGLHDlrSRISIIPQDPVlfsgtirsNLDPFGEYSDEELwQAL- 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324585 851 rgdgDRAYL-DTVSNLL-KLPSDILVADLNPT--QRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLK 921
Cdd:cd03244 114 ----ERVGLkEFVESLPgGLDTVVEEGGENLSvgQRQLLCLARALLRKSKILV-LDEATASVDPETDALIQKTIR 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
779-951 |
3.06e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSqrvetGV---VSGEILIDGHPL---TDEDAFKRSIGfVQQQDLHL-DLLSVKESLEISCL-- 849
Cdd:PRK11288 34 ALMGENGAGKSTLLKILS-----GNyqpDAGSILIDGQEMrfaSTTAALAAGVA-IIYQELHLvPEMTVAENLYLGQLph 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 850 LRGDGDRAYL--DTVSNLLKLPSDIlvadlNP-TQRKLLSIG----VEL---VTKPSLLLFLDEPTSGLDAEAALTIVKF 919
Cdd:PRK11288 108 KGGIVNRRLLnyEAREQLEHLGVDI-----DPdTPLKYLSIGqrqmVEIakaLARNARVIAFDEPTSSLSAREIEQLFRV 182
|
170 180 190
....*....|....*....|....*....|...
gi 6324585 920 LKQLSLQGQAIFctihqpsksVISH-FDNIFLL 951
Cdd:PRK11288 183 IRELRAEGRVIL---------YVSHrMEEIFAL 206
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
779-965 |
4.74e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHP---LTDEDAFKRSIGFVQQQDLHLDLLSVKESLeiscLLRG 852
Cdd:PRK15439 41 ALLGGNGAGKSTLMKIIA-----GIVppdSGTLEIGGNPcarLTPAKAHQLGIYLVPQEPLLFPNLSVKENI----LFGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 853 DGDRAYLDTVSNLLK-----LPSDILVADLNPTQRKLLSIGVELVtKPSLLLFLDEPTSGLDAEAALTIVKFLKQLSLQG 927
Cdd:PRK15439 112 PKRQASMQKMKQLLAalgcqLDLDSSAGSLEVADRQIVEILRGLM-RDSRILILDEPTASLTPAETERLFSRIRELLAQG 190
|
170 180 190
....*....|....*....|....*....|....*....
gi 6324585 928 QAIFCTIHQ-PSKSVISHFDNIFllkRGGECVFFGPMDD 965
Cdd:PRK15439 191 VGIVFISHKlPEIRQLADRISVM---RDGTIALSGKTAD 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
751-936 |
5.57e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.71 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLnvlsqRVETGV---VSGEILIDGHPLTDEDAFKRSIG 826
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGqMVALLGPSGSGKTTLL-----RIIAGLehqTSGHIRFHGTDVSRLHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 827 FVQQqdlHLDL---LSVKESLE--ISCLLRGD-GDRAYLDT-VSNLLKLPSDILVADLNPTQrklLSIGVE--------L 891
Cdd:PRK10851 78 FVFQ---HYALfrhMTVFDNIAfgLTVLPRRErPNAAAIKAkVTQLLEMVQLAHLADRYPAQ---LSGGQKqrvalaraL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6324585 892 VTKPSLLLfLDEPTSGLDAEAALTIVKFLKQL--SLQGQAIFCTIHQ 936
Cdd:PRK10851 152 AVEPQILL-LDEPFGALDAQVRKELRRWLRQLheELKFTSVFVTHDQ 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
49-262 |
5.76e-09 |
|
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: 60.30 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGYPTStlfktlfhGKTSLSYS-----PP-----GSIKFKNNEFKSFSEKCPHQIIYNNEQD-- 116
Cdd:COG1123 22 VDGVSLTIAPGETVALVGESGS--------GKSTLALAlmgllPHggrisGEVLLDGRDLLELSEALRGRRIGMVFQDpm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 117 VHFPFLTVEQTIDFALSCkFDIPKGERDQIRNELLREFGLSHVLKtivgnDFFRGVSGGERKRISIIETFIANGSVYLWD 196
Cdd:COG1123 94 TQLNPVTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLD-----RYPHQLSGGQRQRVAIAMALALDPDLLIAD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 197 NSTKGLDSATALDFLEILRKMAKaTRSVNLVRISQASDKIVDKFDKILMLSDSYQLFYGTVDECLT 262
Cdd:COG1123 168 EPTTALDVTTQAEILDLLRELQR-ERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
782-935 |
6.47e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 782 GESGAGKTTLLNVLSQRVETGvvSGEILIDGHPLTDEDAfKRSIGFVQ-----QQDlhldlLSVKESLEISCLLRGdgdR 856
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVE--SGQIQIDGKTATRGDR-SRFMAYLGhlpglKAD-----LSTLENLHFLCGLHG---R 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 857 AYLDTVSNLLKLP-----SDILVADLNPTQRKLLSIGvELVTKPSLLLFLDEPTSGLDAEaALTIVKFLKQLSLQGQ-AI 930
Cdd:PRK13543 113 RAKQMPGSALAIVglagyEDTLVRQLSAGQKKRLALA-RLWLSPAPLWLLDEPYANLDLE-GITLVNRMISAHLRGGgAA 190
|
....*
gi 6324585 931 FCTIH 935
Cdd:PRK13543 191 LVTTH 195
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
779-944 |
7.80e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSQRVETGVVSGEILIDGhpltDEDAFK-----RSIGFVQ-QQDLHL-DLLSVKESL----EIS 847
Cdd:NF040905 31 ALCGENGAGKSTLMKVLSGVYPHGSYEGEILFDG----EVCRFKdirdsEALGIVIiHQELALiPYLSIAENIflgnERA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 848 clLRG--DGDRAYLDTVSNL----LKLPSDILVADLNPTQRKLLSIGVELvTKPSLLLFLDEPTSGL---DAEAALTIVk 918
Cdd:NF040905 107 --KRGviDWNETNRRARELLakvgLDESPDTLVTDIGVGKQQLVEIAKAL-SKDVKLLILDEPTAALneeDSAALLDLL- 182
|
170 180
....*....|....*....|....*.
gi 6324585 919 flkqLSLQGQAIFCTIhqpsksvISH 944
Cdd:NF040905 183 ----LELKAQGITSII-------ISH 197
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
750-923 |
8.11e-09 |
|
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: 57.59 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTVGTK----KLINNASGFISSG-LTALMGESGAGKTTLLNVLSQrVETGvVSGEILIDGHPLTDED----- 819
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGeIFGIIGRSGAGKSTLIRCING-LERP-TSGSVLVDGTDLTLLSgkelr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 820 AFKRSIGFVQQqdlHLDLLSVKESLE-ISCLLRGDG-DRAYLDT-VSNLLKL-----PSDILVADLNPTQRKLLSIGVEL 891
Cdd:cd03258 79 KARRRIGMIFQ---HFNLLSSRTVFEnVALPLEIAGvPKAEIEErVLELLELvgledKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190
....*....|....*....|....*....|..
gi 6324585 892 VTKPSLLLfLDEPTSGLDAEAALTIVKFLKQL 923
Cdd:cd03258 156 ANNPKVLL-CDEATSALDPETTQSILALLRDI 186
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
765-954 |
8.27e-09 |
|
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: 57.88 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 765 LINNASGFISSG-LTALMGESGAGKTTLLNVLsQRVETGvVSGEILIDGHPL--TDEDAFKRSIGFVQQQDLHLDlLSVK 841
Cdd:cd03252 17 ILDNISLRIKPGeVVGIVGRSGSGKSTLTKLI-QRFYVP-ENGRVLVDGHDLalADPAWLRRQVGVVLQENVLFN-RSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 842 ESLeisCLLRGDGDRAYLDTVSNL-------LKLPS--DILV----ADLNPTQRKLLSIGVELVTKPSLLLFlDEPTSGL 908
Cdd:cd03252 94 DNI---ALADPGMSMERVIEAAKLagahdfiSELPEgyDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIF-DEATSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6324585 909 DAEAALTIVKFLKQLsLQGQAIFCTIHQpsKSVISHFDNIFLLKRG 954
Cdd:cd03252 170 DYESEHAIMRNMHDI-CAGRTVIIIAHR--LSTVKNADRIIVMEKG 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
49-248 |
9.09e-09 |
|
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: 59.78 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLfhgktsLSYSPP--GSIKFKNNEFKSFSEKCPHQIIYNNEQDVHFpFL 122
Cdd:COG4987 351 LDGLSLTLPPGERVAIVG-PSgsgkSTLLALL------LRFLDPqsGSITLGGVDLRDLDEDDLRRRIAVVPQRPHL-FD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 123 -TVEQTIDFALsckfdiPKGERDQIRnELLREFGLSHVLK-------TIVGNDFfRGVSGGERKRISIIETFIANGSVYL 194
Cdd:COG4987 423 tTLRENLRLAR------PDATDEELW-AALERVGLGDWLAalpdgldTWLGEGG-RRLSGGERRRLALARALLRDAPILL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 195 WDNSTKGLDSATALDFLEILRKMAKaTRSVNLV--RISQasdkiVDKFDKILMLSD 248
Cdd:COG4987 495 LDEPTEGLDAATEQALLADLLEALA-GRTVLLIthRLAG-----LERMDRILVLED 544
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
746-923 |
9.40e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.19 E-value: 9.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 746 TQKHIISWKNINYTVGTKKLINNASGFISSG--LTaLMGESGAGKTTLLNVLSQrVETgVVSGEILIDGHPLTDEDAFKR 823
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGefLT-LLGPSGCGKTTVLRLIAG-FET-PDSGRIMLDGQDITHVPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 824 SIGFVQQQDLHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKLPSDILVADLNPTQrklLS--------IGVELVTKP 895
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQ---LSggqqqrvaIARAVVNKP 163
|
170 180
....*....|....*....|....*...
