|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-1610 |
0e+00 |
|
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: 1432.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 1 MAFWTQLMLLLWKNFMYRRRQPVQLLVELLWPLFLFFILVAVRHSHPPLEHHECHFPNKPLPSAGTVPWLQGLICNVNNT 80
Cdd:TIGR01257 1 MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 81 CFPQLTPGEEPGRLSNFNDSLVSRLLADARTVLGGA--SAH-----RTLAGLGKLIATLR------AAR----------- 136
Cdd:TIGR01257 81 CFQSPTPGESPGIVSNYNNSILARVYRDFQELLMDApeSQHlgqvwAELRTLSQFMDTLRthperiAGRgirirdilkde 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 137 -----------------------STAQPQPTKQSPLEPPMLDVA---ELLTSLL-----------RTESLGLALGQAQ-- 177
Cdd:TIGR01257 161 ealtlflmkniglsdsvvyllvnSQVRPEQFAYGVPDLELKDIAcseALLERFIifsqrrgaqtvRDALCSLSQGTLQwi 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 178 --------------EPLHSLLEAAE-------------DLA---QELLALRSLVEL----RALLQR--PRGTSGPLELLS 221
Cdd:TIGR01257 241 edtlyanvdffklfHVLPTLLDSRSqginlrswggilsDMSpriQEFIHRPSVQDLlwvtRPLLQNggPETFTQLMGILS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 222 EALCSV-RGPSSTVGpSLNWYEASDLMELVGQEPESALP----DSSLSPACSELIGALDSHPLSRLLWRRLKPLILGKLL 296
Cdd:TIGR01257 321 DLLCGYpEGGGSRVF-SFNWYEDNNYKAFLGIDSTRKDPiysyDKRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKIL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 297 FAPDTPFTRKLMAQVNRTFEELTLLRDVREVWEMLGPRIFTFMNDSSNVAMLQRLLQ---MQDEGRRQPRPGGRDhMEAL 373
Cdd:TIGR01257 400 FTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDKSTQMTMIRDTLQnptVKDFINRQLGEEGIT-AEAV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 374 RSFLDPGS--------GGYSWQDAHADVGHLVGTLGRVTECLSLDKLEAAPSEAALVSRALQLLAEHRFWAGVVFlgped 445
Cdd:TIGR01257 479 LNFLYNGPrekqaddmTNFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVF----- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 446 ssdPTEHPTPDLGPGHVRIKIRMDIDVVTRTNKIRDRFWDPGPAADPLTDLRYVWGGFVYLQDLVERAAVRVLSGANPRA 525
Cdd:TIGR01257 554 ---PDMYPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQMQAEPPV 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 526 GLYLQQMPYPCYVDDVFLRVLSRSLPLFLTLAWIYSVTLTVKAVVREKETRLRDTMRAMGLSRAVLWLGWFLSCLGPFLL 605
Cdd:TIGR01257 631 GIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSM 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 606 SAALLVLVLKLGDILPYSHPGVVFLFLAAFAVATVTQSFLLSAFFSRANLAAACGGLAYFSLYLPYVLCVAWRDRLPAGG 685
Cdd:TIGR01257 711 SIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADL 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 686 RVAASLLSPVAFGFGCESLALLEEQGEGAQWHNVGTRPT-ADVFSLAQVSGLLLLDAALYGLATWYLEAVCPGQYGIPEP 764
Cdd:TIGR01257 791 KTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLeGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLP 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 765 WNFPFRRSYWCG--------PRPPKSPAPCPTPL-DPK-------VLVEEAPPGLSPGVSVRSLEKRFPGSPQPALRGLS 828
Cdd:TIGR01257 871 WYFLLQESYWLGgegcstreERALEKTEPLTEEMeDPEhpegindSFFERELPGLVPGVCVKNLVKIFEPSGRPAVDRLN 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 829 LDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNVLFDMLTVDEHVWFYGRL 908
Cdd:TIGR01257 951 ITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQL 1030
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 909 KGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREG 988
Cdd:TIGR01257 1031 KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 989 RTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKARLPLTTNEK--------ADTDMEGSVDT 1060
Cdd:TIGR01257 1111 RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKMKNIQSQRGgcegtcscTSKGFSTRCPA 1190
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 1061 RQEKKNGSQGSRVGTPQLLALVQHWVPGARLVEELPHELVLVLPYTGAHDGSFATLFRELDTRLAELRLTGYGISDTSLE 1140
Cdd:TIGR01257 1191 RVDEITPEQVLDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLE 1270
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 1141 EIFLKVVEECAADTDMEDGSCGQ-------HLCTGiagldVTLRLKMPPQETALEN-GEPA----GSAPETDQGSGPDAv 1208
Cdd:TIGR01257 1271 EIFLKVTEDADSGSLFAGGAQQKrenanlrHPCSG-----PTEKAGQTPQASHTCSpGQPAahpeGQPPPEPEDPGVPL- 1344
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 1209 grVQGWALTRQQLQALLLKRFLLARRSRRGLFAQIVLPALFVGLALVFSLIVPPFGHYPALRLSPTMYGAQVSFFSEDAP 1288
Cdd:TIGR01257 1345 --NTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYGQQYTFFSMDEP 1422
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 1289 GDPGRARLLEALLQEAG----------LEEPPVQHSShRFSAPEVPAEVAKVLASGNWTPESPSPACQCSRPGARRLLPD 1358
Cdd:TIGR01257 1423 NSEHLEVLADVLLNKPGfgnrclkeewLPEYPCGNST-PWKTPSVSPNITHLFQKQKWTAAHPSPSCRCSTREKLTMLPE 1501
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 1359 CPAAAGGPPPPQAVTGSGEVVQNLTGRNLSDFLVKTYPRLVRQGLKTKKWVNEVRYGGFSLGGRDPGLP-SGQELGRSVE 1437
Cdd:TIGR01257 1502 CPEGAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPAIPiTGEALVGFLS 1581
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 1438 ELWALLSpLPGGALDR-VLKNLTAWAHSLDAQDSLKIWFNNKGWHSMVAFVNRASNAILRAHLPPGPARHAHSITTLNHP 1516
Cdd:TIGR01257 1582 DLGQMMN-VSGGPVTReASKEMPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRDPEEYGITVISQP 1660
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 1517 LNLTKEQLSEGALMASSVDVLVSICVVFAMSFVPASFTLVLIEERVTRAKHLQLMGGLSPTLYWLGNFLWDMCNYLVPAC 1596
Cdd:TIGR01257 1661 LNLTKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAG 1740
|
1770
....*....|....
gi 768000599 1597 IVVLIFLAFQQRAY 1610
Cdd:TIGR01257 1741 LVVGIFIGFQKKAY 1754
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
807-1026 |
1.14e-104 |
|
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: 332.93 E-value: 1.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 967 TAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLR 1026
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
807-1039 |
5.29e-80 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 263.46 E-value: 5.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768000599 967 TAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPL-FLRRHLGSgYYLTLVK 1039
Cdd:COG1131 159 TSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDeLKARLLED-VFLELTG 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
807-1016 |
4.03e-63 |
|
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: 212.64 E-value: 4.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMLTVDEHVwfygrlkglsaavvgpeqdrllqdvglvskqsvqtrHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03230 79 PEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768000599 967 TAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03230 123 TSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
822-1031 |
4.05e-57 |
|
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: 200.31 E-value: 4.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNVLFDMLTVDEH 901
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 902 VWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWEL 981
Cdd:TIGR01188 87 LEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768000599 982 LLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGS 1031
Cdd:TIGR01188 167 IRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGK 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
807-1022 |
4.48e-56 |
|
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: 194.13 E-value: 4.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 967 TAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:cd03265 159 TIGLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
809-1016 |
1.86e-55 |
|
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: 193.54 E-value: 1.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 809 VRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQ 888
Cdd:COG4555 4 VENLSKKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 889 YNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTA 968
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768000599 969 GVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:COG4555 162 GLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
807-1020 |
8.61e-49 |
|
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: 173.15 E-value: 8.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGhITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGL--VSKQSVQTrhLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLgdRAKKKIGS--LSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 965 EPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCG 1020
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
808-1015 |
2.28e-48 |
|
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: 171.88 E-value: 2.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 808 SVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVC 886
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQY-NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDE 965
Cdd:cd03225 81 FQNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768000599 966 PTAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
807-1022 |
9.14e-46 |
|
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: 165.20 E-value: 9.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPqPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIRPHLGV 885
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQY--NVLFdMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:COG1122 80 VFQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 964 DEPTAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
807-1016 |
4.97e-45 |
|
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: 162.00 E-value: 4.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRpHLGVC 886
Cdd:cd03268 1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR-RIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAvvgpEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768000599 967 TAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
807-1149 |
2.24e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 160.66 E-value: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFpGSpQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRssmAAIRPHLGVC 886
Cdd:COG4152 2 LELKGLTKRF-GD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 967 TAGVDPASRRGIWELLLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYltlvkarlplt 1045
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTL----------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 1046 tnekadtdmegsvdtrqekkngsqgsRVGTPQLLALVQHWvPGARLVEELPHELVLVLPytgaHDGSFATLFRELdtrLA 1125
Cdd:COG4152 226 --------------------------RLEADGDAGWLRAL-PGVTVVEEDGDGAELKLE----DGADAQELLRAL---LA 271
|
330 340
....*....|....*....|....
gi 768000599 1126 ELRLTGYGISDTSLEEIFLKVVEE 1149
Cdd:COG4152 272 RGPVREFEEVRPSLNEIFIEVVGE 295
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
807-1016 |
2.33e-43 |
|
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: 157.53 E-value: 2.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRF--PGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLG 884
Cdd:cd03266 2 ITADALTKRFrdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 885 VCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 768000599 965 EPTAGVDPASRRGIWELLLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
805-1002 |
4.16e-41 |
|
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: 150.71 E-value: 4.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 805 PGVSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLG 884
Cdd:COG4133 1 MMLEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 885 VCPQYNVLFDMLTVDEHVWFYGRLKGLSAAvvGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 768000599 965 EPTAGVDPASRRGIWELLLKYRE-GRTLILSTHHLDEAE 1002
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLArGGAVLLTTHQPLELA 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
812-1156 |
1.59e-40 |
|
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: 165.19 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 812 LEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNV 891
Cdd:TIGR01257 1943 LTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDA 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 892 LFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVD 971
Cdd:TIGR01257 2023 IDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 972 PASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLvKARLPlttneka 1050
Cdd:TIGR01257 2103 PQARRMLWNTIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTM-KIKSP------- 2174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 1051 DTDMEGSVDTRQEKKNGSQGSRVGTPQLLALVQHWVPGArlveelphelvlvlpytgahdgSFATLFRELDTRLAELRLT 1130
Cdd:TIGR01257 2175 KDDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSS----------------------SLARIFQLLISHKDSLLIE 2232
|
330 340
....*....|....*....|....*.
gi 768000599 1131 GYGISDTSLEEIFLKVVEECAADTDM 1156
Cdd:TIGR01257 2233 EYSVTQTTLDQVFVNFAKQQTETYDL 2258
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
807-1015 |
1.82e-40 |
|
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: 148.97 E-value: 1.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFpGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRssmAAIRPHLGVC 886
Cdd:cd03269 1 LEVENVTKRF-GRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 768000599 967 TAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
807-1022 |
4.41e-40 |
|
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: 148.80 E-value: 4.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIRPH 882
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 883 LGVCPQYNVLFDMLTVDEHVWFYGRLKG-LSAAVVGpEQDRL-LQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQV 960
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIR-EIVLEkLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768000599 961 VILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
824-968 |
1.32e-39 |
|
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: 144.33 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMLTVDEHV 902
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 903 WFYGRLKGLSAAVVGPEQDRLLQDVGLV----SKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTA 968
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
801-1022 |
2.87e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 149.19 E-value: 2.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 801 PGLSPGVSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIR 880
Cdd:PRK13537 2 PMSVAPIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 881 PHLGVCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQV 960
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 961 VILDEPTAGVDPASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
805-1014 |
2.34e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 144.85 E-value: 2.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 805 PGVSVRSLEKRFP--GSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRssmaAIRPH 882
Cdd:COG1116 6 PALELRGVSKRFPtgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----GPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 883 LGVCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVI 962
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 768000599 963 LDEPTAGVDPASRRGIWELLLKY--REGRTLILSTHHLDEAELLGDRVAVVAGG 1014
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
805-1022 |
7.99e-38 |
|
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: 142.43 E-value: 7.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 805 PGVSVRSLEKRFpGSpQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIR 880
Cdd:COG1127 4 PMIEVRNLTKSF-GD-RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 881 PHLGVCPQYNVLFDMLTVDEHVWFYGR-LKGLSAAVVgpeQDR---LLQDVGLVskqsvQTRH-----LSGGMQRKLSVA 951
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEI---RELvleKLELVGLP-----GAADkmpseLSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 952 IAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
808-1015 |
1.54e-37 |
|
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: 138.53 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 808 SVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIRPHLGVC 886
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQynvlfdmltvdehvwfygrlkglsaavvgpeqdrllqdvglvskqsvqtrhLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd00267 79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 768000599 967 TAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:cd00267 108 TSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
780-1022 |
2.85e-37 |
|
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: 148.51 E-value: 2.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 780 PKSPAPCPTPLDPKVLVEEAPPGLSPGVSVRSLEKRFPGSPQ---PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSG 856
Cdd:COG1123 234 PQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 857 LFPPSGGSAFILGHDV----RSSMAAIRPHLGVCPQ--YNVLFDMLTVDEHVWFygrlkGLSAAVVGPEQDR------LL 924
Cdd:COG1123 314 LLRPTSGSILFDGKDLtklsRRSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAE-----PLRLHGLLSRAERrervaeLL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 925 QDVGLvsKQSVQTRH---LSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLD 999
Cdd:COG1123 389 ERVGL--PPDLADRYpheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLA 466
|
250 260
....*....|....*....|...