gi 6324585 896 SLLLfLDEPTSGLDAEAALTIVKFLKQL 923
Cdd:PRK09452 164 KVLL-LDESLSALDYKLRKQMQNELKAL 190
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
754-922 |
9.59e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 59.69 E-value: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVEtgVVSGEILIDGHpltdedafkRSIGFVQQQD 832
Cdd:COG0488 2 ENLSKSFGGRPLLDDVSLSINPGdRIGLVGRNGAGKSTLLKILAGELE--PDSGEVSIPKG---------LRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 833 LHLDLLSVKESL-----EISCLLR-------------GDGDR------------AY-----LDTVSNLLKLPSDIL---V 874
Cdd:COG0488 71 PLDDDLTVLDTVldgdaELRALEAeleeleaklaepdEDLERlaelqeefealgGWeaearAEEILSGLGFPEEDLdrpV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6324585 875 ADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQ 922
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLL-LDEPTNHLDLESIEWLEEFLKN 197
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
746-966 |
1.01e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 746 TQKHIISWKNINYTVGTKKLINNASGFISSGLTALM-GESGAGKTTLLNVLSQRVETgvVSGEILIDGHPLT--DEDAFK 822
Cdd:PRK10247 3 ENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLItGPSGCGKSTLLKIVASLISP--TSGTLLFEGEDIStlKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 823 RSIGF-VQQQDLHLDllSVKESLEISCLLRGDG--DRAYLDTVSNlLKLPSDIL---VADLNPTQRKLLSIGVELVTKPS 896
Cdd:PRK10247 81 QQVSYcAQTPTLFGD--TVYDNLIFPWQIRNQQpdPAIFLDDLER-FALPDTILtknIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 897 LLLfLDEPTSGLDaEAALTIV-----KFLKQlslQGQAIFCTIHqpSKSVISHFDN-IFLLKRGGEcvffgpMDDA 966
Cdd:PRK10247 158 VLL-LDEITSALD-ESNKHNVneiihRYVRE---QNIAVLWVTH--DKDEINHADKvITLQPHAGE------MQEA 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
755-936 |
1.10e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 755 NINYTVGTKKLINNASGFI-SSGLTALMGESGAGKTTLLNVLSQRVETGvvSGEILIDGHPL-TDEDAFKRSIGFVQ--- 829
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLpAGGLLHLKGSNGAGKTTLLKLIAGLLNPE--KGEILFERQSIkKDLCTYQKQLCFVGhrs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 830 --------QQDLHLDLLSVKESLEISCLLRgdgdrayLDTVSNLLKLPSDILVADlnptQRKLLSIgVELVTKPSLLLFL 901
Cdd:PRK13540 84 ginpyltlRENCLYDIHFSPGAVGITELCR-------LFSLEHLIDYPCGLLSSG----QKRQVAL-LRLWMSKAKLWLL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 6324585 902 DEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQ 936
Cdd:PRK13540 152 DEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
782-923 |
1.16e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 58.55 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 782 GESGAGKTTLL---NVLsQRVEtgvvSGEILIDGHPLTDED-----AFKRSIGFVQQqdlHLDLLS---VKE----SLEI 846
Cdd:COG1135 38 GYSGAGKSTLIrciNLL-ERPT----SGSVLVDGVDLTALSerelrAARRKIGMIFQ---HFNLLSsrtVAEnvalPLEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 847 ScllrgdG-DRAYLDT-VSNLLKlpsdiLV-----ADLNPTQrklLS------IGV--ELVTKPSLLLfLDEPTSGLDAE 911
Cdd:COG1135 110 A------GvPKAEIRKrVAELLE-----LVglsdkADAYPSQ---LSggqkqrVGIarALANNPKVLL-CDEATSALDPE 174
|
170
....*....|..
gi 6324585 912 AALTIVKFLKQL 923
Cdd:COG1135 175 TTRSILDLLKDI 186
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
778-954 |
1.26e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.47 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 778 TALMGESGAGKTTLLNVLSqrvetGVVS--GEILIDGHPLT--DEDAFKRSIGFVqQQDLHLDLLSVKESL--------- 844
Cdd:PRK11174 379 IALVGPSGAGKTSLLNALL-----GFLPyqGSLKINGIELRelDPESWRKHLSWV-GQNPQLPHGTLRDNVllgnpdasd 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 845 -EISCLLrgdgDRAYLDTVSNLLKLPSDILVADLNPT------QRklLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIV 917
Cdd:PRK11174 453 eQLQQAL----ENAWVSEFLPLLPQGLDTPIGDQAAGlsvgqaQR--LALARALLQPCQLLL-LDEPTASLDAHSEQLVM 525
|
170 180 190
....*....|....*....|....*....|....*..
gi 6324585 918 KFLKQLSLQGQAIFCTiHQPSKsvISHFDNIFLLKRG 954
Cdd:PRK11174 526 QALNAASRRQTTLMVT-HQLED--LAQWDQIWVMQDG 559
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
722-954 |
1.34e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 722 QISPSNKEMALNDYNEQPITETVETQKhIISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVE 800
Cdd:COG2401 3 RYNPFFVLMRVTKVYSSVLDLSERVAI-VLEAFGVELRVVERYVLRDLNLEIEPGeIVLIVGASGSGKSTLLRLLAGALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 801 TGVVSGEILIDGHPLTDEDAFKRSIGFVQQQDLHLDLLSvkesleiscllrgdgdRAYLDTVSNLLKLPSdilvaDLNPT 880
Cdd:COG2401 82 GTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAVELLN----------------AVGLSDAVLWLRRFK-----ELSTG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 881 QRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLS--LQGQAIFCTIH-------QPSKSVISHFDNIFLL 951
Cdd:COG2401 141 QKFRFRLALLLAERPKLLV-IDEFCSHLDRQTAKRVARNLQKLArrAGITLVVATHHydviddlQPDLLIFVGYGGVPEE 219
|
...
gi 6324585 952 KRG 954
Cdd:COG2401 220 KRR 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
741-923 |
1.39e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 57.35 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 741 TETVETQKHIISWKNINYTVGTKKLINNAS-GFISSGLTALMGESGAGKTTLL---NVLSQRVETGVVSGEILIDG---- 812
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINlDIPENKVTALIGPSGCGKSTLLrclNRMNDLIPGARVEGEILLDGediy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 813 HPLTDEDAFKRSIGFVQQQ---------D-------LH-------LDLLsVKESLEiscllrgdgdRAYL-DTVSNLLKL 868
Cdd:COG1117 82 DPDVDVVELRRRVGMVFQKpnpfpksiyDnvayglrLHgikskseLDEI-VEESLR----------KAALwDEVKDRLKK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6324585 869 PsdilVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQL 923
Cdd:COG1117 151 S----ALGLSGGQQQRLCIARALAVEPEVLL-MDEPTSALDPISTAKIEELILEL 200
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
747-954 |
1.40e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.20 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 747 QKHIISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQrvETGVVSGEILIDGHPLTD---EDAFK 822
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGeIVTLIGANGAGKTTLLGTLCG--DPRATSGRIVFDGKDITDwqtAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 823 RSIGFVQQQDLHLDLLSVKESLEISCLLrgdGDRA-YLDTVSNLLKLPSDIL------VADLNPTQRKLLSIGVELVTKP 895
Cdd:PRK11614 80 EAVAIVPEGRRVFSRMTVEENLAMGGFF---AERDqFQERIKWVYELFPRLHerriqrAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324585 896 SLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFcTIHQPSKSVISHFDNIFLLKRG 954
Cdd:PRK11614 157 RLLL-LDEPSLGLAPIIIQQIFDTIEQLREQGMTIF-LVEQNANQALKLADRGYVLENG 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
739-954 |
1.42e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.07 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 739 PITETVETQKHIISWKNIN--YTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQrvETGVVSGEILIDGHPL 815
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSftYPDQPQPVLKGLSLQIKAGeKVALLGRTGCGKSTLLQLLTR--AWDPQQGEILLNGQPI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 816 TD--EDAFKRSIGFVQQQdLHLDLLSVKESLEISCLLRGDGD-RAYLDTV--SNLLKLPS--DILVAD----LNPTQRKL 884
Cdd:PRK11160 405 ADysEAALRQAISVVSQR-VHLFSATLRDNLLLAAPNASDEAlIEVLQQVglEKLLEDDKglNAWLGEggrqLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 885 LSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTiHQpsKSVISHFDNIFLLKRG 954
Cdd:PRK11160 484 LGIARALLHDAPLLL-LDEPTEGLDAETERQILELLAEHAQNKTVLMIT-HR--LTGLEQFDRICVMDNG 549
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
779-909 |
1.57e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.24 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSQRVETGvvSGEILIDGHPLTDEDAFKRS-----------IGFVQQQDLHLDLLSVKESLEIS 847
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSARLAPD--AGEVHYRMRDGQLRDLYALSeaerrrllrteWGFVHQHPRDGLRMQVSAGGNIG 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324585 848 CLLRGDGDRAY----------LDTVsnllKLPSDILvaDLNPT-------QRklLSIGVELVTKPSlLLFLDEPTSGLD 909
Cdd:PRK11701 114 ERLMAVGARHYgdiratagdwLERV----EIDAARI--DDLPTtfsggmqQR--LQIARNLVTHPR-LVFMDEPTGGLD 183
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
776-912 |
2.11e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.04 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 776 GLTALMGESGAGKTTLLNVLS--QRVEtgvvSGEILIDGHPLTDEDAFKRS--IGfvqqqdlHLD----LLSVKESLEIS 847
Cdd:PRK13539 29 EALVLTGPNGSGKTTLLRLIAglLPPA----AGTIKLDGGDIDDPDVAEAChyLG-------HRNamkpALTVAENLEFW 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 848 CLLRGDGDR---AYLDTV--SNLLKLPSdilvADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEA 912
Cdd:PRK13539 98 AAFLGGEELdiaAALEAVglAPLAHLPF----GYLSAGQKRRVALARLLVSNRPIWI-LDEPTAALDAAA 162
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
751-842 |
2.16e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 56.63 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSqRVeTGVVSGEILIDGHPL----TDEDAFKRSI 825
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGgITALIGPNGAGKSTLLSMIS-RL-LPPDSGEVLVDGLDVattpSRELAKRLAI 79
|
90
....*....|....*...
gi 6324585 826 gfvQQQDLHLDL-LSVKE 842
Cdd:COG4604 80 ---LRQENHINSrLTVRE 94
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
779-923 |
2.75e-08 |
|
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: 56.19 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDGHPLTDEDAFKRSIGFVQQQDLHLDLLSVKESLEISCLLRGDG- 854
Cdd:cd03299 29 VILGPTGSGKSVLLETI-----AGFIkpdSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDk 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324585 855 --DRAYLDTVSNLLKLpSDIL---VADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQL 923
Cdd:cd03299 104 keIERKVLEIAEMLGI-DHLLnrkPETLSGGEQQRVAIARALVVNPKILL-LDEPFSALDVRTKEKLREELKKI 175
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
754-954 |
4.14e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 55.93 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGvvSGEILIDGHPLTD----EDAFKRSigfV 828
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGeVVAILGPNGAGKSTLLRALSGELSPD--SGEVRLNGRPLADwspaELARRRA---V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 829 QQQDLHLDL-LSVKESLE---ISCLLRGDGDRAYLDTVsnllklpsdILVADLNP-TQRKL--LSIG----VEL------ 891
Cdd:PRK13548 81 LPQHSSLSFpFTVEEVVAmgrAPHGLSRAEDDALVAAA---------LAQVDLAHlAGRDYpqLSGGeqqrVQLarvlaq 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324585 892 ---VTKPSLLLFLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCtihqpsksVISH--------FDNIFLLKRG 954
Cdd:PRK13548 152 lwePDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVI--------VVLHdlnlaaryADRIVLLHQG 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
749-954 |
4.15e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 56.35 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 749 HIISWKNINYTV-GTKKLINNASgFISSGLT--ALMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPLTDED--A 820
Cdd:PRK13652 2 HLIETRDLCYSYsGSKEALNNIN-FIAPRNSriAVIGPNGAGKSTLFRHFN-----GILkptSGSVLIRGEPITKENirE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 821 FKRSIGFVQQ------------QD-------LHLDLLSVKEslEISCLLRGDGDRAYLDTVSNllklpsdilvaDLNPTQ 881
Cdd:PRK13652 76 VRKFVGLVFQnpddqifsptveQDiafgpinLGLDEETVAH--RVSSALHMLGLEELRDRVPH-----------HLSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324585 882 RKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQ-GQAIFCTIHQPSkSVISHFDNIFLLKRG 954
Cdd:PRK13652 143 KKRVAIAGVIAMEPQVLV-LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLD-LVPEMADYIYVMDKG 214
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
751-961 |
4.35e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.81 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFI-SSGLTALMGESGAGKTTLLNVLSQRVEtgvVSGEILIDG----------HPLTDED 819
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIyQSKVTAIIGPSGCGKSTFLKCLNRMNE---LESEVRVEGrveffnqniyERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 820 AFKRSIGFVQQQDlHLDLLSVKESLEISCLLRG-------DG-------DRAYLDTVSNllKLPSDILvaDLNPTQRKLL 885
Cdd:PRK14258 85 RLRRQVSMVHPKP-NLFPMSVYDNVAYGVKIVGwrpkleiDDivesalkDADLWDEIKH--KIHKSAL--DLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 886 SIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQ--AIFCTIHQPSKSVISHFDNIFL--LKRGGECVFFG 961
Cdd:PRK14258 160 CIARALAVKPKVLL-MDEPCFGLDPIASMKVESLIQSLRLRSEltMVIVSHNLHQVSRLSDFTAFFKgnENRIGQLVEFG 238
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
765-935 |
5.22e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.21 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 765 LINNASGFISSG-LTALMGESGAGKTTLLNVLSqrvetGV---VSGEILIDGHPLTD------EDAFKRSIGFVQQQDLH 834
Cdd:PRK11629 24 VLHNVSFSIGEGeMMAIVGSSGSGKSTLLHLLG-----GLdtpTSGDVIFNGQPMSKlssaakAELRNQKLGFIYQFHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 835 LDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKL----------PSDilvadLNPTQRKLLSIGVELVTKPSLLLfLDEP 904
Cdd:PRK11629 99 LPDFTALENVAMPLLIGKKKPAEINSRALEMLAAvglehranhrPSE-----LSGGERQRVAIARALVNNPRLVL-ADEP 172
|
170 180 190
....*....|....*....|....*....|..