gi 768000599 1000 EAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG1123 467 VVRYIADRVAVMYDGRIVEDGPT 489
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
807-1015 |
5.33e-37 |
|
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: 137.51 E-value: 5.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGV 885
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQYNVLFDMlTVDEHVwfygrlkglsaavvgpeqdrllqdvglvskqsvqtrhLSGGMQRKLSVAIAFVGGSQVVILDE 965
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 768000599 966 PTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAElLGDRVAVVAGGR 1015
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
807-1013 |
5.51e-36 |
|
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: 136.45 E-value: 5.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFP--GSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGhdvrSSMAAIRPHLG 884
Cdd:cd03293 1 LEVRNVSKTYGggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 885 VCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768000599 965 EPTAGVDPASRRGIWELLLK--YREGRTLILSTHHLDEAELLGDRVAVVAG 1013
Cdd:cd03293 157 EPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
808-1022 |
6.27e-36 |
|
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: 136.80 E-value: 6.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 808 SVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCP 887
Cdd:cd03219 2 EVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 888 --QYNVLFDMLTVDEHV------------WFYGRLKGLSAAVvgpEQ-DRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAI 952
Cdd:cd03219 80 tfQIPRLFPELTVLENVmvaaqartgsglLLARARREEREAR---ERaEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000599 953 AFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
804-1016 |
7.75e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 136.33 E-value: 7.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 804 SPGVSVRSLEKRFP--GSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMA 877
Cdd:COG1136 2 SPLLELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 878 AIRP-HLGVCPQ-YNvLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGG-MQRklsVAIA- 953
Cdd:COG1136 82 RLRRrHIGFVFQfFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGqQQR---VAIAr 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 954 -FVGGSQVVILDEPTAGVDPASRRGIWELLLKY--REGRTLILSTHHLDEAElLGDRVAVVAGGRL 1016
Cdd:COG1136 158 aLVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
796-1022 |
8.63e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 139.97 E-value: 8.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 796 VEEAPPGLSPGVSVR--SLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVR 873
Cdd:PRK13536 29 AKASIPGSMSTVAIDlaGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 874 SSMAAIRPHLGVCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIA 953
Cdd:PRK13536 107 ARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 954 FVGGSQVVILDEPTAGVDPASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP 256
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
804-1022 |
5.13e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.45 E-value: 5.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 804 SPGVSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSmaaiRPHL 883
Cdd:COG1121 4 MPAIELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 884 GVCPQY-NVLFDM-LTVDE--------HVWFYGRLKGLSAAVVgpeqDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIA 953
Cdd:COG1121 78 GYVPQRaEVDWDFpITVRDvvlmgrygRRGLFRRPSRADREAV----DEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 954 FVGGSQVVILDEPTAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAgGRLCCCGSP 1022
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPP 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
797-1034 |
1.17e-34 |
|
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: 141.44 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 797 EEAPPGLSPGVSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-S 875
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 876 MAAIRPHLGVCPQYNVLFDMlTV------------DEHVWFYGRLKGLSAAVVGPEQ--DRLLQDVGlvskqsvqtRHLS 941
Cdd:COG4987 404 EDDLRRRIAVVPQRPHLFDT-TLrenlrlarpdatDEELWAALERVGLGDWLAALPDglDTWLGEGG---------RRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 942 GGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAElLGDRVAVVAGGRLCCCGS 1021
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGT 552
|
250
....*....|...
gi 768000599 1022 PLFLRRHlgSGYY 1034
Cdd:COG4987 553 HEELLAQ--NGRY 563
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
807-1016 |
1.59e-34 |
|
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: 132.23 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGS--PQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSS----MAAIR 880
Cdd:cd03255 1 IELKNLSKTYGGGgeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 881 -PHLG-VCPQYNVLfDMLTVDEHVWFYGRLKGlsaavVGPEQDR-----LLQDVGLVSKQSVQTRHLSGGMQRKLSVAIA 953
Cdd:cd03255 81 rRHIGfVFQSFNLL-PDLTALENVELPLLLAG-----VPKKERReraeeLLERVGLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768000599 954 FVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAElLGDRVAVVAGGRL 1016
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
804-1022 |
1.72e-34 |
|
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: 140.04 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 804 SPGVSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSG---GSAFILGHDVRSSMAAIR 880
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 881 -PHLGVCPQ-YNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGS 958
Cdd:COG1123 82 gRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 959 QVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPP 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
807-1016 |
8.33e-34 |
|
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: 129.95 E-value: 8.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVrSSMAAIRPHLGVC 886
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768000599 967 TAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03259 158 LSALDAKLREELREELKELQRelGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
821-1020 |
1.04e-33 |
|
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: 129.58 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 821 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSmaaiRPHLGVCPQ-YNVLFDM-LTV 898
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQrRSIDRDFpISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 899 DE--------HVWFYGRLKGLSAAVVgpeqDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGV 970
Cdd:cd03235 88 RDvvlmglygHKGLFRRLSKADKAKV----DEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768000599 971 DPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAgGRLCCCG 1020
Cdd:cd03235 164 DPKTQEDIYELLRELRrEGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
808-1022 |
4.16e-33 |
|
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: 129.39 E-value: 4.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 808 SVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC- 886
Cdd:COG0411 6 EVRGLTKRFGGLV--AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIAr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 ----PQynvLFDMLTVDEHV----------WFYGRLKGLSAAVVGPEQ-----DRLLQDVGLVSKQSVQTRHLSGGMQRK 947
Cdd:COG0411 84 tfqnPR---LFPELTVLENVlvaaharlgrGLLAALLRLPRARREEREareraEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599 948 LSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDerGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
807-1028 |
9.14e-33 |
|
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: 128.19 E-value: 9.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSpQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGV 885
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQ--TRHLSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADryPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599 964 DEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRH 1028
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
804-1022 |
1.03e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 128.29 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 804 SPGVSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVrSSMAAIRPHL 883
Cdd:COG3842 3 MPALELENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPEKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 884 GVCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGG-MQRklsVAIA--FVGGSQV 960
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqQQR---VALAraLAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768000599 961 VILDEPTAGVDPASRRGIWELLLKY--REGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLqrELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTP 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
807-1016 |
1.15e-31 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 124.54 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFP--GSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIR 880
Cdd:cd03257 2 LEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 881 PHLGVCPQ--YNVLFDMLTVDEHV----WFYGRLKGLSAAvvgpEQDRLLQDVGLVSKQSVQTR---HLSGGMQRKLSVA 951
Cdd:cd03257 82 KEIQMVFQdpMSSLNPRMTIGEQIaeplRIHGKLSKKEAR----KEAVLLLLVGVGLPEEVLNRyphELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599 952 IAFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
809-1015 |
2.01e-31 |
|
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: 121.91 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 809 VRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPH---LGV 885
Cdd:cd03229 3 LKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQYNVLFDMLTVdehvwfygrlkglsaavvgpeqdrlLQDVGLVskqsvqtrhLSGGMQRKLSVAIAFVGGSQVVILDE 965
Cdd:cd03229 81 VFQDFALFPHLTV-------------------------LENIALG---------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768000599 966 PTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:cd03229 127 PTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
807-1022 |
2.02e-31 |
|
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: 124.39 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGV 885
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQYNVLFDMLTVDE--------HVWFYGRLKGLSAAVVgpeqDRLLQDVGLV--SKQSVQTrhLSGGMQRKLSVAIAFV 955
Cdd:COG1120 80 VPQEPPAPFGLTVRElvalgrypHLGLFGRPSAEDREAV----EEALERTGLEhlADRPVDE--LSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599 956 GGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
807-1016 |
4.01e-31 |
|
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: 120.61 E-value: 4.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV--RSSMAAIRphLG 884
Cdd:cd03216 1 LELRGITKRFGG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsfASPRDARR--AG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 885 vcpqynvlfdmltvdehvwfygrlkglsaavvgpeqdrllqdVGLVSkQsvqtrhLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:cd03216 77 ------------------------------------------IAMVY-Q------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 768000599 965 EPTAGVDPASRRGIWELL--LKyREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03216 108 EPTAALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
814-1016 |
1.12e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 121.31 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 814 KRFPGSpQPALRGLSLDFYQGHItAFL-GHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIRPHLGVCPQ 888
Cdd:COG2884 9 KRYPGG-REALSDVSLEIEKGEF-VFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkRREIPYLRRRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 889 -YNVLFDMlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPT 967
Cdd:COG2884 87 dFRLLPDR-TVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 768000599 968 AGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:COG2884 166 GNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
822-1015 |
1.77e-30 |
|
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: 120.62 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGV--CPQYNVLFDMLTVD 899
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIgyVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 900 EHVwfygrlkgLSAAVVGPEQD--RLLQDV-----GLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDP 972
Cdd:cd03224 94 ENL--------LLGAYARRRAKrkARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 768000599 973 ASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:cd03224 166 KIVEEIFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
816-1001 |
1.47e-29 |
|
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: 117.14 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 816 FPGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV---RSSMAAIRPHLGVCPQY--N 890
Cdd:TIGR01166 1 YPGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDpdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 891 VLFDMlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGV 970
Cdd:TIGR01166 80 QLFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|..
gi 768000599 971 DPASRRGIWELLLKYR-EGRTLILSTHHLDEA 1001
Cdd:TIGR01166 159 DPAGREQMLAILRRLRaEGMTVVISTHDVDLA 190
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
809-1015 |
1.75e-29 |
|
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: 118.44 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 809 VRSLEKRFPGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIRPHLG 884
Cdd:cd03256 3 VENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 885 -VCPQYNvLFDMLTVDEHVWFyGRLKGLSA--AVVG--PEQDR-----LLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAF 954
Cdd:cd03256 82 mIFQQFN-LIERLSVLENVLS-GRLGRRSTwrSLFGlfPKEEKqralaALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 955 VGGSQVVILDEPTAGVDPASRRGIWELLLKY--REGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
808-1020 |
2.35e-29 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 116.00 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 808 SVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVC 886
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQynvlfdmltvdehvwfygrlkglsaavvgpeqdrLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 967 TAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCG 1020
Cdd:cd03214 125 TSHLDIAHQIELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
807-1016 |
1.61e-28 |
|
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: 115.37 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQ--PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIR 880
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 881 PHLG-VCPQYNvLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQ 959
Cdd:cd03258 82 RRIGmIFQHFN-LLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599 960 VVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
796-1022 |
2.50e-28 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 116.20 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 796 VEEAPPGLSPGVSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV--- 872
Cdd:cd03294 14 PQKAFKLLAKGKSKEEILKKT--GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaam 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 873 -RSSMAAIRPH-LGVCPQYNVLFDMLTVDEHVWFygrlkGLSAAVVgPEQDRL------LQDVGLVSKQSVQTRHLSGGM 944
Cdd:cd03294 92 sRKELRELRRKkISMVFQSFALLPHRTVLENVAF-----GLEVQGV-PRAEREeraaeaLELVGLEGWEHKYPDELSGGM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 945 QRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKY--REGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:cd03294 166 QQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
808-1022 |
5.36e-28 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 114.29 E-value: 5.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 808 SVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGV-- 885
Cdd:TIGR04406 3 VAENLIKSYKK--RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQYNVLFDMLTVDEHVW-FYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 965 EPTAGVDPASRRGIWELLLKYREGRTLILSTHHlDEAELLG--DRVAVVAGGRLCCCGSP 1022
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDH-NVRETLDicDRAYIISDGKVLAEGTP 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
797-1022 |
1.04e-27 |
|
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: 120.25 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 797 EEAPPGLSPGVSVRSLEKRFPGSpQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-S 875
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 876 MAAIRPHLGVCPQYNVLFDMlTVDEHVwfygrlkGLSAAVVGPEQ-DRLLQDVGL---VSK--QSVQT------RHLSGG 943
Cdd:COG4988 406 PASWRRQIAWVPQNPYLFAG-TIRENL-------RLGRPDASDEElEAALEAAGLdefVAAlpDGLDTplgeggRGLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 944 -MQRkLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAElLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG4988 478 qAQR-LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILVLDDGRIVEQGTH 555
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
807-1022 |
1.16e-27 |
|
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: 113.10 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPhLGVC 886
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-VNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 967 TAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:cd03300 158 LGALDLKLRKDMQLELkrLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
823-1016 |
1.18e-27 |
|
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: 112.66 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFP-----PSGGSAFILGHDVRSS---MAAIRPHLGVCPQYNVLFD 894
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvdVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 895 MlTVDEHVWFYGRLKG-LSAAVVGPEQDRLLQDVGL---VsKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGV 970
Cdd:cd03260 95 G-SIYDNVAYGLRLHGiKLKEELDERVEEALRKAALwdeV-KDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 768000599 971 DPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03260 173 DPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
807-1016 |
1.38e-27 |
|
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: 110.87 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDmltvdehvwfygrlkglsaavvgpeqDRLLQDVGlvskqsvqtRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03247 81 NQRPYLFD--------------------------TTLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 768000599 967 TAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLgDRVAVVAGGRL 1016
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
800-1016 |
2.89e-27 |
|
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: 119.94 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 800 PPGLSPGVSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAA 878
Cdd:COG2274 467 LPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 879 IRPHLGVCPQYNVLF-----DMLTV------DEHVWFYGRLKGLSAAVVG-PEQ-DRLLQDVGlvskqsvqtRHLSGGMQ 945
Cdd:COG2274 547 LRRQIGVVLQDVFLFsgtirENITLgdpdatDEEIIEAARLAGLHDFIEAlPMGyDTVVGEGG---------SNLSGGQR 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000599 946 RKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLgDRVAVVAGGRL 1016
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA-DRIIVLDKGRI 687
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
833-1027 |
3.89e-27 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 120.23 E-value: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 833 QGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNVLFDMLTVDEHVWFYGRLKGLS 912
Cdd:NF033858 291 RGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLP 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 913 AAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRT 990
Cdd:NF033858 371 AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLieLSREDGVT 450
|
170 180 190
....*....|....*....|....*....|....*..
gi 768000599 991 LILSTHHLDEAELLgDRVAVVAGGRLCCCGSPLFLRR 1027
Cdd:NF033858 451 IFISTHFMNEAERC-DRISLMHAGRVLASDTPAALVA 486
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
807-1016 |
6.62e-27 |
|
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: 110.37 E-value: 6.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGV 885
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQYNVLF-----DMLTV------DEHVWFYGRLKGLSAAVVGPEQ--DRLLQDVGlvskqsvqtRHLSGGMQRKLSVAI 952
Cdd:cd03245 83 VPQDVTLFygtlrDNITLgapladDERILRAAELAGVTDFVNKHPNglDLQIGERG---------RGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768000599 953 AFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLgDRVAVVAGGRL 1016
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLV-DRIIVMDSGRI 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
804-1023 |
6.89e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 112.01 E-value: 6.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 804 SPGVSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIRPH 882
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIsKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 883 LGVCPQY-NVLFDMLTVDEHVWFygrlkGLSAAVVGPEQ-----DRLLQDVGLVSKQSVQTRHLSGGM-QRklsVAIAFV 955
Cdd:PRK13632 85 IGIIFQNpDNQFIGATVEDDIAF-----GLENKKVPPKKmkdiiDDLAKKVGMEDYLDKEPQNLSGGQkQR---VAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768000599 956 GG--SQVVILDEPTAGVDPASRRGIWELLLKYREGR--TLILSTHHLDEAeLLGDRVAVVAGGRLCCCGSPL 1023
Cdd:PRK13632 157 LAlnPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPK 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
796-1016 |
7.38e-27 |
|
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: 110.88 E-value: 7.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 796 VEEAPPGLspGVSVRSLEKRFPGSpQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSS 875
Cdd:cd03267 12 VYSKEPGL--IGSLKSLFKRKYRE-VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 876 MAAIRPHLG-VCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRL--LQDVGLVSKQSVqtRHLSGGMQRKLSVAI 952
Cdd:cd03267 89 RKKFLRRIGvVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELseLLDLEELLDTPV--RQLSLGQRMRAEIAA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 953 AFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGR--TLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
815-1016 |
7.70e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.91 E-value: 7.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 815 RFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLF 893
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 894 DMlTVDEHVWFYGRLKGLSAAvvGPEQDRLLQDVGL---VSKQSVQtrHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGV 970
Cdd:COG4619 87 GG-TVRDNLPFPFQLRERKFD--RERALELLERLGLppdILDKPVE--RLSGGERQRLALIRALLLQPDVLLLDEPTSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768000599 971 DPASRRGIWELLLKYR--EGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:COG4619 162 DPENTRRVEELLREYLaeEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
823-1016 |
9.07e-27 |
|
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: 108.67 E-value: 9.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV--RSSMAAIRphLGVCpqynvlfdmltvde 900
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIR--AGIA-------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 901 HVwfygrlkglsaavvgPEqDRLLQdvGLVSKQSVQ-----TRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASR 975
Cdd:cd03215 79 YV---------------PE-DRKRE--GLVLDLSVAenialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768000599 976 RGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03215 141 AEIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
807-1022 |
3.77e-26 |
|
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: 108.40 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 --PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:cd03218 79 ylPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599 965 EPTAGVDPASRRGIWELLLKYREGRTLILST-HHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
808-1029 |
3.99e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 109.57 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 808 SVRSLEKRFPGS--PQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSmAAIRphlGV 885
Cdd:COG4525 5 TVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP-GADR---GV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDE 965
Cdd:COG4525 81 VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 966 PTAGVDPASRRGIWELLLKY--REGRTLILSTHHLDEAELLGDRVAVVAG--GRLCCCGSPLFLRRHL 1029
Cdd:COG4525 161 PFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVERLELDFSRRFL 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
807-1022 |
1.00e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.63 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVR---SSMAAIRPHL 883
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 884 GVCPQY--NVLFdMLTVDEHVWFyGRLK-GLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQV 960
Cdd:PRK13639 81 GIVFQNpdDQLF-APTVEEDVAF-GPLNlGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 961 VILDEPTAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
807-1025 |
1.13e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.67 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIRPHLGV 885
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQ--YNVLFDMlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:PRK13647 84 VFQdpDDQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 964 DEPTAGVDPASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFL 1025
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
806-1022 |
1.18e-25 |
|
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: 107.43 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 806 GVSVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVrSSMAAIRPHLGV 885
Cdd:cd03296 2 SIEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQYNVLFDMLTVDEHVWFYGRLK----GLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVV 961
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 962 ILDEPTAGVDPASRRGI--WELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:cd03296 159 LLDEPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
807-1044 |
2.11e-25 |
|
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: 106.81 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSP--QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIRPHL 883
Cdd:COG1124 2 LEVRNLSVSYGQGGrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 884 GVCPQ--YNVLFDMLTVDEHVwfygrLKGLSAAVVGPEQDR---LLQDVGLvsKQSVQTR--H-LSGGMQRKLSVAIAFV 955
Cdd:COG1124 82 QMVFQdpYASLHPRHTVDRIL-----AEPLRIHGLPDREERiaeLLEQVGL--PPSFLDRypHqLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 956 GGSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGY 1033
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
250
....*....|.
gi 768000599 1034 YLTLVKARLPL 1044
Cdd:COG1124 235 TRELLAASLAF 245
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
824-1014 |
4.34e-25 |
|
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: 104.65 E-value: 4.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSafILGHDVRSSMAAIRPHLGVCPQ---YNVLFDmlTVDE 900
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGS--ILLNGKPIKAKERRKSIGYVMQdvdYQLFTD--SVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 901 HVWFygRLKGLSAAvvGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWE 980
Cdd:cd03226 92 ELLL--GLKELDAG--NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGE 167
|
170 180 190
....*....|....*....|....*....|....*
gi 768000599 981 LLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGG 1014
Cdd:cd03226 168 LIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
827-1016 |
1.03e-24 |
|
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: 103.73 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 827 LSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPhLGVCPQYNVLFDMLTVDEHVWFyg 906
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-VSMLFQENNLFAHLTVEQNVGL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 907 rlkGLSAAVVGPEQDR-----LLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWEL 981
Cdd:cd03298 94 ---GLSPGLKLTAEDRqaievALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 768000599 982 LLKYREGR--TLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03298 171 VLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
814-1016 |
1.29e-24 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 103.64 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 814 KRFPGSpQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIRPHLGVCPQY 889
Cdd:cd03292 8 KTYPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 890 NVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 969
Cdd:cd03292 87 FRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768000599 970 VDPASRRGIWELLLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
822-1015 |
1.45e-24 |
|
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: 103.91 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGV--CPQYNVLFDMLTVD 899
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIgyVPEGRRIFPSLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 900 EHvwfygrLK-GLSAAVVGPEQDRLLQDVG-----LVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPA 973
Cdd:COG0410 97 EN------LLlGAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 768000599 974 SRRGIWELL--LKyREGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:COG0410 171 IVEEIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
807-1016 |
1.64e-24 |
|
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: 103.38 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV---RSSMAAIRPHL 883
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 884 G-VCPQYNvLFDMLTVDEHVWFYGR-LKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVV 961
Cdd:cd03262 79 GmVFQQFN-LFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 962 ILDEPTAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
823-1032 |
2.28e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 111.37 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSM--AAIRPHLGVCPQ---YNvLFDMLT 897
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARhrRAVCPRIAYMPQglgKN-LYPTLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 898 VDEHVWFYGRLKGLSAAvvgpEQ----DRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPA 973
Cdd:NF033858 95 VFENLDFFGRLFGQDAA----ERrrriDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768000599 974 SRRGIWELLLKYREGR---TLILSTHHLDEAELLgDRVAVVAGGRLCCCGSPLFLRRHLGSG 1032
Cdd:NF033858 171 SRRQFWELIDRIRAERpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLARTGAD 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
805-1016 |
5.24e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.80 E-value: 5.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 805 PGVSVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV--RSSMAAIRPH 882
Cdd:COG1129 3 PLLEMRGISKSFGGVK--ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 883 LGVCPQYNVLFDMLTVDEHVWFyGRLKGLSAAVvgpeqDR---------LLQDVGLVSKQSVQTRHLSGGmQRKLsVAI- 952
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFL-GREPRRGGLI-----DWramrrrareLLARLGLDIDPDTPVGDLSVA-QQQL-VEIa 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599 953 -AFVGGSQVVILDEPTAGVDPASRRGIWELL--LKyREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:COG1129 153 rALSRDARVLILDEPTASLTEREVERLFRIIrrLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
806-1000 |
6.72e-24 |
|
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: 102.47 E-value: 6.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 806 GVSVRSLEKrfpgspqPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPP-SGGSAFILGHDV-RSSMAAIRPHL 883
Cdd:COG1119 8 NVTVRRGGK-------TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGERRgGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 884 GVCpqYNVLFDMLTVDEHVW------FYGRLkGLSAAVvGPEQ----DRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIA 953
Cdd:COG1119 81 GLV--SPALQLRFPRDETVLdvvlsgFFDSI-GLYREP-TDEQreraRELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768000599 954 FVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDE 1000
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVEE 205
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
797-1011 |
8.16e-24 |
|
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: 107.76 E-value: 8.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 797 EEAPPGLSPGVSVRSLEKRFPGSPqPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-S 875
Cdd:TIGR02857 312 APVTAAPASSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 876 MAAIRPHLGVCPQYNVLFDMlTVDEHVWFYgrLKGLSAAVVgpeqDRLLQDVGLVS-----KQSVQT------RHLSGGM 944
Cdd:TIGR02857 391 ADSWRDQIAWVPQHPFLFAG-TIAENIRLA--RPDASDAEI----REALERAGLDEfvaalPQGLDTpigeggAGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599 945 QRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLgDRVAVV 1011
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
805-1016 |
8.17e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.42 E-value: 8.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 805 PGVSVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV--RSSMAAIRPH 882
Cdd:COG3845 4 PALELRGITKRFGGVV--ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVriRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 883 LGVCPQYNVLFDMLTVDEHVW--------FYGRLKGLSAAVvgpeqDRLLQDVGL-------VSKQSVqtrhlsgGMQRK 947
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVlgleptkgGRLDRKAARARI-----RELSERYGLdvdpdakVEDLSV-------GEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768000599 948 lsVAI--AFVGGSQVVILDEPTAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:COG3845 150 --VEIlkALYRGARILILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
807-1043 |
4.40e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.08 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV---RSSMAAIRPHL 883
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 884 GVCPQY--NVLFDMlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVV 961
Cdd:PRK13636 85 GMVFQDpdNQLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 962 ILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP--LFLRRHLgsgyyLTL 1037
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPkeVFAEKEM-----LRK 238
|
....*.
gi 768000599 1038 VKARLP 1043
Cdd:PRK13636 239 VNLRLP 244
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
810-1020 |
4.47e-23 |
|
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: 99.65 E-value: 4.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 810 RSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPpSGGSAF--ILGHDVRSSMAAIRPHLGVCP 887
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE-GGGTTSgqILFNGQPRKPDQFQKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 888 QYNVLFDMLTVDEHVWFYGRLKG---LSAAVVGPE-QDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:cd03234 88 QDDILLPGLTVRETLTYTAILRLprkSSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 964 DEPTAGVDPASRRGIWELLLKY-REGRTLILSTHHlDEAEL--LGDRVAVVAGGRLCCCG 1020
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLaRRNRIVILTIHQ-PRSDLfrLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
818-1022 |
6.61e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.59 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 818 GSP--QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSS-----MAAIRPHLGVCPQY- 889
Cdd:PRK13649 15 GTPfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkdIKQIRKKVGLVFQFp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 890 -NVLFDMlTVDEHVWFYGRLKGLS---AAVVGPEQDRLlqdVG----LVSKQSVQtrhLSGGMQRKlsVAIAFVGGSQ-- 959
Cdd:PRK13649 95 eSQLFEE-TVLKDVAFGPQNFGVSqeeAEALAREKLAL---VGisesLFEKNPFE---LSGGQMRR--VAIAGILAMEpk 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768000599 960 VVILDEPTAGVDPASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
807-1016 |
7.49e-23 |
|
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: 98.01 E-value: 7.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQPA----LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPH 882
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 883 LGVCPQYNVLFDMLTVDEHVWFYGRLKGlsaavvgpeqdrllqdvglvskqsvqtrhLSGGMQRKLSVAIAFVGGSQVVI 962
Cdd:cd03213 84 IGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 963 LDEPTAGVDPASRRGIWELLLKYR-EGRTLILSTHHL-DEAELLGDRVAVVAGGRL 1016
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
823-1016 |
9.50e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 100.93 E-value: 9.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHD-VRSSMAAIRpHLGVcpqynV-------LFD 894
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpFKRRKEFAR-RIGV-----VfgqrsqlWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 895 mLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGmQR-KLSVAIAFVGGSQVVILDEPTAGVDPA 973
Cdd:COG4586 111 -LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLG-QRmRCELAAALLHRPKILFLDEPTIGLDVV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768000599 974 SRRGIWELLLKY--REGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:COG4586 189 SKEAIREFLKEYnrERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
807-1028 |
1.06e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 101.69 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVrSSMAAIRPHLGVC 886
Cdd:COG3839 4 LELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAvvgpEQDRLLQDV----GLVS------KQsvqtrhLSGG-MQRklsVAI--A 953
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKA----EIDRRVREAaellGLEDlldrkpKQ------LSGGqRQR---VALgrA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 954 FVGGSQVVILDEPTAGVDPASR---RGiwEL--LLKyREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRH 1028
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRvemRA--EIkrLHR-RLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDR 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
828-1015 |
1.41e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 98.29 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 828 SLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPhLGVCPQYNVLFDMLTVDEHVWFyG- 906
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP-VSMLFQENNLFPHLTVAQNIGL-Gl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 907 --RLKgLSAAvvgpEQDRL---LQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWEL 981
Cdd:COG3840 97 rpGLK-LTAE----QRAQVeqaLERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 768000599 982 L--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:COG3840 172 VdeLCRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
817-1022 |
1.85e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 99.35 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 817 PGSP--QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV---RSSMAAIRPHLGVCPQY-- 889
Cdd:PRK13637 14 EGTPfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKKVGLVFQYpe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 890 NVLFDMlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLvSKQSVQTR---HLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:PRK13637 94 YQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGL-DYEDYKDKspfELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 967 TAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13637 172 TAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
779-998 |
3.34e-22 |
|
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: 102.82 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 779 PPKSPAPCPTPLDPKVLVEEAPpglspGVSVRSLEKRFPGSPqPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLF 858
Cdd:TIGR02868 312 DAAGPVAEGSAPAAGAVGLGKP-----TLELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 859 PPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMlTVDEHVWFyGR--------LKGLSAAVVGPEQDRLLQdvGL 929
Cdd:TIGR02868 386 DPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVRENLRL-ARpdatdeelWAALERVGLADWLRALPD--GL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599 930 VSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHL 998
Cdd:TIGR02868 462 DTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
807-1016 |
3.56e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 102.87 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGV 885
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQYNVLFDMlTVDEHVwFYGRLKGLSAA-VVGPEQDRLLQDV------GLVSKQSVQTRHLSGGMQRKLSVAIAFVGGS 958
Cdd:TIGR02203 411 VSQDVVLFND-TIANNI-AYGRTEQADRAeIERALAAAYAQDFvdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 959 QVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAElLGDRVAVVAGGRL 1016
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRI 545
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
807-1022 |
3.88e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.33 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPP---SGGSAFILGHDVRS-SMAAIRPH 882
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAkTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 883 LGVCPQY-NVLFDMLTVDEHVWFygrlkGL-SAAVVGPEQDRL----LQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVG 956
Cdd:PRK13640 86 VGIVFQNpDNQFVGATVGDDVAF-----GLeNRAVPRPEMIKIvrdvLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 957 GSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAElLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIrkLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSP 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
807-1016 |
5.14e-22 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 96.17 E-value: 5.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRpHLGVC 886
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR-DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGP---EQDRLLQDVGLVSKqsvQTRHLSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDErvrEVAELLQIEHLLDR---KPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768000599 964 DEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
821-1016 |
5.20e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 102.55 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 821 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMlTV- 898
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDTFLFSG-TIr 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 899 -----------DEHVW----------FYGRL-KGLsAAVVGPEqdrllqdvGlvskqsvqtRHLSGGmQR-KLSVAIAFV 955
Cdd:COG1132 432 enirygrpdatDEEVEeaakaaqaheFIEALpDGY-DTVVGER--------G---------VNLSGG-QRqRIAIARALL 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768000599 956 GGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLD---EAellgDRVAVVAGGRL 1016
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLStirNA----DRILVLDDGRI 552
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
808-1016 |
7.65e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 95.68 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 808 SVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGhdvrssmaAIRPHLGVcp 887
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------RVSSLLGL-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 888 qyNVLFD-MLTVDEHVWFYGRLKGLSAAvvgpEQDRLLQDV----GLVSKQSVQTRHLSGGMQRKL--SVAIAFvgGSQV 960
Cdd:cd03220 92 --GGGFNpELTGRENIYLNGRLLGLSRK----EIDEKIDEIiefsELGDFIDLPVKTYSSGMKARLafAIATAL--EPDI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599 961 VILDEPTAGVDPASRRGIWELLLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLRELLKqGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
824-1022 |
1.16e-21 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 95.87 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVrSSMAAIRPHLGVCPQYNVLFDMLTVDEHVW 903
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 904 FYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLL 983
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768000599 984 KYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:cd03299 174 KIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKP 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
808-1022 |
1.28e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.99 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 808 SVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVC 886
Cdd:PRK13548 4 EARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVL-FDmLTVDEHVWFyGRLK-GLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGG-MQRklsVAIAFV-------- 955
Cdd:PRK13548 82 PQHSSLsFP-FTVEEVVAM-GRAPhGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGeQQR---VQLARVlaqlwepd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599 956 GGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLArqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
808-1035 |
1.36e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.48 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 808 SVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAiRPHLGV- 885
Cdd:COG1137 5 EAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDItHLPMHK-RARLGIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 -CPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:COG1137 82 yLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 965 EPTAGVDPASRRGIWELLLKYREgRTL-ILST-HHLDEAELLGDRVAVVAGGRLCCCGSPLFL------RRH-LGSGYYL 1035
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHLKE-RGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEIlnnplvRKVyLGEDFRL 240
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
807-1022 |
2.69e-21 |
|
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: 94.10 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGV 885
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQYNVLFDMlTV-----------DEHVWFYGRLKGLSAAVVGpeqdrllQDVGLVSKQSVQTRHLSGGmQRKL-SVAIA 953
Cdd:cd03244 83 IPQDPVLFSG-TIrsnldpfgeysDEELWQALERVGLKEFVES-------LPGGLDTVVEEGGENLSVG-QRQLlCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599 954 FVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDeAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
817-1022 |
4.48e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.28 E-value: 4.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 817 PGSPQPA--LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-----SMAAIRPHLGVCPQY 889
Cdd:PRK13641 14 PGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnkNLKKLRKKVSLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 890 --NVLFDMlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLvsKQSVQTR---HLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:PRK13641 94 peAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGL--SEDLISKspfELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599 965 EPTAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
810-1022 |
1.18e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.84 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 810 RSLEKRFPGSPQP------ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAfilghDVRSSMAAIrphL 883
Cdd:COG1134 22 RSLKELLLRRRRTrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-----EVNGRVSAL---L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 884 GVcpqyNVLFDM-LTVDEHVWFYGRLKGLSAAvvgpEQDRLLQDV------GLVSKQSVqtRHLSGGMQRKLSVAIAFVG 956