gi 6324585 905 TSGLDAEAALTIVKFLKQLSL-QGQAIFCTIH 935
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRlQGTAFLVVTH 204
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
43-224 |
5.41e-08 |
|
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: 55.11 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 43 PNPANQLNDITFQAEAGEMVLVLGYP---TSTLFKTLFHGKTSLSysppGSIKFKNNEFKSFSEKcphQIIYNNE----- 114
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSgagKSTLLKLIYKEELPTS----GTIRVNGQDVSDLRGR---AIPYLRRkigvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 115 -QDVHF-PFLTVEQTIDFALSCKFDIPKGERDQIRnELLREFGLSHVLktivgNDFFRGVSGGERKRISIIETFIANGSV 192
Cdd:cd03292 84 fQDFRLlPDRNVYENVAFALEVTGVPPREIRKRVP-AALELVGLSHKH-----RALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190
....*....|....*....|....*....|..
gi 6324585 193 YLWDNSTKGLDSATALDFLEILRKMAKATRSV 224
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTV 189
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
750-935 |
6.86e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.47 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTV--GTKKLiNNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETgvVSGEILIDGHPLTDED----AFK 822
Cdd:PRK13639 1 ILETRDLKYSYpdGTEAL-KGINFKAEKGeMVALLGPNGAGKSTLFLHFNGILKP--TSGEVLIKGEPIKYDKksllEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 823 RSIGFV-QQQDLHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKLPSDILVADLNP-----TQRKLLSIGVELVTKPS 896
Cdd:PRK13639 78 KTVGIVfQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPhhlsgGQKKRVAIAGILAMKPE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 6324585 897 LLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIH 935
Cdd:PRK13639 158 IIV-LDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
750-923 |
7.11e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.12 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTVGTKKLINNASGFISSG--LTaLMGESGAGKTTLLnvlsqRVETGVVSgeilidghplTDEDAFKRS--- 824
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGkiLT-LLGPNGAGKSTLV-----RVVLGLVA----------PDEGVIKRNgkl 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 825 -IGFVQQQdLHLDL---LSVKESLEISCLLRGDGDRAYLDTV--SNLLKLPSDILVAdlNPTQRKLLSIGveLVTKPSLL 898
Cdd:PRK09544 68 rIGYVPQK-LYLDTtlpLTVNRFLRLRPGTKKEDILPALKRVqaGHLIDAPMQKLSG--GETQRVLLARA--LLNRPQLL 142
|
170 180
....*....|....*....|....*
gi 6324585 899 LfLDEPTSGLDAEAALTIVKFLKQL 923
Cdd:PRK09544 143 V-LDEPTQGVDVNGQVALYDLIDQL 166
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
741-923 |
7.44e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.95 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 741 TETVETQKHIISWKNINYTVGTKKL--INNASGFISSGLT-ALMGESGAGKTTLLNVLSQRVEtgVVSGEILIDGHPLTD 817
Cdd:PRK11176 332 KRVIERAKGDIEFRNVTFTYPGKEVpaLRNINFKIPAGKTvALVGRSGSGKSTIANLLTRFYD--IDEGEILLDGHDLRD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 818 ED--AFKRSIGFVQQQdLHL--------------DLLSvKESLE-----------ISCLLRGdgdrayLDTV--SNllkl 868
Cdd:PRK11176 410 YTlaSLRNQVALVSQN-VHLfndtianniayartEQYS-REQIEeaarmayamdfINKMDNG------LDTVigEN---- 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6324585 869 psdilVADLNPTQRKLLSIGVELVtKPSLLLFLDEPTSGLDAEAALTIVKFLKQL 923
Cdd:PRK11176 478 -----GVLLSGGQRQRIAIARALL-RDSPILILDEATSALDTESERAIQAALDEL 526
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
33-219 |
8.09e-08 |
|
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: 56.45 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 33 KKSYDAEDSMPNPAnqLNDITFQAEAGEMVLVLGyPT----STLFKTL--FHGKTSlsysppGSIKFKNNEFKSFSEKCP 106
Cdd:COG1123 267 SKRYPVRGKGGVRA--VDDVSLTLRRGETLGLVG-ESgsgkSTLARLLlgLLRPTS------GSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 107 H------QIIYnneQDVH---FPFLTVEQTIDFALSCKFDIPKGERDQIRNELLREFGLS--------HVLktivgndff 169
Cdd:COG1123 338 RelrrrvQMVF---QDPYsslNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPpdladrypHEL--------- 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6324585 170 rgvSGGERKRISIIETFIANGSVYLWDNSTKGLDSATALDFLEILRKMAK 219
Cdd:COG1123 406 ---SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQR 452
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
777-930 |
8.36e-08 |
|
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: 54.75 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 777 LTALMGESGAGKTTLL-----NVLSQrvetgvvSGEILI--DGHP--LTDEDAF------KRSIGFVQQQdLH------- 834
Cdd:COG4778 39 CVALTGPSGAGKSTLLkciygNYLPD-------SGSILVrhDGGWvdLAQASPReilalrRRTIGYVSQF-LRviprvsa 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 835 LDLlsVKESLeiscLLRGDGDRAYLDTVSNLLK---LPSDIlvADLNPT-------QRklLSIGVELVTKPSLLLfLDEP 904
Cdd:COG4778 111 LDV--VAEPL----LERGVDREEARARARELLArlnLPERL--WDLPPAtfsggeqQR--VNIARGFIADPPLLL-LDEP 179
|
170 180
....*....|....*....|....*.
gi 6324585 905 TSGLDAEAALTIVKFLKQLSLQGQAI 930
Cdd:COG4778 180 TASLDAANRAVVVELIEEAKARGTAI 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
119-219 |
8.91e-08 |
|
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: 54.22 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 119 FPFLTVEQTIDFALscKFDIPKGERDQIrNELLREFGLSHVLKTIVGndffrGVSGGERKRISIIETFIANGSVYLWDNS 198
Cdd:cd03297 87 FPHLNVRENLAFGL--KRKRNREDRISV-DELLDLLGLDHLLNRYPA-----QLSGGEKQRVALARALAAQPELLLLDEP 158
|
90 100
....*....|....*....|.
gi 6324585 199 TKGLDSATALDFLEILRKMAK 219
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKK 179
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
779-910 |
1.27e-07 |
|
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: 55.06 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSQRVE-TGVVSGEILIDGHPLT--DEDAFK----RSIGFVQQqdlhlD-------LLSVKESL 844
Cdd:COG0444 35 GLVGESGSGKSTLARAILGLLPpPGITSGEILFDGEDLLklSEKELRkirgREIQMIFQ-----DpmtslnpVMTVGDQI 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324585 845 EISCLLRGDGDRA-YLDTVSNLLK---LPSDILVADLNPTQrklLS--------IGVELVTKPSLLLfLDEPTSGLDA 910
Cdd:COG0444 110 AEPLRIHGGLSKAeARERAIELLErvgLPDPERRLDRYPHE---LSggmrqrvmIARALALEPKLLI-ADEPTTALDV 183
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
780-954 |
1.88e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.78 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 780 LMGESGAGKTTLLNVLSqrvetGVV--SGEILIDGHPLTDEDAFKRSI--GFVQQQDLHLDLLSVKESLEIS--CLLRGD 853
Cdd:PRK03695 27 LVGPNGAGKSTLLARMA-----GLLpgSGSIQFAGQPLEAWSAAELARhrAYLSQQQTPPFAMPVFQYLTLHqpDKTRTE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 854 GDRAYLDTVSNLLKLpSDILVADLNPT-----QRKLLSiGVELVTKPSL-----LLFLDEPTSGLDA--EAALTivKFLK 921
Cdd:PRK03695 102 AVASALNEVAEALGL-DDKLGRSVNQLsggewQRVRLA-AVVLQVWPDInpagqLLLLDEPMNSLDVaqQAALD--RLLS 177
|
170 180 190
....*....|....*....|....*....|...
gi 6324585 922 QLSLQGQAIFCTIHQPSKSvISHFDNIFLLKRG 954
Cdd:PRK03695 178 ELCQQGIAVVMSSHDLNHT-LRHADRVWLLKQG 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
755-910 |
2.04e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.94 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 755 NINYTVGTKKLinnasgfissgLTALmGESGAGKTTLLNVLSQRVETGvvSGEILIDGHPLTDEDAFKrsiGFVQQQDLH 834
Cdd:PRK11248 19 DINLTLESGEL-----------LVVL-GPSGCGKTTLLNLIAGFVPYQ--HGSITLDGKPVEGPGAER---GVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 835 LDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKLpSDILVAD------LNPTQRKLLSIGVELVTKPSLLLfLDEPTSGL 908
Cdd:PRK11248 82 LPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKK-VGLEGAEkryiwqLSGGQRQRVGIARALAANPQLLL-LDEPFGAL 159
|
..
gi 6324585 909 DA 910
Cdd:PRK11248 160 DA 161
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
51-217 |
2.25e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.36 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 51 DITFQAEAGEMVLVLGyPTSTLFKTLFHGKTSLSYSPPGSIKFKNNEFK--SFSEKCPHQIIYNNEQDVHFPFLTVEQTI 128
Cdd:PRK10895 21 DVSLTVNSGEIVGLLG-PNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLPQEASIFRRLSVYDNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 129 DFALSCKFDIPKGERDQIRNELLREFGLSHVLktivgNDFFRGVSGGERKRISIIETFIANGSVYLWDNSTKGLDSATAL 208
Cdd:PRK10895 100 MAVLQIRDDLSAEQREDRANELMEEFHIEHLR-----DSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
....*....
gi 6324585 209 DFLEILRKM 217
Cdd:PRK10895 175 DIKRIIEHL 183
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
762-939 |
2.35e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.90 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 762 TKKLINNAsgfissgLTALMGESGAGKTTLLNVLSQRVETG----VVSGEILIDGHPLTDEDAFK--RSIGFVQQQDLHL 835
Cdd:PRK14246 30 TIKIPNNS-------IFGIMGPSGSGKSTLLKVLNRLIEIYdskiKVDGKVLYFGKDIFQIDAIKlrKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 836 DLLSVKESLEISCLLRGDGDRAYLDTVSN-------LLKLPSDIL---VADLNPTQRKLLSIGVELVTKPSLLLfLDEPT 905
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEeclrkvgLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLL-MDEPT 181
|
170 180 190
....*....|....*....|....*....|....