Cdd:COG1134 94 EL----GAGFHPeLTGRENIYLNGRLLGLSRK----EIDEKFDEIvefaelGDFIDQPV--KTYSSGMRARLAFAVATAV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 957 GSQVVILDEPTAGVDPA----SRRGIWELLlkyREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:COG1134 164 DPDILLVDEVLAVGDAAfqkkCLARIRELR---ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
817-1022 |
1.38e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.03 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 817 PGSP--QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSA-----FILGHDVRSSMAAIRPHLGVCPQY 889
Cdd:PRK13643 13 PNSPfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdiVVSSTSKQKEIKPVRKKVGVVFQF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 890 --NVLFDMlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLvSKQSVQTR--HLSGGMQRKLSVAIAFVGGSQVVILDE 965
Cdd:PRK13643 93 peSQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGL-ADEFWEKSpfELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 966 PTAGVDPASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
807-1022 |
1.62e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.54 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSaFILGHDVRS--SMAAIRPHLG 884
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGT-ITVGGMVLSeeTVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 885 VCPQY-NVLFDMLTVDEHVWFygrlkGLSAAVVGPEQ--DRLLQDVGLVSKQSVQTR---HLSGGmqRKLSVAIAFVGGS 958
Cdd:PRK13635 85 MVFQNpDNQFVGATVQDDVAF-----GLENIGVPREEmvERVDQALRQVGMEDFLNRephRLSGG--QKQRVAIAGVLAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 959 Q--VVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAeLLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13635 158 QpdIIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTP 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
807-1015 |
1.79e-20 |
|
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: 92.29 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGV 885
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQYNVLFDMlTVDEHVwFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTR------HLSGGMQRKLSVAIAFVGGSQ 959
Cdd:cd03251 81 VSQDVFLFND-TVAENI-AYGRPGATREEVEEAARAANAHEFIMELPEGYDTVigergvKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 960 VVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAElLGDRVAVVAGGR 1015
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIE-NADRIVVLEDGK 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
815-1001 |
1.82e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.76 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 815 RFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSafilghdvRSSMAAIRPHLgvCPQYNVLFD 894
Cdd:NF040873 1 GYGG--RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT--------VRRAGGARVAY--VPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 895 ML--TVDEHV----W----FYGRLKGLSAAVVgpeqDRLLQDVGL--VSKQSVQTrhLSGG-MQRKLsVAIAFVGGSQVV 961
Cdd:NF040873 69 SLplTVRDLVamgrWarrgLWRRLTRDDRAAV----DDALERVGLadLAGRQLGE--LSGGqRQRAL-LAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768000599 962 ILDEPTAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEA 1001
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELV 182
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
807-1017 |
2.52e-20 |
|
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: 93.96 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQP--ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPP---SGGSAFILGHDV----RSSMA 877
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklsEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 878 AIR-PHLGVCPQ--YNVLFDMLTVDEHVW-FYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRH---LSGGMQRKLSV 950
Cdd:COG0444 82 KIRgREIQMIFQdpMTSLNPVMTVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYpheLSGGMRQRVMI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599 951 AIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLC 1017
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
807-1037 |
3.08e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.56 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIRPHLGV 885
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQY--NVLFDMlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:PRK13652 83 VFQNpdDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 964 DEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP--LFLRRHLGSGYYLTL 1037
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVeeIFLQPDLLARVHLDL 239
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
805-1020 |
4.70e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.01 E-value: 4.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 805 PGVSVRSLEKRFPgsPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLG 884
Cdd:PRK09700 4 PYISMAGIGKSFG--PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 885 VCPQYNVL--FDMLTVDEHVwFYGRL---KGLSAAVVGPEQDR-----LLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAF 954
Cdd:PRK09700 82 IGIIYQELsvIDELTVLENL-YIGRHltkKVCGVNIIDWREMRvraamMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599 955 VGGSQVVILDEPTAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCG 1020
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
798-1022 |
4.91e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 94.24 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 798 EAPPGLSPGVSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMA 877
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 878 AIRPHLGVCPQYnVLFDMLTVDEHVWFYGRLKGLSAAVVGPeqdRLLQDVGLVSKQSVQTR---HLSGGMQRKLSVAIAF 954
Cdd:PRK09452 84 ENRHVNTVFQSY-ALFPHMTVFENVAFGLRMQKTPAAEITP---RVMEALRMVQLEEFAQRkphQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000599 955 VGGSQVVILDEPTAGVDPASRRGIwELLLKY--RE-GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQM-QNELKAlqRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
817-1022 |
7.14e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.01 E-value: 7.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 817 PGSP--QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFIlGHDVRSS------MAAIRPHLGVCPQ 888
Cdd:PRK13634 14 YKTPfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAgkknkkLKPLRKKVGIVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 889 Y--NVLFDMlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLvsKQSVQTR---HLSGGMQRKlsVAIAFVGGSQ--VV 961
Cdd:PRK13634 93 FpeHQLFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGL--PEELLARspfELSGGQMRR--VAIAGVLAMEpeVL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 962 ILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTP 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
821-1048 |
7.25e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.61 E-value: 7.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 821 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSS---MAAIRPHLGVC---PQYNVLFD 894
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSkrgLLALRQQVATVfqdPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 895 mlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQ--DVGLVSKQSVQTrhLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDP 972
Cdd:PRK13638 94 --DIDSDIAFSLRNLGVPEAEITRRVDEALTlvDAQHFRHQPIQC--LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 973 ASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP--LFLRRHLGSGYYLT---LVKAR----L 1042
Cdd:PRK13638 170 AGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPgeVFACTEAMEQAGLTqpwLVKLHtqlgL 249
|
....*.
gi 768000599 1043 PLTTNE 1048
Cdd:PRK13638 250 PLCKTE 255
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
777-1033 |
8.21e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.36 E-value: 8.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 777 PRPPKSPAPCPTPLdpkvlveeappglspgVSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSG 856
Cdd:PRK11607 6 PRPQAKTRKALTPL----------------LEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 857 LFPPSGGSAFILGHDVRSSMAAIRPhLGVCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVgpeQDRLLQDVGLVSKQSVQ 936
Cdd:PRK11607 68 FEQPTAGQIMLDGVDLSHVPPYQRP-INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEI---ASRVNEMLGLVHMQEFA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 937 TR---HLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASR-RGIWELL-LKYREGRTLILSTHHLDEAELLGDRVAVV 1011
Cdd:PRK11607 144 KRkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdRMQLEVVdILERVGVTCVMVTHDQEEAMTMAGRIAIM 223
|
250 260
....*....|....*....|..
gi 768000599 1012 AGGRLCCCGSPLFLRRHLGSGY 1033
Cdd:PRK11607 224 NRGKFVQIGEPEEIYEHPTTRY 245
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
804-1016 |
8.94e-20 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 90.19 E-value: 8.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 804 SPGVSVRSLEKRFPGSPQP--ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVrSSM----- 876
Cdd:COG4181 6 APIIELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL-FALdedar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 877 AAIRP-HLGVCPQYNVLFDMLTVDEHVWFYGRLKGLSAAvvgpeQDR---LLQDVGLVSKQSVQTRHLSGGMQRKLSVAI 952
Cdd:COG4181 85 ARLRArHVGFVFQSFQLLPTLTALENVMLPLELAGRRDA-----RARaraLLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 953 AFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHhldEAELLG--DRVAVVAGGRL 1016
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLfeLNRERGTTLVLVTH---DPALAArcDRVLRLRAGRL 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
823-1043 |
1.27e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.99 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSS-----MAAIRPHLGVCPQY--NVLFDM 895
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyIRPVRKRIGMVFQFpeSQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 896 lTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVG----LVSKQSVQtrhLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVD 971
Cdd:PRK13646 102 -TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGfsrdVMSQSPFQ---MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768000599 972 PASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPlflRRHLGSGYYLTLVKARLP 1043
Cdd:PRK13646 178 PQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP---KELFKDKKKLADWHIGLP 248
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
822-1027 |
1.99e-19 |
|
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: 88.82 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMlTVDE 900
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG-TIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 901 HVwFYGRLKG------LSAAVVGPEQ--DRLLQdvGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDP 972
Cdd:cd03254 96 NI-RLGRPNAtdeeviEAAKEAGAHDfiMKLPN--GYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 973 ASRRGIWELLLKYREGRTLILSTHHLD---EAellgDRVAVVAGGRLCCCGSP--LFLRR 1027
Cdd:cd03254 173 ETEKLIQEALEKLMKGRTSIIIAHRLStikNA----DKILVLDDGKIIEEGTHdeLLAKK 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
821-1025 |
2.69e-19 |
|
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: 88.83 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 821 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFdmltvD 899
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLF-----N 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 900 EHVWF---YGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTR------HLSGGMQRKLSVAIAFVGGSQVVILDEPTAGV 970
Cdd:cd03253 89 DTIGYnirYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIvgerglKLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768000599 971 DPASRRGIWELLLKYREGRTLILSTHHLDEAeLLGDRVAVVAGGRLCCCGSPLFL 1025
Cdd:cd03253 169 DTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEEL 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
823-1021 |
2.85e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.06 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTL-SI--LSGLFP--PSGGSAFILGHDV---RSSMAAIRPHLGVCPQYNVLFD 894
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLrSInrMNDLNPevTITGSIVYNGHNIyspRTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 895 MlTVDEHVWFYGRLKG--------------LSAAVVGPEQDRLLQDVGLvskqsvqtrHLSGGMQRKLSVAIAFVGGSQV 960
Cdd:PRK14239 100 M-SIYENVVYGLRLKGikdkqvldeaveksLKGASIWDEVKDRLHDSAL---------GLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000599 961 VILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGS 1021
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYND 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
807-1016 |
2.87e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.04 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFI----------LGHDvRSSM 876
Cdd:PRK11264 4 IEVKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarsLSQQ-KGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 877 AAIRPHLGVCPQYNVLFDMLTVDEHVwFYGRL--KGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAF 954
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENI-IEGPVivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 955 VGGSQVVILDEPTAGVDPASrrgIWELLLKYR----EGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPEL---VGEVLNTIRqlaqEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
824-1014 |
3.87e-19 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 88.29 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSmaaiRPHLGVCPQYNVLFDMLTVDEHVw 903
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEP----GPDRMVVFQNYSLLPWLTVRENI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 904 fYGRLKGLSAAVVGPEQDRLLQD----VGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIW 979
Cdd:TIGR01184 76 -ALAVDRVLPDLSKSERRAIVEEhialVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 768000599 980 ELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGG 1014
Cdd:TIGR01184 155 EELMQIWEehRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
804-1021 |
4.16e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.35 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 804 SPGVSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPH 882
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 883 LGVCPQyNVlfdmltvdeHVwFYGRLKG-LSAAVVGPEQDRL---LQDVGLV----SKQSVQT------RHLSGGMQRKL 948
Cdd:PRK11160 416 ISVVSQ-RV---------HL-FSATLRDnLLLAAPNASDEALievLQQVGLEklleDDKGLNAwlgeggRQLSGGEQRRL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 949 SVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLgDRVAVVAGGRLCCCGS 1021
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
807-1015 |
6.88e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.22 E-value: 6.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRF-PGSP--QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-------RSSM 876
Cdd:COG1101 2 LELKNLSKTFnPGTVneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 877 AAiR----PHLGVCPQynvlfdmLTVDEHV---WFYGRLKGLSAAVVGPEQDR---LLQ--DVGLVSKQSVQTRHLSGGm 944
Cdd:COG1101 82 IG-RvfqdPMMGTAPS-------MTIEENLalaYRRGKRRGLRRGLTKKRRELfreLLAtlGLGLENRLDTKVGLLSGG- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768000599 945 QRK-LSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKY--REGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:COG1101 153 QRQaLSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
824-1004 |
7.32e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.85 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPH-LGvcpQYNVLFDMLTVDEHV 902
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHyLG---HRNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 903 WFYGRLKGLSAAVVgpeqDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL 982
Cdd:PRK13539 95 EFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
170 180
....*....|....*....|....*.
gi 768000599 983 LKYRE-GRTLILSTHH---LDEAELL 1004
Cdd:PRK13539 171 RAHLAqGGIVIAATHIplgLPGAREL 196
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
807-1016 |
8.22e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 89.75 E-value: 8.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQP--ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIR 880
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalsERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 881 PHLGVCPQ-YNvLFDMLTVDEHVWFYGRLKGLSAAvvgpEQDR----LLQDVGLVSKQSVQTRHLSGGM-QRklsVAIA- 953
Cdd:COG1135 82 RKIGMIFQhFN-LLSSRTVAENVALPLEIAGVPKA----EIRKrvaeLLELVGLSDKADAYPSQLSGGQkQR---VGIAr 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 954 -FVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:COG1135 154 aLANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
807-1022 |
8.79e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.46 E-value: 8.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMA---AIRPHL 883
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVderLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 884 G-VCPQYNvLFDMLTVDEHVWFyG--RLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQV 960
Cdd:PRK09493 80 GmVFQQFY-LFPHLTALENVMF-GplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 961 VILDEPTAGVDPASRRgiwELLLKYR----EGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK09493 158 MLFDEPTSALDPELRH---EVLKVMQdlaeEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
810-1016 |
2.47e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 88.32 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 810 RSLEKRFPGSPQP--ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIRPHL 883
Cdd:PRK11153 5 KNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 884 GVCPQYnvlFDML---TVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGM-QRklsVAIAFVGGS- 958
Cdd:PRK11153 85 GMIFQH---FNLLssrTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQkQR---VAIARALASn 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000599 959 -QVVILDEPTAGVDPASRRGIWELLLKY-RE-GRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK11153 159 pKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
821-1026 |
5.02e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.32 E-value: 5.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 821 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIRPHLGVCPQY-NVLFDMLTV 898
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLtEENVWDIRHKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 899 DEHVWFYGRLKGLSAAVVgpeQDRLLQDVGLVSKQSVQTRH---LSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASR 975
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEM---KERVNEALELVGMQDFKEREparLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768000599 976 RGIWELLLKYRE--GRTLILSTHHLDEAElLGDRVAVVAGGRLCCCGSP--LFLR 1026
Cdd:PRK13650 177 LELIKTIKGIRDdyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPreLFSR 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
815-1035 |
5.99e-18 |
|
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: 84.85 E-value: 5.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 815 RFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLF 893
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 894 DMLTVD-----------EHVWFYGRLKGLSAAVV----GPEQdrllqdvgLVSKQSVQtrhLSGGMQRKLSVAIAFVGGS 958
Cdd:cd03252 89 NRSIRDnialadpgmsmERVIEAAKLAGAHDFISelpeGYDT--------IVGEQGAG---LSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599 959 QVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLdEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYL 1035
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
815-1040 |
8.79e-18 |
|
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: 84.51 E-value: 8.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 815 RFPGSP-QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVL 892
Cdd:cd03249 9 RYPSRPdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 893 FDMlTVDEHVwFYGRLKGLSAAVVG--------------PEQ-DRLLQDVGLvskqsvqtrHLSGGMQRKLSVAIAFVGG 957
Cdd:cd03249 89 FDG-TIAENI-RYGKPDATDEEVEEaakkanihdfimslPDGyDTLVGERGS---------QLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 958 SQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLD---EAellgDRVAVVAGGRLCCCGSPLFLRRhlGSGYY 1034
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLStirNA----DLIAVLQNGQVVEQGTHDELMA--QKGVY 231
|
....*.