gi 6324585 906 SGLDAEAALTIVKFLKQLSLQgQAIFCTIHQPSK 939
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQ 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
777-954 |
2.48e-07 |
|
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: 53.24 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 777 LTALMGESGAGKTTLLNVLSQRVE-TGvvsGEILIDGHPLTDEDA--FKRSIGFVQQQDLhLDLLSVKE-------SLEI 846
Cdd:cd03248 42 VTALVGPSGSGKSTVVALLENFYQpQG---GQVLLDGKPISQYEHkyLHSKVSLVGQEPV-LFARSLQDniayglqSCSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 847 SCLLRGdGDRAYLDTVSNLLKLPSDILV----ADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIvkflkq 922
Cdd:cd03248 118 ECVKEA-AQKAHAHSFISELASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLI-LDEATSALDAESEQQV------ 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 6324585 923 lslqGQAIFCTIHQPSKSVISH-------FDNIFLLKRG 954
Cdd:cd03248 190 ----QQALYDWPERRTVLVIAHrlstverADQILVLDGG 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
49-259 |
2.51e-07 |
|
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: 53.27 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLfhgktsLSYSPP--GSIKFKNNEFKSFSEKCPHQIIYNN----EQDVH 118
Cdd:cd03261 16 LKGVDLDVRRGEILAIIG-PSgsgkSTLLRLI------VGLLRPdsGEVLIDGEDISGLSEAELYRLRRRMgmlfQSGAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 119 FPFLTVEQTIDFALSCKFDIPKGERDQIRNELLREFGLSHVLKTIVGNdffrgVSGGERKRISIIETFIANGSVYLWDNS 198
Cdd:cd03261 89 FDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324585 199 TKGLDSATALDFLEILRKMAKATRSVNLVrIS---QASDKIVdkfDKILMLSDSYQLFYGTVDE 259
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSLKKELGLTSIM-VThdlDTAFAIA---DRIAVLYDGKIVAEGTPEE 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
40-247 |
2.65e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 53.84 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 40 DSMPNPAnqLNDITFQAEAGEMVLVLGYPTStlfktlfhGKTSLS------YSP-PGSIKFKNNEFKsfSEKCPH----- 107
Cdd:PRK13632 18 PNSENNA--LKNVSFEINEGEYVAILGHNGS--------GKSTISkiltglLKPqSGEIKIDGITIS--KENLKEirkki 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 108 QIIYNNEqDVHFPFLTVEQTIDFALSCKfDIPKGERDQIRNELLREFGLSHVLKTIVGNdffrgVSGGERKRISIIETFI 187
Cdd:PRK13632 86 GIIFQNP-DNQFIGATVEDDIAFGLENK-KVPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----LSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 188 ANGSVYLWDNSTKGLDSATALDFLEILRKMAKaTRSVNLVRISQASDKIVdKFDKILMLS 247
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRK-TRKKTLISITHDMDEAI-LADKVIVFS 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
750-909 |
2.80e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.55 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTV--GT---KKLINNAS-----G-FISsgltaLMGESGAGKTTLLNVLSqrvetGVV---SGEILIDGHPL 815
Cdd:COG1101 1 MLELKNLSKTFnpGTvneKRALDGLNltieeGdFVT-----VIGSNGAGKSTLLNAIA-----GSLppdSGSILIDGKDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 816 TDEDAFKRS--IGFVQQqdlhlD-------LLSVKESLEIScLLRG----------DGDRAYL-DTVSNL-LKLPS--DI 872
Cdd:COG1101 71 TKLPEYKRAkyIGRVFQ-----DpmmgtapSMTIEENLALA-YRRGkrrglrrgltKKRRELFrELLATLgLGLENrlDT 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 6324585 873 LVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLD 909
Cdd:COG1101 145 KVGLLSGGQRQALSLLMATLTKPKLLL-LDEHTAALD 180
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
748-940 |
2.80e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.31 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 748 KHIISWKNINYTVGTKKLINNASGFI-SSGLTALMGESGAGKTTLL---NVLSQRVETGVVSGEILIDGHPLTDEDA--- 820
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIpQNGVFALMGPSGCGKSTLLrtfNRLLELNEEARVEGEVRLFGRNIYSPDVdpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 821 -FKRSIGFVQQQDLHLDLLSVKESLEISC----LLRGDGD-----------RAYLDTVSNLLK-LPSdilvaDLNPTQRK 883
Cdd:PRK14267 82 eVRREVGMVFQYPNPFPHLTIYDNVAIGVklngLVKSKKEldervewalkkAALWDEVKDRLNdYPS-----NLSGGQRQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6324585 884 LLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTiHQPSKS 940
Cdd:PRK14267 157 RLVIARALAMKPKILL-MDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSPAQA 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
782-910 |
3.12e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.27 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 782 GESGAGKTTLLnvlsqRVETG---VVSGEILIDGHPLTDEDAFKRSIGFVQQQDLHLDLLSVKESLEISCLLRGdGDRAY 858
Cdd:PRK11000 36 GPSGCGKSTLL-----RMIAGledITSGDLFIGEKRMNDVPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAG-AKKEE 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 6324585 859 LDT----VSNLLKLPS--DILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDA 910
Cdd:PRK11000 110 INQrvnqVAEVLQLAHllDRKPKALSGGQRQRVAIGRTLVAEPSVFL-LDEPLSNLDA 166
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
49-261 |
3.31e-07 |
|
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: 53.00 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLFHGKTSLSysppGSIKFKNNEFKS-------------------FSEKC 105
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVG-PSgsgkSTILRLLFRFYDVSS----GSILIDGQDIREvtldslrraigvvpqdtvlFNDTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 106 PHQIIYNNeqdvhfPFLTVEQTIDFALSCkfdipkgerdQIRNELLR-EFGLShvlkTIVGNdffRGV--SGGERKRISI 182
Cdd:cd03253 92 GYNIRYGR------PDATDEEVIEAAKAA----------QIHDKIMRfPDGYD----TIVGE---RGLklSGGEKQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 183 IETFIANGSVYLWDNSTKGLDSATALDFLEILRKMAKATRSV----NLVRISQAsdkivdkfDKILMLSDSYQLFYGTVD 258
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIviahRLSTIVNA--------DKIIVLKDGRIVERGTHE 220
|
...
gi 6324585 259 ECL 261
Cdd:cd03253 221 ELL 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
49-203 |
3.32e-07 |
|
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: 52.93 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPTSTlfktlfhGKTSLSYSPPGSIKfknnefksfsekcPHQ-IIYNNEQDV-HFPF----- 121
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLG-PNGA-------GKTTTFYMIVGLVK-------------PDSgKILLDGQDItKLPMhkrar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 122 ---------------LTVEQTIDFALSCKFDiPKGERDQIRNELLREFGLSHVLKTivgndFFRGVSGGERKRISIIETF 186
Cdd:cd03218 75 lgigylpqeasifrkLTVEENILAVLEIRGL-SKKEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARAL 148
|
170
....*....|....*..
gi 6324585 187 IANGSVYLWDNSTKGLD 203
Cdd:cd03218 149 ATNPKFLLLDEPFAGVD 165
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
49-237 |
3.99e-07 |
|
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: 52.62 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTL--FHGKTSlsysppGSIKFKNNEFKSFSEKCPHQIIYNNEQDVHFPFL 122
Cdd:cd03251 18 LRDISLDIPAGETVALVG-PSgsgkSTLVNLIprFYDVDS------GRILIDGHDVRDYTLASLRRQIGLVSQDVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 123 TVEQTIDFAlscKFDIPKGE-RDQIRNELLREF--GLSHVLKTIVGNdffRGV--SGGERKRISIIETFIANGSVYLWDN 197
Cdd:cd03251 91 TVAENIAYG---RPGATREEvEEAARAANAHEFimELPEGYDTVIGE---RGVklSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6324585 198 STKGLDSAT------ALDFLeilrkMAKATRSVNLVRIS--QASDKIV 237
Cdd:cd03251 165 ATSALDTESerlvqaALERL-----MKNRTTFVIAHRLStiENADRIV 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
751-950 |
4.09e-07 |
|
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: 50.91 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETgvVSGEILIDGhpltdedafKRSIGFVQ 829
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGdRIGLVGRNGAGKSTLLKLIAGELEP--DEGIVTWGS---------TVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 830 QqdlhldlLSvkesleiscllrgDGDRAyldtvsnllklpsdilvadlnptqRKLLSIGveLVTKPSLLLfLDEPTSGLD 909
Cdd:cd03221 70 Q-------LS-------------GGEKM------------------------RLALAKL--LLENPNLLL-LDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6324585 910 AEAALTIVKFLKQlsLQGQAIFctihqpsksvISHfDNIFL 950
Cdd:cd03221 103 LESIEALEEALKE--YPGTVIL----------VSH-DRYFL 130
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
751-923 |
5.33e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 53.27 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNIN--YTVGTKKLI--NNASGFISSG-LTALMGESGAGKTTLL---NVLSQRvetgvVSGEILIDGHPLT--DED- 819
Cdd:PRK11153 2 IELKNISkvFPQGGRTIHalNNVSLHIPAGeIFGVIGASGAGKSTLIrciNLLERP-----TSGRVLVDGQDLTalSEKe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 820 --AFKRSIGFVQQqdlHLDLLS-------VKESLEISCLLRGDGDRayldTVSNLLKL-----PSDILVADLNPTQRKLL 885
Cdd:PRK11153 77 lrKARRQIGMIFQ---HFNLLSsrtvfdnVALPLELAGTPKAEIKA----RVTELLELvglsdKADRYPAQLSGGQKQRV 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 6324585 886 SIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQL 923
Cdd:PRK11153 150 AIARALASNPKVLL-CDEATSALDPATTRSILELLKDI 186
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
759-944 |
5.96e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 759 TVGTKKLINNASGFISSGLT-ALMGESGAGKTT----LLNVLSQRvetgvvsGEILIDGHPLTDED-----AFKRSIGFV 828
Cdd:PRK15134 295 TVDHNVVVKNISFTLRPGETlGLVGESGSGKSTtglaLLRLINSQ-------GEIWFDGQPLHNLNrrqllPVRHRIQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 829 QQqDLHLDL---LSVKESLEiscllrgDGDRAYLDTVSNLLKLPSDILVAD---LNPT------------QRKLLSIGVE 890
Cdd:PRK15134 368 FQ-DPNSSLnprLNVLQIIE-------EGLRVHQPTLSAAQREQQVIAVMEevgLDPEtrhrypaefsggQRQRIAIARA 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6324585 891 LVTKPSLLLfLDEPTSGLDAEAALTIVKFLKqlSLQGQaifctiHQPSKSVISH 944
Cdd:PRK15134 440 LILKPSLII-LDEPTSSLDKTVQAQILALLK--SLQQK------HQLAYLFISH 484
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
776-930 |
8.23e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.48 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 776 GLTALMGesgAGKTTLLNVLSqrvetGV---VSGEILIDGHPL---TDEDAFKRSIGFV----QQQDLHLDLlSVKESLE 845
Cdd:COG1129 282 GIAGLVG---AGRTELARALF-----GAdpaDSGEIRLDGKPVrirSPRDAIRAGIAYVpedrKGEGLVLDL-SIRENIT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 846 ISCL--------LRGDGDRAYLDTVSNLL--KLPS-DILVADL---NptQRKLLsIGVELVTKPSLLLfLDEPTSGLDAE 911
Cdd:COG1129 353 LASLdrlsrgglLDRRRERALAEEYIKRLriKTPSpEQPVGNLsggN--QQKVV-LAKWLATDPKVLI-LDEPTRGIDVG 428
|
170
....*....|....*....
gi 6324585 912 AALTIVKFLKQLSLQGQAI 930
Cdd:COG1129 429 AKAEIYRLIRELAAEGKAV 447
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
33-219 |
8.25e-07 |
|
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: 51.74 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 33 KKSYDaEDSMPNPAnqLNDITFQAEAGEMVLVLGyPT----STLFKTL--FHGKTSlsysppGSIKFKNNEFKSFSEKCP 106
Cdd:cd03257 8 SVSFP-TGGGSVKA--LDDVSFSIKKGETLGLVG-ESgsgkSTLARAIlgLLKPTS------GSIIFDGKDLLKLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 107 H------QIIYnneQDVHF---PFLTVEQTIDFALSCKF-DIPKGERDQIRNELLREFGLShvlkTIVGNDFFRGVSGGE 176
Cdd:cd03257 78 KirrkeiQMVF---QDPMSslnPRMTIGEQIAEPLRIHGkLSKKEARKEAVLLLLVGVGLP----EEVLNRYPHELSGGQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6324585 177 RKRISIIETFIANGSVYLWDNSTKGLDSATALDFLEILRKMAK 219
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQE 193
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
773-937 |
8.90e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.96 E-value: 8.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 773 ISSG-LTALMGESGAGKTTLLNV---LSQRVEtgvvsGEILIDGHPL-TDEDAFkrsigfvqQQDL----HL----DLLS 839
Cdd:PRK13538 24 LNAGeLVQIEGPNGAGKTSLLRIlagLARPDA-----GEVLWQGEPIrRQRDEY--------HQDLlylgHQpgikTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 840 VKESLEISCLLRGDGDR----AYLDTVSnlLKLPSDILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAalt 915
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDealwEALAQVG--LAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWI-LDEPFTAIDKQG--- 164
|
170 180
....*....|....*....|....*..
gi 6324585 916 iVKFLKQLSLQ-----GQAIFcTIHQP 937
Cdd:PRK13538 165 -VARLEALLAQhaeqgGMVIL-TTHQD 189
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
778-909 |
1.31e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 50.91 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 778 TALMGESGAGKTTLLNVLSqrvetG---VVSGEILIDGHPLTDEDAFKR--SIGFvQQQDL--HldlLSVKE--SLEISC 848
Cdd:COG3840 28 VAILGPSGAGKSTLLNLIA-----GflpPDSGRILWNGQDLTALPPAERpvSMLF-QENNLfpH---LTVAQniGLGLRP 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324585 849 LLR-GDGDRAYLDTV------SNLLK-LPsdilvADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLD 909
Cdd:COG3840 99 GLKlTAEQRAQVEQAlervglAGLLDrLP-----GQLSGGQRQRVALARCLVRKRPILL-LDEPFSALD 161
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
727-930 |
1.58e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 727 NKEMALNDYNEQPITETVETQKHIISWKNinytvgtkKLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTGV-- 803
Cdd:PRK09700 248 NRFNAMKENVSNLAHETVFEVRNVTSRDR--------KKVRDISFSVCRGeILGFAGLVGSGRTELMNCL-----FGVdk 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 804 -VSGEILIDG---HPLTDEDAFKRSIGFV---QQQDLHLDLLSVKESLEISCLLRGDG------------DRAYLDTVSN 864
Cdd:PRK09700 315 rAGGEIRLNGkdiSPRSPLDAVKKGMAYItesRRDNGFFPNFSIAQNMAISRSLKDGGykgamglfhevdEQRTAENQRE 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 865 LLKLPSDILVADLNP----TQRKLLsIGVELVTKPSLLLFlDEPTSGLDAEAALTIVKFLKQLSLQGQAI 930
Cdd:PRK09700 395 LLALKCHSVNQNITElsggNQQKVL-ISKWLCCCPEVIIF-DEPTRGIDVGAKAEIYKVMRQLADDGKVI 462
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
763-935 |
1.67e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.05 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 763 KKLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDghpltDEDA--------FKRSIGFVQQ 830
Cdd:PRK10895 16 RRVVEDVSLTVNSGeIVGLLGPNGAGKTTTFYMV-----VGIVprdAGNIIID-----DEDIsllplharARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 831 QDLHLDLLSVKESLEISCLLRGD------GDRA-YLDTVSNLLKLpSDILVADLNPTQRKLLSIGVELVTKPSLLLfLDE 903
Cdd:PRK10895 86 EASIFRRLSVYDNLMAVLQIRDDlsaeqrEDRAnELMEEFHIEHL-RDSMGQSLSGGERRRVEIARALAANPKFIL-LDE 163
|
170 180 190
....*....|....*....|....*....|..
gi 6324585 904 PTSGLDAEAALTIVKFLKQLSLQGQAIFCTIH 935
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
756-964 |
1.78e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.25 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 756 INYTVG--TKKLINNAS-GFISSGLTALMGESGAGKTTL---LNVLSQRVETGVVSGEILIDGHPL---TDEDAFKRSIG 826
Cdd:PRK14271 25 VNLTLGfaGKTVLDQVSmGFPARAVTSLMGPTGSGKTTFlrtLNRMNDKVSGYRYSGDVLLGGRSIfnyRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 827 FVQQQ------DLHLDLLSVKESLEISCLLRGDGDRAYLDTVSNLLKLPSDILVAD---LNPTQRKLLSIGVELVTKPSL 897
Cdd:PRK14271 105 MLFQRpnpfpmSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324585 898 LLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSKSVISHFDNIFLlkrGGECVFFGPMD 964
Cdd:PRK14271 185 LL-LDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFF---DGRLVEEGPTE 247
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
779-954 |
1.91e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 52.27 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLsQRVETGvVSGEILIDGHPLTD--EDAFKRSIGFVQQQDLHLDlLSVKESLEISCL------L 850
Cdd:PRK13657 365 AIVGPTGAGKSTLINLL-QRVFDP-QSGRILIDGTDIRTvtRASLRRNIAVVFQDAGLFN-RSIEDNIRVGRPdatdeeM 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 851 RGDGDRAY-LDTV-SNLLKLpsDILVAD----LNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLS 924
Cdd:PRK13657 442 RAAAERAQaHDFIeRKPDGY--DTVVGErgrqLSGGERQRLAIARALLKDPPILI-LDEATSALDVETEAKVKAALDELM 518
|
170 180 190
....*....|....*....|....*....|
gi 6324585 925 lQGQAIFCTIHQpsKSVISHFDNIFLLKRG 954
Cdd:PRK13657 519 -KGRTTFIIAHR--LSTVRNADRILVFDNG 545
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
778-954 |
2.07e-06 |
|
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: 50.18 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 778 TALMGESGAGKTTLLNVLSQrVETGvVSGEILIDGHPLTDEDAFKRSIGFV-QQQDL--HLDL-----LSVKESLEISCL 849
Cdd:cd03298 27 TAIVGPSGSGKSTLLNLIAG-FETP-QSGRVLINGVDVTAAPPADRPVSMLfQENNLfaHLTVeqnvgLGLSPGLKLTAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 850 LRGDGDRAYLDT-VSNLLK-LPSdilvaDLNPTQRKLLSIGVELV-TKPSLLlfLDEPTSGLDA---EAALTIVkfLKQL 923
Cdd:cd03298 105 DRQAIEVALARVgLAGLEKrLPG-----ELSGGERQRVALARVLVrDKPVLL--LDEPFAALDPalrAEMLDLV--LDLH 175
|
170 180 190
....*....|....*....|....*....|.
gi 6324585 924 SLQGQAIFCTIHQPSKSViSHFDNIFLLKRG 954
Cdd:cd03298 176 AETKMTVLMVTHQPEDAK-RLAQRVVFLDNG 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
779-922 |
2.43e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSQRVETGvvSGEILIDGHPL---TDEDAFKRSIGFVQQQdlhLDLL---SVKESLEISCL-LR 851
Cdd:PRK10982 28 ALMGENGAGKSTLLKCLFGIYQKD--SGSILFQGKEIdfkSSKEALENGISMVHQE---LNLVlqrSVMDNMWLGRYpTK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 852 G---DGDRAYLDTVSNLLKLPSDI----LVADLNPTQRKLLSIGvELVTKPSLLLFLDEPTSGL---DAEAALTIVKFLK 921
Cdd:PRK10982 103 GmfvDQDKMYRDTKAIFDELDIDIdpraKVATLSVSQMQMIEIA-KAFSYNAKIVIMDEPTSSLtekEVNHLFTIIRKLK 181
|
.
gi 6324585 922 Q 922
Cdd:PRK10982 182 E 182
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
746-935 |
2.85e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 746 TQKHIISWKNINYTVGTKKLINNASGFISSGLT-ALMGESGAGKTTLLNVLSQRVETGVVSGEILIDGHPLTDEDAFKRS 824
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIhAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 825 igfvqqqdlHLDL-LSVKESLEISCLLRGDGDRAYLDTVSNLLKLP-----------SDIL-VADLNPT----------- 880
Cdd:CHL00131 83 ---------HLGIfLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPeldplefleiiNEKLkLVGMDPSflsrnvnegfs 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6324585 881 --QRKLLSIgVELVTKPSLLLFLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIH 935
Cdd:CHL00131 154 ggEKKRNEI-LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
750-954 |
3.58e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.50 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYT------VGTKKLINNASGFISSGLTALMGESGAGKTTLL---NVLSQRVETGVVSGEILIDGHPLTDE-D 819
Cdd:PRK13643 1 MIKFEKVNYTyqpnspFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLqhlNGLLQPTEGKVTVGDIVVSSTSKQKEiK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 820 AFKRSIGFVQQ--------QDLHLDLLSVKESLEIScllRGDGDRAYLDTVSnLLKLPSDILVA---DLNPTQRKLLSIG 888
Cdd:PRK13643 81 PVRKKVGVVFQfpesqlfeETVLKDVAFGPQNFGIP---KEKAEKIAAEKLE-MVGLADEFWEKspfELSGGQMRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 889 VELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQpSKSVISHFDNIFLLKRG 954
Cdd:PRK13643 157 GILAMEPEVLV-LDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHL-MDDVADYADYVYLLEKG 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
41-272 |
3.78e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 50.08 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 41 SMPNPANQLNDITFQAEAGEMVLVLGyPT----STLF------------KTLFHGKTsLSYSPPGSIKFKNNEfksfsek 104
Cdd:PRK13639 10 SYPDGTEALKGINFKAEKGEMVALLG-PNgagkSTLFlhfngilkptsgEVLIKGEP-IKYDKKSLLEVRKTV------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 105 cphQIIYNNEQDVHF-PflTVEQTIDFAlSCKFDIPKGERDQIRNELLREFGLSHVLKTIVGNdffrgVSGGERKRISII 183
Cdd:PRK13639 81 ---GIVFQNPDDQLFaP--TVEEDVAFG-PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHH-----LSGGQKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 184 ETFIANGSVYLWDNSTKGLDSATALDFLEILRKMAK-------ATRSVNLVRISQasdkivdkfDKILMLSDSYQLFYGT 256
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegitiiiSTHDVDLVPVYA---------DKVYVMSDGKIIKEGT 220
|
250
....*....|....*.
gi 6324585 257 VDECltyFRDTLGIEK 272
Cdd:PRK13639 221 PKEV---FSDIETIRK 233
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
750-917 |
3.95e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 750 IISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGVVSGEILIDGHPLTDED--------- 819
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGeVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSpedragegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 820 --AFKRSI---GFVQQQDLHLDLLSVKESLEISCLLRGDGDRaYLDTVSNLLKLPSDILVADLN----PTQRKLLSIGVE 890
Cdd:PRK09580 81 fmAFQYPVeipGVSNQFFLQTALNAVRSYRGQEPLDRFDFQD-LMEEKIALLKMPEDLLTRSVNvgfsGGEKKRNDILQM 159
|
170 180
....*....|....*....|....*..