gi 768000599 1035 LTLVKA 1040
Cdd:cd03249 232 AKLVKA 237
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
821-1022 |
1.26e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.30 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 821 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMA-AIRPHLGVCPQYNVLFDMLTVD 899
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALLPQHHLTPEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 900 E--------HVWFYGRLKGLSAAVVgpeqDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVD 971
Cdd:PRK11231 95 ElvaygrspWLSLWGRLSAEDNARV----NQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768000599 972 PASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK11231 171 INHQVELMRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
808-1016 |
1.40e-17 |
|
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: 81.88 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 808 SVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVC 886
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMlTVDEHVwfygrlkglsaavvgpeqdrllqdvglvskqsvqtrhLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03246 82 PQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768000599 967 TAGVDPASRRGIWELLLKYRE-GRTLILSTHHLDEAELLgDRVAVVAGGRL 1016
Cdd:cd03246 124 NSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
813-1016 |
1.93e-17 |
|
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: 82.73 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 813 EKRFPGSpqpalrGLSLDF-YQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAI-----RPHLGVC 886
Cdd:cd03297 7 EKRLPDF------TLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDMLTVDEHVWFygrlkGLSAAVVGPEQDRLLQDVGLVSKQSVQTRH---LSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:cd03297 81 FQQYALFPHLNVRENLAF-----GLKRKRNREDRISVDELLDLLGLDHLLNRYpaqLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768000599 964 DEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:cd03297 156 DEPFSALDRALRLQLLPELkqIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
824-996 |
2.72e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.86 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIR-PHLGVCPQYNVLFDMLTV 898
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldADALAQLRrEHFGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 899 DEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGI 978
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170
....*....|....*....
gi 768000599 979 WELLLKYRE-GRTLILSTH 996
Cdd:PRK10535 184 MAILHQLRDrGHTVIIVTH 202
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
812-1016 |
3.25e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.23 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 812 LEKRFPGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIRPHLGVCP 887
Cdd:PRK10908 7 VSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 888 QYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPT 967
Cdd:PRK10908 86 QDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 768000599 968 AGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
827-1035 |
5.96e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 827 LSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVR--SSMAAIRPHLGVCPQYNVLFDMLTVDEHVWF 904
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLPQEASIFRRLSVYDNLMA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 905 YGRL-KGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLL 983
Cdd:PRK10895 102 VLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIE 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 984 KYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFL-------RRHLGSGYYL 1035
Cdd:PRK10895 182 HLRDsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIlqdehvkRVYLGEDFRL 241
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
823-1021 |
7.38e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 82.09 E-value: 7.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIrPHLGVC-----PqyNVlFDML 896
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLtGLDEHEI-ARLGIGrkfqkP--TV-FEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 897 TVDEH----------VW---FYGRLKGLSAAVvgpeqDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:COG4674 101 TVFENlelalkgdrgVFaslFARLTAEERDRI-----EEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 964 DEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGS 1021
Cdd:COG4674 176 DEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
822-1022 |
7.83e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.73 E-value: 7.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV--RSSMAAIRPHLGVCPQY-NVLFDMLTV 898
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIVFQNpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 899 DEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGI 978
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768000599 979 WELLLK-YREGRTLILSTHHLDEAElLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13644 176 LERIKKlHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEP 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
807-1016 |
1.09e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSaFILGHDVRssmaairphLGVC 886
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGETVK---------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYNVLFDM-LTVDEHVWfygrlkglSAAVVGPEQD--RLLQDVGLvSKQSVQT--RHLSGGMQRKLSVAIAFVGGSQVV 961
Cdd:COG0488 384 DQHQEELDPdKTVLDELR--------DGAPGGTEQEvrGYLGRFLF-SGDDAFKpvGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599 962 ILDEPTAGVDPASRRGIWELLLKYrEGrTLILSTHhlDEA--ELLGDRVAVVAGGRL 1016
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSH--DRYflDRVATRILEFEDGGV 507
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
804-1016 |
1.11e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.35 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 804 SPGVSVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVR--SSMAAIRP 881
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 882 HLGVCPQYNVLFDMLTVDEHVWFyGRL--------KGLSAAVVGPEQDRLLQDVglvsKQSVQTRHLSGGMQRKLSVAIA 953
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLYL-GQLphkggivnRRLLNYEAREQLEHLGVDI----DPDTPLKYLSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 954 FVGGSQVVILDEPTAGVdpaSRRGIwELLLKY-----REGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK11288 155 LARNARVIAFDEPTSSL---SAREI-EQLFRVirelrAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
802-1030 |
1.29e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 83.25 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 802 GLSPGVSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTlSILSGLFPPSGGSAFILGHDVRSSMAAIRP 881
Cdd:NF000106 9 GARNAVEVRGLVKHF--GEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 882 HLGVC-PQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQV 960
Cdd:NF000106 86 TIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000599 961 VILDEPTAGVDPASRRGIW-ELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLG 1030
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWdEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
809-1001 |
1.38e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.28 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 809 VRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAairpHLGVCPQ 888
Cdd:PRK11248 4 ISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA----ERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 889 YNVLFDMLTVDEHVWFygrlkGLSAAVVGPEQDR-----LLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:PRK11248 78 NEGLLPWRNVQDNVAF-----GLQLAGVEKMQRLeiahqMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 768000599 964 DEPTAGVDPASRRGIWELLLK--YREGRTLILSTHHLDEA 1001
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEA 192
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
822-1004 |
1.59e-16 |
|
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: 79.71 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNVLFDMLTVDEH 901
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 902 VWFYgrlkglsAAVVGPEQ---DRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGI 978
Cdd:TIGR01189 94 LHFW-------AAIHGGAQrtiEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170 180 190
....*....|....*....|....*....|
gi 768000599 979 WELLLKYRE-GRTLILSTHH---LDEAELL 1004
Cdd:TIGR01189 167 AGLLRAHLArGGIVLLTTHQdlgLVEAREL 196
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
823-1022 |
1.98e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.54 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIR----PHLGVCPQYNVLFDMLT 897
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIaKISDAELRevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 898 VDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRG 977
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 768000599 978 IWELLLKY--REGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK10070 203 MQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1467-1605 |
2.70e-16 |
|
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: 82.44 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 1467 AQDSLKIWFNNKGWHSMVAFVNRASNAILRAHLPPGPARHAHSITTLNHPLNLTKEQLSEGalmaSSVDVLVSICVVFAM 1546
Cdd:pfam12698 97 ESATVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQS----GYAYYLVGLILMIII 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599 1547 SFVPASFTLVLIEERVTRAKHLQLMGGLSPTLYWLGNFLWDMCNYLVPACIVVLIFLAF 1605
Cdd:pfam12698 173 LIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGI 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
810-1016 |
2.91e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 810 RSLEKRFPGSPQP---------------ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-- 872
Cdd:COG1129 239 RELEDLFPKRAAApgevvleveglsvggVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVri 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 873 RSSMAAIRPHLGVCP---QYNVLFDMLTVDEHVWFyGRLKGLSAAVV--GPEQDRLLQDvgLVSKQSVQT-------RHL 940
Cdd:COG1129 319 RSPRDAIRAGIAYVPedrKGEGLVLDLSIRENITL-ASLDRLSRGGLldRRRERALAEE--YIKRLRIKTpspeqpvGNL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 941 SGGMQRKlsVAIA--FVGGSQVVILDEPTAGVDPASRRGIWELLLKY-REGRTLILSTHHLDeaELLG--DRVAVVAGGR 1015
Cdd:COG1129 396 SGGNQQK--VVLAkwLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaAEGKAVIVISSELP--ELLGlsDRILVMREGR 471
|
.
gi 768000599 1016 L 1016
Cdd:COG1129 472 I 472
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
828-1016 |
3.70e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 79.63 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 828 SLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPhLGVCPQYNVLFDMLTVDEHVWFyGR 907
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP-VSMLFQENNLFSHLTVAQNIGL-GL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 908 LKGLSaavVGPEQDRLLQD----VGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLL 983
Cdd:PRK10771 97 NPGLK---LNAAQREKLHAiarqMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190
....*....|....*....|....*....|....*
gi 768000599 984 KYREGR--TLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK10771 174 QVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
805-1022 |
3.87e-16 |
|
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: 83.70 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 805 PGVSVRSLEKRFPGSPQ---PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRP 881
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 882 --------HLGVCPQYNVLFDMLTVdehvwfygrLKGLSAAVVGPEQDRL--------LQDVGLVSKQSVQ-----TRHL 940
Cdd:TIGR03269 358 dgrgrakrYIGILHQEYDLYPHRTV---------LDNLTEAIGLELPDELarmkavitLKMVGFDEEKAEEildkyPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 941 SGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCC 1018
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
....
gi 768000599 1019 CGSP 1022
Cdd:TIGR03269 509 IGDP 512
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
818-1022 |
3.99e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.52 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 818 GSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVR--SSMAAIRPHLGVCPQY--NVLF 893
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeENLWDIRNKAGMVFQNpdNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 894 DMLtVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGmqRKLSVAIAFVGGSQ--VVILDEPTAGVD 971
Cdd:PRK13633 100 ATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGG--QKQRVAIAGILAMRpeCIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768000599 972 PASRR----GIWELLLKYreGRTLILSTHHLDEAeLLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13633 177 PSGRRevvnTIKELNKKY--GITIILITHYMEEA-VEADRIIVMDSGKVVMEGTP 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
805-1022 |
5.32e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.20 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 805 PGVSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHL 883
Cdd:PRK09536 2 PMIDVSDLSVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 884 GVCPQYNVL---FDMLTVDE-----HVWFYGRLKGLSAAVVGPEQDRLlqDVGLVSKQSVQTrhLSGGMQRKLSVAIAFV 955
Cdd:PRK09536 80 ASVPQDTSLsfeFDVRQVVEmgrtpHRSRFDTWTETDRAAVERAMERT--GVAQFADRPVTS--LSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 956 GGSQVVILDEPTAGVDpaSRRGIWELLLKYR---EGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK09536 156 QATPVLLLDEPTASLD--INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
805-1022 |
9.13e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.88 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 805 PGVSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV--RSSMAAIRph 882
Cdd:PRK11300 4 PLLSVSGLMMRFGG--LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPGHQIAR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 883 LGVCPQY-NV-LFDMLTVDE--------HV---WFYGRLKglSAAVVGPEQDRL------LQDVGLVSKQSVQTRHLSGG 943
Cdd:PRK11300 80 MGVVRTFqHVrLFREMTVIEnllvaqhqQLktgLFSGLLK--TPAFRRAESEALdraatwLERVGLLEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 944 MQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGS 1021
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
.
gi 768000599 1022 P 1022
Cdd:PRK11300 238 P 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
824-1022 |
1.28e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.40 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPS---GGSAFILGHDVRSSMaaIRPHLGVCPQYNVLFDMLTVDE 900
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKE--MRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 901 HVWFYGRLKgLSAAVVGPEQ----DRLLQDVGLVSKQSV------QTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGV 970
Cdd:TIGR00955 119 HLMFQAHLR-MPRRVTKKEKrervDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 768000599 971 DPASRRGIWELLLKYREGRTLILSTHHLDEAEL--LGDRVAVVAGGRLCCCGSP 1022
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELfeLFDKIILMAEGRVAYLGSP 251
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
807-1016 |
1.49e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.52 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLF---PPSGGSAFILGH----------DVR 873
Cdd:PRK09984 5 IRVEKLAKTF--NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRtvqregrlarDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 874 SSmaaiRPHLGVCPQYNVLFDMLTVDEHV----------------WFygrlkglsaavvGPEQD----RLLQDVGLV--S 931
Cdd:PRK09984 83 KS----RANTGYIFQQFNLVNRLSVLENVligalgstpfwrtcfsWF------------TREQKqralQALTRVGMVhfA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 932 KQSVQTrhLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVA 1009
Cdd:PRK09984 147 HQRVST--LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYALRYCERIV 224
|
....*..