gi 6324585 891 LVTKPSLLLfLDEPTSGLDAEaALTIV 917
Cdd:PRK09580 160 AVLEPELCI-LDESDSGLDID-ALKIV 184
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
768-950 |
4.53e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.97 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 768 NASGFISsgltaLMGESGAGKTTLL---NVLSQRVE-TGVVSGEILidgHPLTDEDAFKRSIGFVQQQDL---------H 834
Cdd:PRK10619 29 NAGDVIS-----IIGSSGSGKSTFLrciNFLEKPSEgSIVVNGQTI---NLVRDKDGQLKVADKNQLRLLrtrltmvfqH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 835 LDLLSVKESLE--------ISCLLRGDG-DRA--YLDTV----SNLLKLPsdilvADLNPTQRKLLSIGVELVTKPSLLL 899
Cdd:PRK10619 101 FNLWSHMTVLEnvmeapiqVLGLSKQEArERAvkYLAKVgideRAQGKYP-----VHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6324585 900 FlDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQP--SKSVISHFdnIFL 950
Cdd:PRK10619 176 F-DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMgfARHVSSHV--IFL 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-219 |
5.88e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.59 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 13 GSLTFNgaNIQFGADAQgeskksydaedsmPNPAnqLNDITFQAEAGEMVLVLGyPT----STLFKTLfhgktSLSYSP- 87
Cdd:PRK11160 337 VSLTLN--NVSFTYPDQ-------------PQPV--LKGLSLQIKAGEKVALLG-RTgcgkSTLLQLL-----TRAWDPq 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 88 PGSIKFKNNEFKSFSEKCPHQIIYNNEQDVHFPFLTVEQTIDFAlsckfdIPKGERDQIRnELLREFGLSHVLKTIVGND 167
Cdd:PRK11160 394 QGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLA------APNASDEALI-EVLQQVGLEKLLEDDKGLN 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6324585 168 FF-----RGVSGGERKRISIIETFIANGSVYLWDNSTKGLDSATALDFLEILRKMAK 219
Cdd:PRK11160 467 AWlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ 523
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
749-922 |
6.23e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 49.26 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 749 HIISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTGVV---SGEILIDGHPLTDEDAFKRS 824
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGeIVGLLGPNGAGKTTTFYMI-----VGLVkpdSGRIFLDGEDITHLPMHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 825 ---IGFVQQQ-----DlhldlLSVKESLeiscllrgdgdRAYLDTvsnlLKLPS-------DILVADLNPTQRK-----L 884
Cdd:COG1137 77 rlgIGYLPQEasifrK-----LTVEDNI-----------LAVLEL----RKLSKkereerlEELLEEFGITHLRkskayS 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6324585 885 LSIG----VE----LVTKPSLLLfLDEPTSGLDAEAAL---TIVKFLKQ 922
Cdd:COG1137 137 LSGGerrrVEiaraLATNPKFIL-LDEPFAGVDPIAVAdiqKIIRHLKE 184
|
|
| PDR_CDR |
pfam06422 |
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters ... |
1328-1362 |
7.78e-06 |
|
CDR ABC transporter; Corresponds to a region of the PDR/CDR subgroup of ABC transporters comprising extracellular loop 3, transmembrane segment 6 and linker region.
Pssm-ID: 461906 [Multi-domain] Cd Length: 92 Bit Score: 45.53 E-value: 7.78e-06
10 20 30
....*....|....*....|....*....|....*..
gi 6324585 1328 GDDFLKNE-NMSYDHVWRNFGIEWAF-VGFNFFAMFA 1362
Cdd:pfam06422 31 GDDYLAASyGYSYSHLWRNFGILIAFwIFFLALYLIA 67
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
774-954 |
1.04e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.10 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 774 SSGLTALMGESGAGKTTLLNVLsqrveTG---VVSGEILIDGHPLT--DEDAFKRSIGFVQQQDLHL------------- 835
Cdd:PRK10790 366 SRGFVALVGHTGSGKSTLASLL-----MGyypLTEGEIRLDGRPLSslSHSVLRQGVAMVQQDPVVLadtflanvtlgrd 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 836 ----DLLSVKESLEISCLLRG--DGDRAYLDTVSNllklpsdilvaDLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLD 909
Cdd:PRK10790 441 iseeQVWQALETVQLAELARSlpDGLYTPLGEQGN-----------NLSVGQKQLLALARVLVQTPQILI-LDEATANID 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6324585 910 AEAALTIVKFLKQLSLQGQAIfctihqpsksVISH-------FDNIFLLKRG 954
Cdd:PRK10790 509 SGTEQAIQQALAAVREHTTLV----------VIAHrlstiveADTILVLHRG 550
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
49-262 |
1.37e-05 |
|
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: 48.05 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTL--FHGKTSlsysppGSIKFKNNEFKSFSEKcphqiiynnEQDVH---- 118
Cdd:COG1127 21 LDGVSLDVPRGEILAIIG-GSgsgkSVLLKLIigLLRPDS------GEILVDGQDITGLSEK---------ELYELrrri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 119 ---------FPFLTVEQTIDFALSCKFDIPKGERDQIRNELLREFGLSHVlktivgNDFF-RGVSGGERKRISIIETFIA 188
Cdd:COG1127 85 gmlfqggalFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGA------ADKMpSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 189 NGSVYLWDNSTKGLDSATALDFLEILRKMAKA--------TRSVNLVRisqasdKIVdkfDKILMLSDSYQLFYGTVDEC 260
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDElgltsvvvTHDLDSAF------AIA---DRVAVLADGKIIAEGTPEEL 229
|
..
gi 6324585 261 LT 262
Cdd:COG1127 230 LA 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
773-937 |
1.92e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.95 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 773 ISSG-LTALMGESGAGKTTLLNVLsqrvetGVV----SGEILIDGHPLT--DEDAFKR----SIGFVQQQDLHLDLLSVK 841
Cdd:PRK10535 31 IYAGeMVAIVGASGSGKSTLMNIL------GCLdkptSGTYRVAGQDVAtlDADALAQlrreHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 842 ESLEISCLLRGDGDRAYLDTVSNLL-KL---------PSDilvadLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAE 911
Cdd:PRK10535 105 QNVEVPAVYAGLERKQRLLRAQELLqRLgledrveyqPSQ-----LSGGQQQRVSIARALMNGGQVIL-ADEPTGALDSH 178
|
170 180
....*....|....*....|....*.
gi 6324585 912 AALTIVKFLKQLSLQGQAIFCTIHQP 937
Cdd:PRK10535 179 SGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
780-935 |
2.04e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.56 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 780 LMGESGAGKTTLLNVLS--QRVEtgvvSGEILIDGHPLT----DEDAF-KRSIGFVqQQDLHLDL-LSVKESLEISCLLR 851
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICgiERPS----AGKIWFSGHDITrlknREVPFlRRQIGMI-FQDHHLLMdRTVYDNVAIPLIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 852 G----DGDR---AYLDTVSNLLKLPSdiLVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEAALTIVKFLKQLS 924
Cdd:PRK10908 108 GasgdDIRRrvsAALDKVGLLDKAKN--FPIQLSGGEQQRVGIARAVVNKPAVLL-ADEPTGNLDDALSEGILRLFEEFN 184
|
170
....*....|.
gi 6324585 925 LQGQAIFCTIH 935
Cdd:PRK10908 185 RVGVTVLMATH 195
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
747-824 |
2.44e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.48 E-value: 2.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324585 747 QKHIISWKNINYTVGTKKLInnasgfissgltALMGESGAGKTTLLNVLSQRVETgvVSGEILIDGHPLTDEDAFKRS 824
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTL------------AIIGENGSGKSTLAKMLAGMIEP--TSGELLIDDHPLHFGDYSYRS 86
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
49-259 |
2.66e-05 |
|
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: 47.54 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGYPTStlfktlfhGKTSLSYS-----PPGSIKFKNNEFKSFSEKCP--------HQIIYNNEQ 115
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGS--------GKTSLLMLilgelEPSEGKIKHSGRISFSSQFSwimpgtikENIIFGVSY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 116 DvHFPFLTVEQtidfALSCKFDIPK-GERDqirNELLREFGLShvlktivgndffrgVSGGERKRISIIETFIANGSVYL 194
Cdd:cd03291 125 D-EYRYKSVVK----ACQLEEDITKfPEKD---NTVLGEGGIT--------------LSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324585 195 WDNSTKGLDSATALDFLE--ILRKMAKATRSVNLVRISQasdkiVDKFDKILMLSDSYQLFYGTVDE 259
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFEscVCKLMANKTRILVTSKMEH-----LKKADKILILHEGSSYFYGTFSE 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
725-965 |
3.47e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 48.14 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 725 PSNKEMALNdyneqpITETVETQKHIISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVEtgV 803
Cdd:COG0488 296 RRDKTVEIR------FPPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGdRIGLIGPNGAGKSTLLKLLAGELE--P 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 804 VSGEILIdGHPLTdedafkrsIGFVQQqdlHLDLLSVKESL--EISCLLRGDGDRayldTVSNLLKL----PSDIL--VA 875
Cdd:COG0488 368 DSGTVKL-GETVK--------IGYFDQ---HQEELDPDKTVldELRDGAPGGTEQ----EVRGYLGRflfsGDDAFkpVG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 876 DLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAEA--ALT--IVKFlkqlslQGQAIFctihqpsksvISH---F--- 945
Cdd:COG0488 432 VLSGGEKARLALAKLLLSPPNVLL-LDEPTNHLDIETleALEeaLDDF------PGTVLL----------VSHdryFldr 494
|
250 260
....*....|....*....|..
gi 6324585 946 --DNIFLLKRGGECVFFGPMDD 965
Cdd:COG0488 495 vaTRILEFEDGGVREYPGGYDD 516
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
49-223 |
3.97e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.00 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPTSTlfktlfhGKTSL-----SYSPP--GSIKFKNNEFKSFSEKcpHQIIYNNEQdvHFPF 121
Cdd:PRK11248 17 LEDINLTLESGELLVVLG-PSGC-------GKTTLlnliaGFVPYqhGSITLDGKPVEGPGAE--RGVVFQNEG--LLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 122 LTVEQTIDFALSCKfDIPKGERDQIRNELLREFGLSHVlktivGNDFFRGVSGGERKRISIIETFIANGSVYLWDNSTKG 201
Cdd:PRK11248 85 RNVQDNVAFGLQLA-GVEKMQRLEIAHQMLKKVGLEGA-----EKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180
....*....|....*....|..
gi 6324585 202 LDSATALDFLEILRKMAKATRS 223
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGK 180
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1114-1278 |
4.23e-05 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 47.38 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1114 IFFCFMALCVSSPLINQIQDKALKTKEVYVAREARSNTYhwtvlLLSQSIIELPLALTSSTLFFVCAFfSCGFNNAGWsa 1193
Cdd:pfam12698 167 ILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQY-----WLGKILGDFLVGLLQLLIILLLLF-GIGIPFGNL-- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 1194 GVFFLNYMLFAAYYSTLGLWLIYTAPNLQTAAVFVAFIYSFTASFCGVMQPYSLFPTFWKFMYRVSPYTYFVETFVSILL 1273
Cdd:pfam12698 239 GLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLIY 318
|
....*..