gi 768000599 1010 VVAGGRL 1016
Cdd:PRK09984 225 ALRQGHV 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
807-1085 |
1.60e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.15 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFpGSpQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC 886
Cdd:PRK11432 7 VVLKNITKRF-GS-NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 PQYnVLFDMLTVDEHVWFYGRLKGLSAAVVgpeQDRLLQDVGLVSKQSVQTRH---LSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:PRK11432 85 QSY-ALFPHMSLGENVGYGLKMLGVPKEER---KQRVKEALELVDLAGFEDRYvdqISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 964 DEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP---------LFLRRHLG-- 1030
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPqelyrqpasRFMASFMGda 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599 1031 -------SGYYLTLVKARLPLTTNEKAD-TDMEGSVDTRQE----KKNGSQGSRVGTPQLLALVQHW 1085
Cdd:PRK11432 241 nifpatlSGDYVDIYGYRLPRPAAFAFNlPDGECTVGVRPEaitlSEQGEESQRCTIKHVAYMGPQY 307
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
807-1022 |
2.69e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.70 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVR------------- 873
Cdd:PRK10619 6 LNVIDLHKRY--GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 874 -SSMAAIRPHLGVCPQYNVLFDMLTVDEHVWFYG-RLKGLSAAVVGPEQDRLLQDVGLVSKQSVQ-TRHLSGGMQRKLSV 950
Cdd:PRK10619 84 kNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 951 AIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
804-1014 |
3.56e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 804 SPGVSVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHL 883
Cdd:PRK15439 9 PPLLCARSISKQYSGVE--VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 884 GV--CPQYNVLFDMLTVDEHVWFygRLKGLSAAVVGPEQdrLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVV 961
Cdd:PRK15439 87 GIylVPQEPLLFPNLSVKENILF--GLPKRQASMQKMKQ--LLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 768000599 962 ILDEPTAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGG 1014
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLaQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
824-1013 |
5.47e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.97 E-value: 5.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVrSSM-----AAIRP-HLGVCPQYNVLFDMLT 897
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL-HQMdeearAKLRAkHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 898 VDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRG 977
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 768000599 978 IWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAG 1013
Cdd:PRK10584 185 IADLLfsLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
823-1013 |
7.47e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.85 E-value: 7.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSsmaAIRPHL-GVCPQYN-VLFDMLTVDE 900
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLvAYVPQSEeVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 901 HVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRH-----LSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASR 975
Cdd:PRK15056 99 DVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHrqigeLSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 768000599 976 RGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAG 1013
Cdd:PRK15056 179 ARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
823-1016 |
1.02e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.69 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAA--IRPHLGVCPQYNVLFDMLTVDE 900
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 901 HVWFYGRLkglsaAVVGPEQDRLLQDVGLV----SKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRR 976
Cdd:PRK11614 100 NLAMGGFF-----AERDQFQERIKWVYELFprlhERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 768000599 977 GIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK11614 175 QIFDTIEQLReQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
825-1016 |
1.18e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 825 RGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVC------PQYNVLFDM--- 895
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDApla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 896 -----LTVDEHVWFYGRLKglSAAVVgpeqDRLLQDVGLVSKQSVQT-RHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 969
Cdd:PRK15439 360 wnvcaLTHNRRGFWIKPAR--ENAVL----ERYRRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768000599 970 VDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK15439 434 VDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
805-1015 |
1.36e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.73 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 805 PGVSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSA-FILGHDVRSSMAAI---- 879
Cdd:PRK11701 5 PLLSVRGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYALseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 880 RPHL-----GVCPQY-------------NV---LfdMLTVDEHvwfYGRLKglSAAVvgpeqdRLLQDVGL-VSKQSVQT 937
Cdd:PRK11701 83 RRRLlrtewGFVHQHprdglrmqvsaggNIgerL--MAVGARH---YGDIR--ATAG------DWLERVEIdAARIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 938 RHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
799-1016 |
1.42e-14 |
|
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: 74.81 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 799 APPGLSPGVSVRSLEKRFPGSP-QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SM 876
Cdd:cd03248 4 APDHLKGIVKFQNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 877 AAIRPHLGVCPQYNVLFDMlTVDEHVwFYG----RLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTR--HLSGGMQRKLSV 950
Cdd:cd03248 84 KYLHSKVSLVGQEPVLFAR-SLQDNI-AYGlqscSFECVKEAAQKAHAHSFISELASGYDTEVGEKgsQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 951 AIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAElLGDRVAVVAGGRL 1016
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
807-1026 |
1.46e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLekRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIRPH 882
Cdd:PRK11831 8 VDMRGV--SFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 883 LGVCPQYNVLFDMLTVDEHVWFYGRLKG-LSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVV 961
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLREHTqLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599 962 ILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLR 1026
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLIseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
823-1022 |
1.56e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.56 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQ------------Y 889
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdNFEKLRKHIGIVFQnpdnqfvgsivkY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 890 NVLFDMltvDEHVWFYGRLKGLSAAVvgpeqdrlLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 969
Cdd:PRK13648 104 DVAFGL---ENHAVPYDEMHRRVSEA--------LKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768000599 970 VDPASRRGIWELLLKYREGR--TLILSTHHLDEAeLLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEGTP 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
807-1016 |
1.70e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 75.33 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFpGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLF-----PPSGGSAFILGHDV-RSSMAAIR 880
Cdd:PRK14247 4 IEIRDLKVSF-GQVE-VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 881 PHLGVCPQYNVLFDMLTVDEHVwfygrlkglsaaVVGPEQDRLLQdvglvSKQSVQTR---------------------- 938
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENV------------ALGLKLNRLVK-----SKKELQERvrwalekaqlwdevkdrldapa 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599 939 -HLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK14247 145 gKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
824-1022 |
1.90e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 76.66 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVrSSMAAIRPHLGVCPQYNVLFDMLTVDEHVW 903
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVFQHYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 904 F----YGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIW 979
Cdd:PRK10851 97 FgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768000599 980 ELL------LKYregrTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK10851 177 RWLrqlheeLKF----TSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
790-1016 |
2.04e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 790 LDPKVLVEEAPPGlSPGVSVRSLEKRfPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILG 869
Cdd:COG3845 242 VLLRVEKAPAEPG-EVVLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 870 HDV---------RSSMAAI---RPHLGVCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGlVSKQSVQT 937
Cdd:COG3845 320 EDItglsprerrRLGVAYIpedRLGRGLVPDMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELIEEFD-VRTPGPDT 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 938 --RHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGG 1014
Cdd:COG3845 399 paRSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILALSDRIAVMYEG 478
|
..
gi 768000599 1015 RL 1016
Cdd:COG3845 479 RI 480
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
824-997 |
2.49e-14 |
|
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: 73.30 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILG---HDVRSSMAAIRPHLGVCPQYNVLfdmLTVDE 900
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgplDFQRDSIARGLLYLGHAPGIKTT---LSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 901 HVWFYGRLKGLSAAvvgpeqDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWE 980
Cdd:cd03231 93 NLRFWHADHSDEQV------EEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170
....*....|....*...
gi 768000599 981 LLLKYRE-GRTLILSTHH 997
Cdd:cd03231 167 AMAGHCArGGMVVLTTHQ 184
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
823-1029 |
4.47e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.27 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSA----FILGHDVRSSMAAIRPH-------------LGV 885
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPYskkiknfkelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 C---PQYNVLFDmlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLvsKQSVQTRH---LSGGMQRKLSVAIAFVGGSQ 959
Cdd:PRK13631 121 VfqfPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGL--DDSYLERSpfgLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 960 VVILDEPTAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP--LFLRRHL 1029
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPyeIFTDQHI 269
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
826-1042 |
5.37e-14 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 73.17 E-value: 5.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 826 GLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPP----SGGSAFILGHDVRSSmaAIRP-HLGVCPQ-----YNVLFDM 895
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPL--SIRGrHIATIMQnprtaFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 896 ltvDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRH---LSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDP 972
Cdd:TIGR02770 82 ---GNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLKKYpfqLSGGMLQRVMIALALLLEPPFLIADEPTTDLDV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768000599 973 ASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKARL 1042
Cdd:TIGR02770 159 VNQARVLKLLRELRQlfGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSAHL 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
807-1016 |
5.90e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 74.74 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRF-PGSPQ--PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSA-FILGHDVRSSMA----- 877
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKNKKKTkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 878 -------------------AIRPHLGVCPQYN--VLFDMlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLvsKQSVQ 936
Cdd:PRK13651 83 vleklviqktrfkkikkikEIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL--DESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 937 TR---HLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVA 1012
Cdd:PRK13651 160 QRspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
....
gi 768000599 1013 GGRL 1016
Cdd:PRK13651 240 DGKI 243
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
823-1023 |
7.02e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.27 E-value: 7.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAI------RPHLGVC---PQYNVLF 893
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlRKEIGLVfqfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 894 DmlTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTR-HLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDP 972
Cdd:PRK13645 106 E--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 768000599 973 ASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPL 1023
Cdd:PRK13645 184 KGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
804-967 |
1.20e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 804 SPGVSVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-----RSSMAA 878
Cdd:PRK10762 2 QALLQLKGIDKAFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 879 ----IRPHLGVCPQynvlfdmLTVDEHVW----FYGRLKGLSAAVVGPEQDRLLQDVGL--VSKQSVQTrhLSGGMQRKL 948
Cdd:PRK10762 80 gigiIHQELNLIPQ-------LTIAENIFlgreFVNRFGRIDWKKMYAEADKLLARLNLrfSSDKLVGE--LSIGEQQMV 150
|
170
....*....|....*....
gi 768000599 949 SVAIAFVGGSQVVILDEPT 967
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPT 169
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
824-1008 |
2.31e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.39 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS----SMAAIRPH-LGVCPQYNVLFDMLTV 898
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaAKAELRNQkLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 899 DEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGI 978
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190
....*....|....*....|....*....|..
gi 768000599 979 WELL--LKYREGRTLILSTHHLDEAELLGDRV 1008
Cdd:PRK11629 185 FQLLgeLNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
824-1022 |
2.49e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.43 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQY-NVLFDMLTVDEH 901
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAeNVWNLRRKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 902 VWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWEL 981
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 768000599 982 L--LKYREGRTLILSTHHLDEAElLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13642 183 IheIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAP 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
803-1013 |
3.22e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.61 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 803 LSPGVSVRSLEkrFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSG-----GSAFILGHDV---RS 874
Cdd:PRK14258 4 LIPAIKVNNLS--FYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 875 SMAAIRPHLG-VCPQYNvLFDMlTVDEHVWFYGRLKGLSAAVvgpEQDRLLQDVGLVSKQSVQTRH--------LSGGMQ 945
Cdd:PRK14258 82 NLNRLRRQVSmVHPKPN-LFPM-SVYDNVAYGVKIVGWRPKL---EIDDIVESALKDADLWDEIKHkihksaldLSGGQQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 946 RKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAG 1013
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
823-1009 |
3.66e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.35 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSI---LSGLFPP--SGGSAFILGHDVRSSM---AAIRPHLGVCPQYNVLFD 894
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLYAPDvdpVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 895 MlTVDEHVWFYGRLKG------------LSAAVVGPE-QDRLlqdvglvsKQSVQTrhLSGGMQRKLSVAIAFVGGSQVV 961
Cdd:PRK14243 105 K-SIYDNIAYGARINGykgdmdelversLRQAALWDEvKDKL--------KQSGLS--LSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768000599 962 ILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVA 1009
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
825-997 |
3.73e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 825 RGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRssmaAIRPHLgvcpQYNVLF--------DML 896
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDEY----HQDLLYlghqpgikTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 897 TVDEHVWFYGRLKGLsaavvgPEQDRL---LQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPA 973
Cdd:PRK13538 90 TALENLRFYQRLHGP------GDDEALweaLAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170 180
....*....|....*....|....*
gi 768000599 974 SRRGIWELLLKY-REGRTLILSTHH 997
Cdd:PRK13538 164 GVARLEALLAQHaEQGGMVILTTHQ 188
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
821-1016 |
4.32e-13 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 71.37 E-value: 4.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 821 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIRPHLGVCPQ--YNVLFD 894
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldRKQRRAFRRDVQLVFQdsPSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 895 MLTVDEHVWFYGR-LKGLSAAVVGPEQDRLLQDVGLVSKQSVQ-TRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDP 972
Cdd:TIGR02769 104 RMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 768000599 973 ASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:TIGR02769 184 VLQAVILELLrkLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
821-1016 |
4.79e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 821 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-------RSSMAAIRPHLG-VCPQYNvL 892
Cdd:COG4161 15 HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLRQKVGmVFQQYN-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 893 FDMLTVDEH-VWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVD 971
Cdd:COG4161 94 WPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 768000599 972 PASRRGIWELLLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:COG4161 174 PEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
824-1016 |
8.66e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.26 E-value: 8.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSG-----GSAFILGHDVRSSMA---AIRPHLGVCPQYNVLFDM 895
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVdpiEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 896 LTVDEHVWFYGRLKGLSAAvvgpeQDRLLQDVGLVSKQS-----VQTR------HLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLVKS-----KKELDERVEWALKKAalwdeVKDRlndypsNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768000599 965 EPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
796-1027 |
1.04e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.20 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 796 VEEAPPGLSPGVSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS- 874
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESw 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 875 SMAAIRPHLGVCPQYNVLFDMLTVDEHV------WfYGRLKGLSAAvvgpEQDRLLQDVGLVSKQSVQTR---HLSGGMQ 945
Cdd:PRK10575 79 SSKAFARKVAYLPQQLPAAEGMTVRELVaigrypW-HGALGRFGAA----DREKVEEAISLVGLKPLAHRlvdSLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 946 RKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPL 1023
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
....
gi 768000599 1024 FLRR 1027
Cdd:PRK10575 234 ELMR 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
809-996 |
1.62e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 809 VRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGhDVRssmaairphLGVCPQ 888
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR---------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 889 YNVLFDMLTVDEHVwFYG---------RLKGLSAAVVGPEQD------------------------RLLQDVGL-VSKQS 934
Cdd:COG0488 69 EPPLDDDLTVLDTV-LDGdaelraleaELEELEAKLAEPDEDlerlaelqeefealggweaearaeEILSGLGFpEEDLD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768000599 935 VQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRgiW--ELLLKYReGrTLILSTH 996
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYP-G-TVLVVSH 207
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
807-1016 |
1.88e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.89 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKrFPGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGH--DVRSS-----MAAI 879
Cdd:PRK11124 3 IQLNGINC-FYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTpsdkaIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 880 RPHLG-VCPQYNvLFDMLTVDEH-VWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGG 957
Cdd:PRK11124 81 RRNVGmVFQQYN-LWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 958 SQVVILDEPTAGVDPASRRGIWELLLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
836-1022 |
2.26e-12 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 70.53 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 836 ITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIR--PH---LGVCPQYNVLFDMLTVDEHVwFYGRlKG 910
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlpPEkrrIGYVFQEARLFPHLSVRGNL-RYGM-KR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 911 LSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE--G 988
Cdd:TIGR02142 103 ARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAefG 182
|
170 180 190
....*....|....*....|....*....|....
gi 768000599 989 RTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:TIGR02142 183 IPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPI 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
778-1035 |
3.20e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 71.68 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 778 RPPKSPAPcptpldpkvlVEEAPPGLSPGVSVRSLEKRFPGSP-QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSG 856
Cdd:TIGR00958 460 RKPNIPLT----------GTLAPLNLEGLIEFQDVSFSYPNRPdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 857 LFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMlTVDEHVwFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSV 935
Cdd:TIGR00958 530 LYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFSG-SVRENI-AYGLTDTPDEEIMAAAKAANAHDFIMEFPNGY 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 936 QTR------HLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWEllLKYREGRTLILSTHHLDEAElLGDRVA 1009
Cdd:TIGR00958 608 DTEvgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVE-RADQIL 684
|
250 260
....*....|....*....|....*.
gi 768000599 1010 VVAGGRLCCCGSPLFLRRHLGSGYYL 1035
Cdd:TIGR00958 685 VLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
827-1022 |
3.31e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 827 LSLDFYQGHITAFLGHNGAGKTTTLSILSGLFpPSGGSAFILGHDVR----SSMAAIRPHLgvCPQYNVLFDMltvdeHV 902
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEawsaAELARHRAYL--SQQQTPPFAM-----PV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 903 WFYGRLKGLSAAVVGPEQD---RLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVG-------GSQVVILDEPTAGVDP 972
Cdd:PRK03695 87 FQYLTLHQPDKTRTEAVASalnEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768000599 973 ASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK03695 167 AQQAALDRLLSELcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
805-1016 |
3.85e-12 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 68.32 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 805 PGVSVRSLEKRFpgSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHD------------- 871
Cdd:TIGR02323 2 PLLQVSGLSKSY--GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelyqlseae 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 872 ----VRSSMAAIRPH------LGVCPQYNVLFDMLTV-DEHvwfYGRLKglSAAV-----VGPEQDRLlqdvglvskqSV 935
Cdd:TIGR02323 80 rrrlMRTEWGFVHQNprdglrMRVSAGANIGERLMAIgARH---YGNIR--ATAQdwleeVEIDPTRI----------DD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 936 QTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAG 1013
Cdd:TIGR02323 145 LPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQ 224
|
...