gi 6324585 1274 --HNWEI 1278
Cdd:pfam12698 319 gdSLWEI 325
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
49-261 |
5.33e-05 |
|
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: 46.06 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPTSTlfktlfhGKTSLS------YSP-PGSIKFKNNEFKSFSEKCPHQIIYNNEQDvhfPF 121
Cdd:cd03254 19 LKDINFSIKPGETVAIVG-PTGA-------GKTTLInllmrfYDPqKGQILIDGIDIRDISRKSLRSMIGVVLQD---TF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 122 L---TVEQTIdfalscKFDIPKGERDQIrNELLREFGLSHVLK-------TIVGNdffRG--VSGGERKRISIIETFIAN 189
Cdd:cd03254 88 LfsgTIMENI------RLGRPNATDEEV-IEAAKEAGAHDFIMklpngydTVLGE---NGgnLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324585 190 GSVYLWDNSTKGLDSATALDFLEILRKMAKATRSVNLV-RISqasdkIVDKFDKILMLSDSYQLFYGTVDECL 261
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAhRLS-----TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
732-909 |
5.33e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 47.14 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 732 LNDYNEQPITETVETQKHIISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQrVETGvVSGEILI 810
Cdd:PRK11607 1 MNDAIPRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGeIFALLGASGCGKSTLLRMLAG-FEQP-TAGQIML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 811 DGHPLTDEDAFKRSIGFVQQQDLHLDLLSVKESleISCLLRGDG-DRAYL-DTVSNLLKLPSDILVADLNP-----TQRK 883
Cdd:PRK11607 79 DGVDLSHVPPYQRPINMMFQSYALFPHMTVEQN--IAFGLKQDKlPKAEIaSRVNEMLGLVHMQEFAKRKPhqlsgGQRQ 156
|
170 180
....*....|....*....|....*.
gi 6324585 884 LLSIGVELVTKPSLLLfLDEPTSGLD 909
Cdd:PRK11607 157 RVALARSLAKRPKLLL-LDEPMGALD 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
780-944 |
5.57e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 780 LMGESGAGKTTLLNVLSQ-------------------------RVETGVV----------SGEILIDGHPLTDEDAfkrs 824
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGevllddgriiyeqdlivarlqqdppRNVEGTVydfvaegieeQAEYLKRYHDISHLVE---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 825 igfVQQQDLHLDLLS-VKESLEISCLLRGDgDRayLDTVSNLLKLPSDILVADLNPT-QRKLlSIGVELVTKPSLLLfLD 902
Cdd:PRK11147 110 ---TDPSEKNLNELAkLQEQLDHHNLWQLE-NR--INEVLAQLGLDPDAALSSLSGGwLRKA-ALGRALVSNPDVLL-LD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6324585 903 EPTSGLDAEAALTIVKFLKqlSLQGQAIFctihqpsksvISH 944
Cdd:PRK11147 182 EPTNHLDIETIEWLEGFLK--TFQGSIIF----------ISH 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
158-248 |
6.00e-05 |
|
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: 45.38 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 158 HVLKTIVGNDFFRGVSGGERKRISIIETFIANGSVYLWDNSTKGLDSATAldfLEILRKMAKATRSVNLVRISQASdKIV 237
Cdd:cd03247 85 YLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE---RQLLSLIFEVLKDKTLIWITHHL-TGI 160
|
90
....*....|.
gi 6324585 238 DKFDKILMLSD 248
Cdd:cd03247 161 EHMDKILFLEN 171
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
49-259 |
7.23e-05 |
|
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: 47.60 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGYPTStlfktlfhGKTSL-----SYSPPGSIKFKNNEFKSFSEKcphqiiynneqdvhFPFL- 122
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGS--------GKSSLlmmimGELEPSEGKIKHSGRISFSPQ--------------TSWIm 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 123 --TVEQTIDFALS------------CKF--DIPK-GERDQIrneLLREFGLShvlktivgndffrgVSGGERKRISIIET 185
Cdd:TIGR01271 500 pgTIKDNIIFGLSydeyrytsvikaCQLeeDIALfPEKDKT---VLGEGGIT--------------LSGGQRARISLARA 562
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 186 FIANGSVYLWDNSTKGLDSATALDFLE--ILRKMAKATRSVNLVRISQasdkiVDKFDKILMLSDSYQLFYGTVDE 259
Cdd:TIGR01271 563 VYKDADLYLLDSPFTHLDVVTEKEIFEscLCKLMSNKTRILVTSKLEH-----LKKADKILLLHEGVCYFYGTFSE 633
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
422-575 |
8.51e-05 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 46.61 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 422 SLTFFSILFFTFLSLAdMPIAFQRQPVVKKQSQLHFYTNWVETLSTTVFDYcfkLCLVIVFSIILYFLAHLQYKAARFFI 501
Cdd:pfam12698 165 GLILMIIILIGAAIIA-VSIVEEKESRIKERLLVSGVSPLQYWLGKILGDF---LVGLLQLLIILLLLFGIGIPFGNLGL 240
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324585 502 FLLFLSFYNFCMVSLFALTTLVAPTISVANLFAGILLLAIAMYASYVIYLKNMHPWFVWIAYLNPAMYAMEAIL 575
Cdd:pfam12698 241 LLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLL 314
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
49-248 |
9.27e-05 |
|
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: 44.94 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLfhgkTSLSYSPPGSIKFKNnefKSFSEKCPHQIIYNNEQDV--HFPFL 122
Cdd:cd03226 16 LDDLSLDLYAGEIIALTG-KNgagkTTLAKIL----AGLIKESSGSILLNG---KPIKAKERRKSIGYVMQDVdyQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 123 TVEQTIDFALSckfdiPKGERDQIRNELLREFGLsHVLKtivgNDFFRGVSGGERKRISIIETFIANGSVYLWDNSTKGL 202
Cdd:cd03226 88 SVREELLLGLK-----ELDAGNEQAETVLKDLDL-YALK----ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6324585 203 DSATALDFLEILRKMAKATRSVnlVRISQASDKIVDKFDKILMLSD 248
Cdd:cd03226 158 DYKNMERVGELIRELAAQGKAV--IVITHDYEFLAKVCDRVLLLAN 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
49-216 |
1.19e-04 |
|
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: 45.26 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGYP---TSTLFKTLfhgkTSLSYSPPGSIKFKNNEFKSFSEKCPHQIiynnEQDV-----HFP 120
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSgagKSTLIRCI----NGLERPTSGSVLVDGTDLTLLSGKELRKA----RRRIgmifqHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 121 FL---TVEQTIDFALSCKFdIPKGERDQIRNELLREFGLSHVLKTIVGNdffrgVSGGERKRISIIETFIANGSVYLWDN 197
Cdd:cd03258 93 LLssrTVFENVALPLEIAG-VPKAEIEERVLELLELVGLEDKADAYPAQ-----LSGGQKQRVGIARALANNPKVLLCDE 166
|
170
....*....|....*....
gi 6324585 198 STKGLDSATALDFLEILRK 216
Cdd:cd03258 167 ATSALDPETTQSILALLRD 185
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
33-256 |
1.80e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 45.11 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 33 KKSYDAEDSMPNPANQLNDITFQAEAGEMVLVLGYpTSTLFKTLFHGKTSLSYSPPGSIKF---------KNNEFKSFSE 103
Cdd:PRK13643 6 KVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGH-TGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstsKQKEIKPVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 104 KCphQIIYNNEQDVHFpfltvEQTI--DFALSCK-FDIPKGERDQIRNELLREFGLShvlKTIVGNDFFRgVSGGERKRI 180
Cdd:PRK13643 85 KV--GVVFQFPESQLF-----EETVlkDVAFGPQnFGIPKEKAEKIAAEKLEMVGLA---DEFWEKSPFE-LSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 181 SIIETFIANGSVYLWDNSTKGLDSATALDFLEILRKMAKATRSVNLVriSQASDKIVDKFDKILMLSDSYQLFYGT 256
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLV--THLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
740-806 |
4.21e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 42.53 E-value: 4.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324585 740 ITETVETQKHIISWKNINYTV---------GTKKLINnasgFISSGLTALMGESGAGKTTLLNVL--SQRVETGVVSG 806
Cdd:pfam03193 66 LDEEEELEELLKIYRAIGYPVlfvsaktgeGIEALKE----LLKGKTTVLAGQSGVGKSTLLNALlpELDLRTGEISE 139
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
511-574 |
4.68e-04 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 42.88 E-value: 4.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324585 511 FCMVSLFALTTLVAPTISVANLFAGILLLaIAMYASYVIY-LKNMHPWFVWIAYLNPAMYAMEAI 574
Cdd:COG0842 96 LAFSGLGLLISTLARSQEQASAISNLVIL-PLTFLSGAFFpIESLPGWLQAIAYLNPLTYFVEAL 159
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
761-927 |
4.76e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 43.52 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 761 GTKKLINNASGFISSGLT-ALMGESGAGKTTLlnvlsQRVETGV---VSGEILIDGHPLT-----DEDAFKRSIGFVQQQ 831
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETvALLGRSGCGKSTL-----ARLLVGLespSQGNVSWRGEPLAklnraQRKAFRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 832 DL------------------HLDLLSVKESLE-ISCLLRGDGDRAyldtvSNLLKLPsdilvADLNPTQRKLLSIGVELV 892
Cdd:PRK10419 98 SIsavnprktvreiireplrHLLSLDKAERLArASEMLRAVDLDD-----SVLDKRP-----PQLSGGQLQRVCLARALA 167
|
170 180 190
....*....|....*....|....*....|....*
gi 6324585 893 TKPSLLLfLDEPTSGLDAEAALTIVKFLKQLSLQG 927
Cdd:PRK10419 168 VEPKLLI-LDEAVSNLDLVLQAGVIRLLKKLQQQF 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
776-930 |
5.44e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 776 GLTALMGesgAGKTTLLNVLsqrveTGVV---SGEILIDGHPL---TDEDAFKRSIGFVQQQDLHLDL---LSVKESLEI 846
Cdd:PRK10762 282 GVSGLMG---AGRTELMKVL-----YGALprtSGYVTLDGHEVvtrSPQDGLANGIVYISEDRKRDGLvlgMSVKENMSL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 847 SCL---------LRGDGDRAyldTVSNLLKL-----PS-DILVADLNPTQRKLLSIGVELVTKPSLLLfLDEPTSGLDAE 911
Cdd:PRK10762 354 TALryfsraggsLKHADEQQ---AVSDFIRLfniktPSmEQAIGLLSGGNQQKVAIARGLMTRPKVLI-LDEPTRGVDVG 429
|
170
....*....|....*....
gi 6324585 912 AALTIVKFLKQLSLQGQAI 930
Cdd:PRK10762 430 AKKEIYQLINQFKAEGLSI 448
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
764-930 |
6.57e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 764 KLINNASGFISSG-LTALMGESGAGKTTLLNVLsqrveTGVVS---GEILIDGHPLT---DEDAFKRSIGFVQQQdlhLD 836
Cdd:PRK10762 18 KALSGAALNVYPGrVMALVGENGAGKSTMMKVL-----TGIYTrdaGSILYLGKEVTfngPKSSQEAGIGIIHQE---LN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 837 L---LSVKESL----EI-SCLLRGDGDRAYLDTVSNLLKL----PSDILVADLNPTQRKLLSIGVELVTKpSLLLFLDEP 904
Cdd:PRK10762 90 LipqLTIAENIflgrEFvNRFGRIDWKKMYAEADKLLARLnlrfSSDKLVGELSIGEQQMVEIAKVLSFE-SKVIIMDEP 168
|
170 180
....*....|....*....|....*..