gi 768000599 1014 GRL 1016
Cdd:TIGR02323 225 GRV 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
827-1022 |
4.16e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.47 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 827 LSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIRPHLGVCPQYNVLFDMLTVDE----- 900
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARRIGLLAQNATTPGDITVQElvarg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 901 ---HVWFYGRLKGLSAAVVgpeqDRLLQDVGL--VSKQSVQTrhLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASR 975
Cdd:PRK10253 106 rypHQPLFTRWRKEDEEAV----TKAMQATGIthLADQSVDT--LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768000599 976 RGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK10253 180 IDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
821-998 |
4.98e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 821 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNV-----LFD 894
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAMVQQDPVvladtFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 895 MLTV-----DEHVWfygrlkGLSAAVVGPEQDRLLQDvGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAG 969
Cdd:PRK10790 434 NVTLgrdisEEQVW------QALETVQLAELARSLPD-GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATAN 506
|
170 180
....*....|....*....|....*....
gi 768000599 970 VDPASRRGIWELLLKYREGRTLILSTHHL 998
Cdd:PRK10790 507 IDSGTEQAIQQALAAVREHTTLVVIAHRL 535
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
822-1040 |
5.68e-12 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 70.54 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMlTVDE 900
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 901 HVwfygrlkgLSAAVVGPEQDRLLQDV--------------GLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:TIGR01193 567 NL--------LLGAKENVSQDEIWAACeiaeikddienmplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 967 TAGVDPASRRGIWELLLKYREgRTLILSTHHLDEAELLgDRVAVVAGGRLCCCGS--PLFLRrhlgSGYYLTLVKA 1040
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGShdELLDR----NGFYASLIHN 708
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
827-1017 |
5.71e-12 |
|
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: 70.24 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 827 LSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPS-GGSAFILGH--DVRSSMAAIRPHLGVCPQ----YNVLFDM---- 895
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkrHGIVPILgvgk 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 896 -LTVDEHVWFYGRLKGLSAAvvgpEQDRLLQDVglvSKQSVQTRH-------LSGGMQRKLSVAIAFVGGSQVVILDEPT 967
Cdd:TIGR02633 359 nITLSVLKSFCFKMRIDAAA----ELQIIGSAI---QRLKVKTASpflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768000599 968 AGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGRLC 1017
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
824-1022 |
6.93e-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: 66.40 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGlFP---PSGGSAFILGHDV-------RSSMAairphLGVCPQYNVLF 893
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDItdlppeeRARLG-----IFLAFQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 894 DMLTVDEhvwfygrlkglsaavvgpeqdrLLQDVGLvskqsvqtrHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPA 973
Cdd:cd03217 90 PGVKNAD----------------------FLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768000599 974 SRRGIWELLLKYR-EGRTLILSTHHLDEAELL-GDRVAVVAGGRLCCCGSP 1022
Cdd:cd03217 139 ALRLVAEVINKLReEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
800-1016 |
7.31e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.99 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 800 PPGLSPGVSVRSLEKRFPGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAA 878
Cdd:PRK13657 328 LGRVKGAVEFDDVSFSYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 879 IRPHLGVCPQYNVLF-----DMLTV------DEHVwfygrlkgLSAAVVGPEQDRLL-QDVGLVSKQSVQTRHLSGGMQR 946
Cdd:PRK13657 407 LRRNIAVVFQDAGLFnrsieDNIRVgrpdatDEEM--------RAAAERAQAHDFIErKPDGYDTVVGERGRQLSGGERQ 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 947 KLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLD---EAellgDRVAVVAGGRL 1016
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLStvrNA----DRILVFDNGRV 547
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
824-1021 |
1.43e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.61 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFP------PSGGSAFILGHDV-RSSMAAIRPHLGVCPQYNVLFDML 896
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 897 TVDEHVWFYGRLKGLSAA-VVGPEQDRLLQDVGL----VSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVD 971
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 768000599 972 PASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGS 1021
Cdd:PRK14246 186 IVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
823-1016 |
1.51e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 66.60 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGL--FPPSG---GSAFILGHDVRSS---MAAIRPHLGVCPQYNVLFD 894
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDIYDPdvdVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 895 MlTVDEHVwFYG-RLKG------LSAAVvgpeqDRLLQDVGL---VS---KQSVqtRHLSGGMQRKLSVAIAFVGGSQVV 961
Cdd:COG1117 106 K-SIYDNV-AYGlRLHGikskseLDEIV-----EESLRKAALwdeVKdrlKKSA--LGLSGGQQQRLCIARALAVEPEVL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768000599 962 ILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:COG1117 177 LMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
807-1017 |
1.55e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.89 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGV 885
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQyNV-LFDMlTVDEHVWF-----YGRLKGLSAAvvgpeqdRLLQDVGLVSK--QSVQT------RHLSGGMQRKLSVA 951
Cdd:PRK11176 422 VSQ-NVhLFND-TIANNIAYarteqYSREQIEEAA-------RMAYAMDFINKmdNGLDTvigengVLLSGGQRQRIAIA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 952 IAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAElLGDRVAVVAGGRLC 1017
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIE-KADEILVVEDGEIV 557
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
807-996 |
1.71e-11 |
|
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: 63.62 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSaFILGHDVRssmaairphlgvc 886
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWGSTVK------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 887 pqynvlfdmltvdehvwfygrlkglsaavvgpeqdrllqdVGLVSkqsvqtrHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:cd03221 65 ----------------------------------------IGYFE-------QLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|
gi 768000599 967 TAGVDPASRRGIWELLLKYRegRTLILSTH 996
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP--GTVILVSH 125
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
822-1017 |
2.00e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSsmaairphlgVCPQynvlfdmltvdeh 901
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT----------RSPQ------------- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 902 vwfygrlKGLSAAVVGPEQDRllQDVGLV-----------------SKQSVQTRH------------------------- 939
Cdd:PRK10762 323 -------DGLANGIVYISEDR--KRDGLVlgmsvkenmsltalryfSRAGGSLKHadeqqavsdfirlfniktpsmeqai 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 940 --LSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYR-EGRTLILSTHhlDEAELLG--DRVAVVAGG 1014
Cdd:PRK10762 394 glLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSS--EMPEVLGmsDRILVMHEG 471
|
...
gi 768000599 1015 RLC 1017
Cdd:PRK10762 472 RIS 474
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
810-1015 |
3.11e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.89 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 810 RSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFpPSG---GSAFILG-----HDVRSSMAA--- 878
Cdd:NF040905 5 RGITKTFPGVK--ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGevcrfKDIRDSEALgiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 879 -IRPHLGVCPQynvlfdmLTVDEHVwFYGRLKGLSAAVVGPEQDR----LLQDVGLvsKQSVQTR--HLSGGMQRKLSVA 951
Cdd:NF040905 82 iIHQELALIPY-------LSIAENI-FLGNERAKRGVIDWNETNRrareLLAKVGL--DESPDTLvtDIGVGKQQLVEIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768000599 952 IAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAqGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
801-1016 |
4.97e-11 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 67.47 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 801 PGLSPGVSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAI 879
Cdd:COG4618 325 PRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 880 RPHLGVCPQYNVLFD---------MLTVD-EHVWFYGRLKGLSAAVVGPEQ--DRLLQDVGLVskqsvqtrhLSGG-MQR 946
Cdd:COG4618 405 GRHIGYLPQDVELFDgtiaeniarFGDADpEKVVAAAKLAGVHEMILRLPDgyDTRIGEGGAR---------LSGGqRQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768000599 947 kLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE-GRTLILSTHH---LDEAellgDRVAVVAGGRL 1016
Cdd:COG4618 476 -IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRpslLAAV----DKLLVLRDGRV 544
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
810-1015 |
5.78e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 810 RSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPpSG---GSAFILGHDVRSS---------MA 877
Cdd:PRK13549 9 KNITKTFGGVK--ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP-HGtyeGEIIFEGEELQASnirdteragIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 878 AIRPHLGVCPQynvlfdmLTVDEHVwFYGR--LKG--LSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIA 953
Cdd:PRK13549 86 IIHQELALVKE-------LSVLENI-FLGNeiTPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768000599 954 FVGGSQVVILDEPTAGVDPASRRGIWELL--LKyREGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIrdLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
550-750 |
7.34e-11 |
|
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: 65.87 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 550 LPLFLTLAWIYSVTLTVKAVVREKETRLRDTMRAMGLSRAVLWLGWFLScLGPFLLSAALLVLVLKLGDILPYSHPGVVF 629
Cdd:pfam12698 164 VGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILG-DFLVGLLQLLIILLLLFGIGIPFGNLGLLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 630 LFLAAFAVATVTQSFLLSAFFSR---ANLAAACGGLAYFSLYLPYVLcvawRDRLPAGGRVAASLLSPVAFGFGCESLAL 706
Cdd:pfam12698 243 LLFLLYGLAYIALGYLLGSLFKNsedAQSIIGIVILLLSGFFGGLFP----LEDPPSFLQWIFSIIPFFSPIDGLLRLIY 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 768000599 707 leeqgegaqwhnvgtrpTADVFSLAQVSGLLLLDAALYGLATWY 750
Cdd:pfam12698 319 -----------------GDSLWEIAPSLIILLLFAVVLLLLALL 345
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
817-1015 |
1.18e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 62.87 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 817 PGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHdvrssmaairphLGVCPQY------- 889
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEpwiqngt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 890 ---NVLFDMlTVDEHvwFYgrLKGLSAAVvgpeqdrLLQDVGLVSKQSvQTR------HLSGGMQRKLSVAIAFVGGSQV 960
Cdd:cd03250 82 ireNILFGK-PFDEE--RY--EKVIKACA-------LEPDLEILPDGD-LTEigekgiNLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599 961 VILDEPTAGVDPASRRGIWELLL--KYREGRTLILSTHHLdeaELLG--DRVAVVAGGR 1015
Cdd:cd03250 149 YLLDDPLSAVDAHVGRHIFENCIlgLLLNNKTRILVTHQL---QLLPhaDQIVVLDNGR 204
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
804-1016 |
1.23e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.35 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 804 SPGVSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPP-SG----GSAFILGHDVRS--SM 876
Cdd:PRK14271 19 APAMAAVNLTLGFAG--KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvSGyrysGDVLLGGRSIFNyrDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 877 AAIRPHLGVCPQYNVLFDMLTVDEhvwfygRLKGLSAAVVGPEQD------RLLQDVGL----VSKQSVQTRHLSGGMQR 946
Cdd:PRK14271 97 LEFRRRVGMLFQRPNPFPMSIMDN------VLAGVRAHKLVPRKEfrgvaqARLTEVGLwdavKDRLSDSPFRLSGGQQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 947 KLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
806-1011 |
1.36e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 806 GVSVRSLEKRFpgspqpaLRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFIlghDVrssmaairphlgv 885
Cdd:COG2401 35 GVELRVVERYV-------LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV---DV------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 cpQYNVLFDMLTVDEHVwfyGRLKGLSAAVvgpeqdRLLQDVGLVSKQSVQTR--HLSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:COG2401 92 --PDNQFGREASLIDAI---GRKGDFKDAV------ELLNAVGLSDAVLWLRRfkELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768000599 964 DEPTAGVDPA-SRRG--IWELLLKyREGRTLILSTHHLD-EAELLGDRVAVV 1011
Cdd:COG2401 161 DEFCSHLDRQtAKRVarNLQKLAR-RAGITLVVATHHYDvIDDLQPDLLIFV 211
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
819-1050 |
2.23e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.79 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 819 SPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPP----SGGSAFILGHDVrsSMAAIR-PHLGVCPQ----- 888
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPV--APCALRgRKIATIMQnprsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 889 YNVLFDMLTvdehvwfYGRLKGLSAAVVGPEQDRL--LQDVGLVSKQSVQTRH---LSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:PRK10418 92 FNPLHTMHT-------HARETCLALGKPADDATLTaaLEAVGLENAARVLKLYpfeMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 964 DEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKAR 1041
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAH 244
|
....*....
gi 768000599 1042 LPLTTNEKA 1050
Cdd:PRK10418 245 LALYGMELA 253
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
817-996 |
9.60e-10 |
|
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: 59.95 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 817 PGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPS--GGSAFILGHDVRSSmaaIRPHLGVCPQYNVLFD 894
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKN---FQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 895 MLTVDEHVWFYGRLKGLSAAvvgpeqdrllqdvglvskqsvqtrhlsggmQRK-LSVAIAFVGGSQVVILDEPTAGVDPA 973
Cdd:cd03232 93 NLTVREALRFSALLRGLSVE------------------------------QRKrLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180
....*....|....*....|....
gi 768000599 974 SRRGIWELLLKY-REGRTLILSTH 996
Cdd:cd03232 143 AAYNIVRFLKKLaDSGQAILCTIH 166
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
807-1015 |
1.28e-09 |
|
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: 62.53 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFIL--GHDVRSS--------- 875
Cdd:TIGR02633 2 LEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYwsGSPLKASnirdterag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 876 MAAIRPHLGVCPQYNVLFDMLTVDEhVWFYGRLKGLSAAVVGPEQdrLLQDVGL-VSKQSVQTRHLSGGMQRKLSVAIAF 954
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNE-ITLPGGRMAYNAMYLRAKN--LLRELQLdADNVTRPVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 955 VGGSQVVILDEPTAGVDPASRRGIWELL--LKyREGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIrdLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
825-1025 |
1.61e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.58 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 825 RGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILG---HDVRSSMAAIrphlGVCPQYNVLFDMLTVDEH 901
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmNDVPPAERGV----GMVFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 902 VWFYGRLKGLSAAVVGPEQD---RLLQDVGLVSKQSvqtRHLSGGmQRKlSVAIA--FVGGSQVVILDEPTAGVDPASR- 975
Cdd:PRK11000 96 MSFGLKLAGAKKEEINQRVNqvaEVLQLAHLLDRKP---KALSGG-QRQ-RVAIGrtLVAEPSVFLLDEPLSNLDAALRv 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768000599 976 --RgIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFL 1025
Cdd:PRK11000 171 qmR-IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
825-1016 |
2.38e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 825 RGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV--RSSMAAIRPHLGVCPQY---NVLFDMLTVD 899
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESrrdNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 900 EHVWFY-----GRLKGLSAAV-------VGPEQDRLLQDVGLVSKQSVQtrHLSGGMQRKLSVAIAFVGGSQVVILDEPT 967
Cdd:PRK09700 360 QNMAISrslkdGGYKGAMGLFhevdeqrTAENQRELLALKCHSVNQNIT--ELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 768000599 968 AGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
812-997 |
3.47e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 812 LEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNV 891
Cdd:PRK13540 5 IELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 892 LFDMLTVDEHVWFygrlkGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVD 971
Cdd:PRK13540 85 INPYLTLRENCLY-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180
....*....|....*....|....*..