gi 6324585 905 TSGL-DAEAAlTIVKFLKQLSLQGQAI 930
Cdd:PRK10762 169 TDALtDTETE-SLFRVIRELKSQGRGI 194
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
765-820 |
6.65e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 43.28 E-value: 6.65e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324585 765 LINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGV------VSGEILIDGHPLTDEDA 820
Cdd:PRK13547 16 ILRDLSLRIEPGrVTALLGRNGAGKSTLLKALAGDLTGGGaprgarVTGDVTLNGEPLAAIDA 78
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
754-911 |
6.70e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETgvVSGEIlidgHPLTdedafKRSIGFVQQQD 832
Cdd:PRK11147 323 ENVNYQIDGKQLVKDFSAQVQRGdKIALIGPNGCGKTTLLKLMLGQLQA--DSGRI----HCGT-----KLEVAYFDQHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 833 LHLDL-LSVKESLeiscllrGDG---------DRAYLDTVSNLLKLPSDILvadlnpTQRKLLSIG-------VELVTKP 895
Cdd:PRK11147 392 AELDPeKTVMDNL-------AEGkqevmvngrPRHVLGYLQDFLFHPKRAM------TPVKALSGGernrlllARLFLKP 458
|
170
....*....|....*.
gi 6324585 896 SLLLFLDEPTSGLDAE 911
Cdd:PRK11147 459 SNLLILDEPTNDLDVE 474
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
745-812 |
7.14e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.22 E-value: 7.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324585 745 ETQKHIISWKNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLSQRVETGvvSGEILIDG 812
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGkITAIMGPSGIGKTTLLRLIGGQIAPD--HGEILFDG 68
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
751-960 |
9.01e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.15 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 751 ISWKNINYTVGTK-----KLINNASGFISSG-LTALMGESGAGKTTL---LNVL------------------SQRVETGV 803
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGeFIAIIGQTGSGKTTFiehLNALllpdtgtiewifkdeknkKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 804 VSGEILID---GHPLTDEDAFKRSIGFVQQ--------QDLHLDLL--------SVKESLEIScllrgdgdRAYLDTVSn 864
Cdd:PRK13651 83 VLEKLVIQktrFKKIKKIKEIRRRVGVVFQfaeyqlfeQTIEKDIIfgpvsmgvSKEEAKKRA--------AKYIELVG- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 865 llkLPSDILVA---DLNPTQRKLLSIGVELVTKPSLLlFLDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQpsksv 941
Cdd:PRK13651 154 ---LDESYLQRspfELSGGQKRRVALAGILAMEPDFL-VFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD----- 224
|
250
....*....|....*....
gi 6324585 942 ishFDNIflLKRGGECVFF 960
Cdd:PRK13651 225 ---LDNV--LEWTKRTIFF 238
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
49-219 |
9.29e-04 |
|
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: 41.79 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLfhgkTSLSYSPPGSIKFKNNEFKSFSEKCPHQiiynnEQDVH------ 118
Cdd:cd03229 16 LNDVSLNIEAGEIVALLG-PSgsgkSTLLRCI----AGLEEPDSGSILIDGEDLTDLEDELPPL-----RRRIGmvfqdf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 119 --FPFLTVEQTIDFALSckfdipkgerdqirnellrefglshvlktivgndffrgvsGGERKRISIIETFIANGSVYLWD 196
Cdd:cd03229 86 alFPHLTVLENIALGLS----------------------------------------GGQQQRVALARALAMDPDVLLLD 125
|
170 180
....*....|....*....|...
gi 6324585 197 NSTKGLDSATALDFLEILRKMAK 219
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQA 148
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
115-224 |
9.68e-04 |
|
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: 42.18 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 115 QDVHF-PFLTVEQTIDFALSCKfDIPKGERDQIRNELLREFGLSHVLKTIVGndffrGVSGGERKRISIIETFIANGSVY 193
Cdd:cd03264 79 QEFGVyPNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGDPSIL 152
|
90 100 110
....*....|....*....|....*....|.
gi 6324585 194 LWDNSTKGLDSATALDFLEILRKMAkATRSV 224
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELG-EDRIV 182
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
162-248 |
1.10e-03 |
|
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: 43.27 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 162 TIVGNdffRGV--SGGERKRISIIETFIANGSVYLWDNSTKGLDSATALDFLEILRKMAKATRSvnLV---RISqasdKI 236
Cdd:COG5265 486 TRVGE---RGLklSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTT--LViahRLS----TI 556
|
90
....*....|..
gi 6324585 237 VDKfDKILMLSD 248
Cdd:COG5265 557 VDA-DEILVLEA 567
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
49-255 |
1.70e-03 |
|
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: 41.50 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLfhgkTSLSYSPPGSIKFKNnefKSFSEKCPHQIIYNNEQDVHFPFLTV 124
Cdd:cd03269 16 LDDISFSVEKGEIFGLLG-PNgagkTTTIRMI----LGIILPDSGEVLFDG---KPLDIAARNRIGYLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 125 -EQTIDFAlSCKfDIPKGE-RDQIRnELLREFGLSHVLKTIVgndffRGVSGGERKRISIIETFIANGSVYLWDNSTKGL 202
Cdd:cd03269 88 iDQLVYLA-QLK-GLKKEEaRRRID-EWLERLELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6324585 203 DSATALDFLEILRKMAKATRSVNLVriSQASDKIVDKFDKILMLSDSYQLFYG 255
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILS--THQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
49-247 |
1.74e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 41.62 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTLfhgkTSLSYSPPGSIKFKNNEFKSFS-EKCPHQIIYNNEQDVHFPfLT 123
Cdd:PRK10247 23 LNNISFSLRAGEFKLITG-PSgcgkSTLLKIV----ASLISPTSGTLLFEGEDISTLKpEIYRQQVSYCAQTPTLFG-DT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 124 VEQTIDFALSCKFDIPkgERDQIRNELLReFGL-SHVL-KTIvgNDffrgVSGGERKRISIIETFIANGSVYLWDNSTKG 201
Cdd:PRK10247 97 VYDNLIFPWQIRNQQP--DPAIFLDDLER-FALpDTILtKNI--AE----LSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6324585 202 LDSATALDFLEILRKMAKaTRSVNLVRISQASDKIvDKFDKILMLS 247
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVR-EQNIAVLWVTHDKDEI-NHADKVITLQ 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
881-954 |
2.65e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 41.76 E-value: 2.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324585 881 QRKLLSIGVELVTKPSLLLFlDEPTSGLDAEAALTIVKFLKQLSLQGQAIFCTIHQPSKsVISHFDNIFLLKRG 954
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIF-DEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEH-VLEVADEVIVMDKG 252
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
772-805 |
3.54e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.46 E-value: 3.54e-03
10 20 30
....*....|....*....|....*....|....*.
gi 6324585 772 FISSGLTALMGESGAGKTTLLNVL--SQRVETGVVS 805
Cdd:cd01854 82 LLKGKTSVLVGQSGVGKSTLLNALlpELVLATGEIS 117
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
43-259 |
3.75e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 40.99 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 43 PNPANQLNDITFQAEAGEMVLVLG---YPTSTLFKTL-----------FHGKTSLSYSPPGSIKFKNNEFKSFSEKcPHQ 108
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGgngAGKSTLFQNLngilkpssgriLFDGKPIDYSRKGLMKLRESVGMVFQDP-DNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 109 I----IYnneQDVHFPFLTVEqtidfalsckfdIPKGE-RDQIRNELLREfGLSHvLKtivgNDFFRGVSGGERKRISII 183
Cdd:PRK13636 95 LfsasVY---QDVSFGAVNLK------------LPEDEvRKRVDNALKRT-GIEH-LK----DKPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 184 ETFIANGSVYLWDNSTKGLDSATALDFLEILRKMAKATrSVNLVRISQASDKIVDKFDKILMLSDSYQLFYGTVDE 259
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKEL-GLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKE 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
149-275 |
4.00e-03 |
|
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: 41.33 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 149 ELLREFGLSHVLKTIVgndffRGVSGGERKRISIIETFIANGSVYLWDNSTKGLDSATALDFLEILRKMAKAtRSVNLVR 228
Cdd:TIGR03269 151 DLIEMVQLSHRITHIA-----RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKA-SGISMVL 224
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 6324585 229 ISQASDKIVDKFDKILMLSDSYQLFYGTVDECLTYFRDTLG-IEKDPN 275
Cdd:TIGR03269 225 TSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAVFMEGVSeVEKECE 272
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
754-955 |
4.85e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 41.24 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSG-LTALMGESGAGKTTLLNVLsQRvETGVVSGEILIDGHPLTD--EDAFKRSIGFVQQ 830
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGqMLGICGPTGSGKSTLLSLI-QR-HFDVSEGDIRFHDIPLTKlqLDSWRSRLAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 831 QDLhldLLSVKESLEIScLLRGDGDRAYLDTVSNLLKLPSDIL---------VAD----LNPTQRKLLSIGVELVTKPSL 897
Cdd:PRK10789 397 TPF---LFSDTVANNIA-LGRPDATQQEIEHVARLASVHDDILrlpqgydteVGErgvmLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6324585 898 LLfLDEPTSGLDAEAALTIVKFLKQLSlQGQAIFCTIHQpsKSVISHFDNIFLLKRGG 955
Cdd:PRK10789 473 LI-LDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHR--LSALTEASEILVMQHGH 526
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
754-793 |
4.91e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.32 E-value: 4.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6324585 754 KNINYTVGTKKLINNASGFISSGLTALMGESGAGKTTLLN 793
Cdd:PRK10246 9 KNLNSLKGEWKIDFTAEPFASNGLFAITGPTGAGKTTLLD 48
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
120-265 |
4.95e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.17 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 120 PFLTVEQTIDFALSCKfDIPKGERDQIRNELLREFGLSHVlktivGNDFFRGVSGGERKRISIIETFIANGSVYLWDNST 199
Cdd:PRK10070 119 PHMTVLDNTAFGMELA-GINAEERREKALDALRQVGLENY-----AHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324585 200 KGLDSATALDFL-EILRKMAKATRSVnlVRISQASDKIVDKFDKILMLSDSYQLFYGTVDECL---------TYFR 265
Cdd:PRK10070 193 SALDPLIRTEMQdELVKLQAKHQRTI--VFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILnnpandyvrTFFR 266
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
49-262 |
6.19e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 40.17 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 49 LNDITFQAEAGEMVLVLGyPT----STLFKTlFHG---KTSLSYSPPGSIKFKNN--EFKSFSekcphQIIYNNEQDVHF 119
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIG-PNgagkSTLFRH-FNGilkPTSGSVLIRGEPITKENirEVRKFV-----GLVFQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 120 PfLTVEQTIDFAlSCKFDIPKGERDQIRNELLREFGLSHVLKTIVGNdffrgVSGGERKRISIIETFIANGSVYLWDNST 199
Cdd:PRK13652 93 S-PTVEQDIAFG-PINLGLDEETVAHRVSSALHMLGLEELRDRVPHH-----LSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324585 200 KGLDSATALDFLEILRKMAKaTRSVNLVRISQASDKIVDKFDKILMLSDSYQLFYGTVDECLT 262
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPE-TYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
779-866 |
8.53e-03 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 37.79 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324585 779 ALMGESGAGKTTLLNVLSQRVETGVVSGEILIDGHPLTDEDAFKRSiGFVQQQDLHLDLLsvkeSLEISCLLRGDGDRAY 858
Cdd:pfam13238 2 LITGTPGVGKTTLAKELSKRLGFGDNVRDLALENGLVLGDDPETRE-SKRLDEDKLDRLL----DLLEENAALEEGGNLI 76
|
....*...
gi 6324585 859 LDTVSNLL 866
Cdd:pfam13238 77 IDGHLAEL 84
|
|
| |