gi 768000599 972 PASRRGIWELLLKYR-EGRTLILSTHH 997
Cdd:PRK13540 160 ELSLLTIITKIQEHRaKGGAVLLTSHQ 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
817-1016 |
3.98e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 817 PGSPQPAlrglSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGH--DVRSSMAAIRPHLGVCPQ---YNV 891
Cdd:PRK11288 266 PGLREPI----SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPEdrkAEG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 892 LFDMLTVDEHVWFYGRLKGLSAA-VVGPEQDRLLQDVgLVSKQSVQTRH-------LSGGMQRKLSVAIAFVGGSQVVIL 963
Cdd:PRK11288 342 IIPVHSVADNINISARRHHLRAGcLINNRWEAENADR-FIRSLNIKTPSreqlimnLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 964 DEPTAGVDPASRRGIWELLLKYRE-GRTLILSTHHLdeAELLG--DRVAVVAGGRL 1016
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAqGVAVLFVSSDL--PEVLGvaDRIVVMREGRI 474
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
801-1014 |
5.44e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 801 PGLSPGVSVRSLEKRF----PGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFilghDVRSSM 876
Cdd:PLN03232 606 PPLQPGAPAISIKNGYfswdSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSV----VIRGSV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 877 AAIrphlgvcPQYNVLFDMlTVDEHVWF--------YGRlkGLSAAVVGPEQDRLL-QDVGLVSKQSVqtrHLSGGMQRK 947
Cdd:PLN03232 682 AYV-------PQVSWIFNA-TVRENILFgsdfeserYWR--AIDVTALQHDLDLLPgRDLTEIGERGV---NISGGQKQR 748
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 948 LSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELLgDRVAVVAGG 1014
Cdd:PLN03232 749 VSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDElKGKTRVLVTNQLHFLPLM-DRIILVSEG 815
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
792-1015 |
5.87e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 60.47 E-value: 5.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 792 PKVLVEEAPPGLSPGVSVRSLEKRFPG---------SPQPALRGLSLDFYQGHITAFLGHNGAGKTTT-LSILsGLFpPS 861
Cdd:COG4172 261 PRGDPRPVPPDAPPLLEARDLKVWFPIkrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RLI-PS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 862 GGSAFILGHDV----RSSMAAIRPHLGVCPQ--YNVLFDMLTVDEHVwfygrLKGLsaAVVGPEQDR---------LLQD 926
Cdd:COG4172 339 EGEIRFDGQDLdglsRRALRPLRRRMQVVFQdpFGSLSPRMTVGQII-----AEGL--RVHGPGLSAaerrarvaeALEE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 927 VGLvskqSVQTRH-----LSGGmQR-KLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHL 998
Cdd:COG4172 412 VGL----DPAARHrypheFSGG-QRqRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLrdLQREHGLAYLFISHDL 486
|
250
....*....|....*..
gi 768000599 999 DEAELLGDRVAVVAGGR 1015
Cdd:COG4172 487 AVVRALAHRVMVMKDGK 503
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
798-1016 |
6.42e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.54 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 798 EAPPGLSPG--VSVRSLEKRFPGspQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGsAFILGhdvRSS 875
Cdd:PRK11247 2 MNTARLNQGtpLLLNAVSKRYGE--RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-ELLAG---TAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 876 MAAIRPHLGVCPQYNVLFDMLTVDEHVWFygrlkGLSAAVvGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFV 955
Cdd:PRK11247 76 LAEAREDTRLMFQDARLLPWKKVIDNVGL-----GLKGQW-RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 956 GGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIesLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
819-1021 |
1.14e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.86 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 819 SPQ--PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGlFPPSGGSAFILGHDVRS-SMAAIRPHL---GVCPQY--- 889
Cdd:PRK11174 359 SPDgkTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRElDPESWRKHLswvGQNPQLphg 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 890 ----NVLF-DMLTVDEHVWfygrlKGLSAAVVGPEQDRLLQdvGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:PRK11174 438 tlrdNVLLgNPDASDEQLQ-----QALENAWVSEFLPLLPQ--GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 768000599 965 EPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLgDRVAVVAGGRLCCCGS 1021
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGD 566
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
813-1004 |
1.52e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 55.44 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 813 EKRFPgspqPALRGLSLDFYQGHITAFLGHNGAGKTTTL-SIlsglfppsggsAFILGHDvrssMAAIRPHLGVCPQYNV 891
Cdd:cd03227 4 LGRFP----SYFVPNDVTFGEGSLTIITGPNGSGKSTILdAI-----------GLALGGA----QSATRRRSGVKAGCIV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 892 lfdmltvdehvwfygrlkglsaavvgpeqdrllqdvGLVSKQSVQTRH-LSGGMQRKLSVAIAF----VGGSQVVILDEP 966
Cdd:cd03227 65 ------------------------------------AAVSAELIFTRLqLSGGEKELSALALILalasLKPRPLYILDEI 108
|
170 180 190
....*....|....*....|....*....|....*....
gi 768000599 967 TAGVDPASRRGIWELLLKYR-EGRTLILSTHHLDEAELL 1004
Cdd:cd03227 109 DRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELA 147
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
834-997 |
2.34e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.74 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 834 GHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDvRSSMAAIRPHLGVCPQYNVLFDMLTVDEHVWFYGRL---KG 910
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLrlpKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 911 LSAAVVGPEQDRLLQDVGLVSKQSVQT-----RHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDP-ASRRGIWELLLK 984
Cdd:PLN03211 173 LTKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAtAAYRLVLTLGSL 252
|
170
....*....|...
gi 768000599 985 YREGRTLILSTHH 997
Cdd:PLN03211 253 AQKGKTIVTSMHQ 265
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
814-1015 |
2.97e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.20 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 814 KRFPGSPqpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV--RSSMAAIRPHLGVCPQYNV 891
Cdd:PRK10982 6 KSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 892 LFDMLTVDEHVWFyGR--LKGLSAavvgpEQDRLLQ---------DVGLVSKQSVQTrhLSGGMQRKLSVAIAFVGGSQV 960
Cdd:PRK10982 84 LVLQRSVMDNMWL-GRypTKGMFV-----DQDKMYRdtkaifdelDIDIDPRAKVAT--LSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 961 VILDEPTAGVDPASRRGIWELLLKYRE-GRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKErGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
808-1016 |
5.76e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 57.39 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 808 SVRSLEKRF--PGSPQPALRGLSLDFYQGHITAFLGHNGAGKT-TTLSILsGLFPPS----GGSAFILGHDV----RSSM 876
Cdd:COG4172 8 SVEDLSVAFgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPaahpSGSILFDGQDLlglsEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 877 AAIR----------------PHLGVCPQynvLFDMLTVdeHvwfygrlKGLSAAVVGPEQDRLLQDVGLvskQSVQTR-- 938
Cdd:COG4172 87 RRIRgnriamifqepmtslnPLHTIGKQ---IAEVLRL--H-------RGLSGAAARARALELLERVGI---PDPERRld 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 939 ---H-LSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVA 1012
Cdd:COG4172 152 aypHqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLkdLQRELGMALLLITHDLGVVRRFADRVAVMR 231
|
....
gi 768000599 1013 GGRL 1016
Cdd:COG4172 232 QGEI 235
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
823-1014 |
9.24e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.18 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGH-----DVRSSMAAIR-----PHLGVCPQYNV- 891
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSYRSQRIRmifqdPSTSLNPRQRIs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 892 -LFDMltvdehvwfygRLKgLSAAVVGPEQDR----LLQDVGLVSKQSVQTRH-LSGGMQRKLSVAIAFVGGSQVVILDE 965
Cdd:PRK15112 108 qILDF-----------PLR-LNTDLEPEQREKqiieTLRQVGLLPDHASYYPHmLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768000599 966 PTAGVDPASRRGIWELLLKYRE--GRTLILSTHHLDEAELLGDRVAVVAGG 1014
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
815-998 |
1.17e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.64 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 815 RFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSafILGHDVRSS---MAAIRPHLGVCPQYNV 891
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD--IRFHDIPLTklqLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 892 LFDMlTVDEHVWFyGRLKGLSAAVvgpEQDRLLQDVG---LVSKQSVQTR------HLSGGMQRKLSVAIAFVGGSQVVI 962
Cdd:PRK10789 400 LFSD-TVANNIAL-GRPDATQQEI---EHVARLASVHddiLRLPQGYDTEvgergvMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190
....*....|....*....|....*....|....*.
gi 768000599 963 LDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHL 998
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRL 510
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
778-1016 |
1.49e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 778 RPPKSPAPCPTPLDPKVLVEEAPPGlSPGVSVRSLEKRFP---------GSPQPALRGLSLDFYQGHITAFLGHNGAGKT 848
Cdd:PRK10261 286 RFPLISLEHPAKQEPPIEQDTVVDG-EPILQVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKS 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 849 TTLSILSGLFPPSGGSAFILGHDVR----SSMAAIR---------PHLGVCPQYNVLFDMLtvdEHVWFYGRLKGLSAAv 915
Cdd:PRK10261 365 TTGRALLRLVESQGGEIIFNGQRIDtlspGKLQALRrdiqfifqdPYASLDPRQTVGDSIM---EPLRVHGLLPGKAAA- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 916 vgPEQDRLLQDVGLVSKQSVQTRH-LSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYRE--GRTLI 992
Cdd:PRK10261 441 --ARVAWLLERVGLLPEHAWRYPHeFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYL 518
|
250 260
....*....|....*....|....
gi 768000599 993 LSTHHLDEAELLGDRVAVVAGGRL 1016
Cdd:PRK10261 519 FISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
829-972 |
1.79e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 829 LDFYQGHITAFL--GHNGAGKTTTLSILSGLFPPSGGSAFILGHDV----RSSMAAIRPHLGVCPQynvlfDMLTVdEHV 902
Cdd:PRK13543 30 LDFHVDAGEALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtrgdRSRFMAYLGHLPGLKA-----DLSTL-ENL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 903 WFYGRLKGLSAAVVgpeQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDP 972
Cdd:PRK13543 104 HFLCGLHGRRAKQM---PGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
822-1015 |
2.09e-07 |
|
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: 53.59 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPH---------LGVCPQY-NV 891
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPReilalrrrtIGYVSQFlRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 892 ------------------------------LFDMLTVDEHVWfygrlkGLSAAVvgpeqdrllqdvglvskqsvqtrhLS 941
Cdd:COG4778 105 iprvsaldvvaepllergvdreeararareLLARLNLPERLW------DLPPAT------------------------FS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768000599 942 GGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKY-REGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
817-1034 |
2.32e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 817 PGSPqPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIRPHLGVCPQYNVLFD- 894
Cdd:PLN03232 1246 PGLP-PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVaKFGLTDLRRVLSIIPQSPVLFSg 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 895 --MLTVD---EH----VWfygrlKGLSAAVVGPEQDRllQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDE 965
Cdd:PLN03232 1325 tvRFNIDpfsEHndadLW-----EALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599 966 PTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAeLLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYY 1034
Cdd:PLN03232 1398 ATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFF 1465
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
833-1016 |
2.67e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 833 QGHITAFLGHNGAGKTTTLSILSGLFP-PSGGSAFILGH--DVRSSMAAIRPHLGVCP----QYNVLFDM-------LTV 898
Cdd:PRK13549 287 RGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPedrkRDGIVPVMgvgknitLAA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 899 DEHVWFYGRL-KGLSAAVVGPEQDRLlqdvglvskqSVQTRH-------LSGGMQRKLSVAIAFVGGSQVVILDEPTAGV 970
Cdd:PRK13549 367 LDRFTGGSRIdDAAELKTILESIQRL----------KVKTASpelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768000599 971 DPASRRGIWELLLKY-REGRTLILSTHHLdeAELLG--DRVAVVAGGRL 1016
Cdd:PRK13549 437 DVGAKYEIYKLINQLvQQGVAIIVISSEL--PEVLGlsDRVLVMHEGKL 483
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
824-1028 |
3.20e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.58 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAfilghdvrssmaaIRPH---LGVCPQyNVLFDM---LT 897
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGklrIGYVPQ-KLYLDTtlpLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 898 VDEhvwfYGRLK-GLSAAVVGPEQDRLlqDVGLVSKQSVQTrhLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRR 976
Cdd:PRK09544 86 VNR----FLRLRpGTKKEDILPALKRV--QAGHLIDAPMQK--LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 768000599 977 GIWELLLKYRE--GRTLILSTHHLDEAELLGDRVaVVAGGRLCCCGSPLFLRRH 1028
Cdd:PRK09544 158 ALYDLIDQLRRelDCAVLMVSHDLHLVMAKTDEV-LCLNHHICCSGTPEVVSLH 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
810-1016 |
4.00e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 810 RSLEKRFP---GSP--------------QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV 872
Cdd:PRK10982 233 RSLTQRFPdkeNKPgevilevrnltslrQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 873 --RSSMAAI----------RPHLGVCPQYNVLFDML--TVDEHVWFYG-----RLKGLSAAVVgpeqdrllqDVGLVSKQ 933
Cdd:PRK10982 313 nnHNANEAInhgfalvteeRRSTGIYAYLDIGFNSLisNIRNYKNKVGlldnsRMKSDTQWVI---------DSMRVKTP 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 934 SVQTR--HLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKY-REGRTLILSTHHLdeAELLG--DRV 1008
Cdd:PRK10982 384 GHRTQigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEM--PELLGitDRI 461
|
....*...
gi 768000599 1009 AVVAGGRL 1016
Cdd:PRK10982 462 LVMSNGLV 469
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
822-974 |
5.42e-07 |
|
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: 51.88 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFIL---GHDVRSSMAAIRPHLGVCPQYNVLFDMLTV 898
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIhynGIPYKEFAEKYPGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768000599 899 DEHVWFYGRLKGlsaavvgpeqdrllqdvglvsKQSVqtRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPAS 974
Cdd:cd03233 101 RETLDFALRCKG---------------------NEFV--RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
807-1021 |
6.42e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQ--PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSA--------------FILGH 870
Cdd:PRK10261 13 LAVENLNIAFMQEQQkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 871 DVRSSMAAIR-PHLGVCPQ--YNVLFDMLTVDEHVWFYGRL-KGLSAAVVGPEQDRLLQDVGLVSKQSVQTRH---LSGG 943
Cdd:PRK10261 93 QSAAQMRHVRgADMAMIFQepMTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTILSRYphqLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 944 MQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGS 1021
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
823-1015 |
7.64e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.19 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 823 ALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSG---GSAFILGHDV--------------------RSSMAAI 879
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREIlnlpekelnklraeqismifQDPMTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 880 RPHLGVCPQY-NVLfdMLtvdeHvwfygrlKGLSAAVVGPEQDRLLQDVGL--VSKQSVQTRH-LSGGMQRKLSVAIAFV 955
Cdd:PRK09473 111 NPYMRVGEQLmEVL--ML----H-------KGMSKAEAFEESVRMLDAVKMpeARKRMKMYPHeFSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768000599 956 GGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
821-1000 |
8.75e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.64 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 821 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMlTVD 899
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLFGD-TVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 900 EHVWFYGRLKGLSaavvgPEQDRLLQDV---GL---VSKQSVQTrhLSGGMQRKLSVA--IAFVggSQVVILDEPTAGVD 971
Cdd:PRK10247 99 DNLIFPWQIRNQQ-----PDPAIFLDDLerfALpdtILTKNIAE--LSGGEKQRISLIrnLQFM--PKVLLLDEITSALD 169
|
170 180 190
....*....|....*....|....*....|.
gi 768000599 972 PASRRGIWELLLKY-REGRTLIL-STHHLDE 1000
Cdd:PRK10247 170 ESNKHNVNEIIHRYvREQNIAVLwVTHDKDE 200
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
824-971 |
2.16e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.93 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGlfPPSGGsaFILGhDVRSS--------MAAIRphlGVCPQYNVLFDM 895
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEG-DIRISgfpkkqetFARIS---GYCEQNDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 896 LTVDEHVWFYGRLKgLSAAVVGPEQ----DRLLQDVGLVS-KQSV----QTRHLSGGMQRKLSVAIAFVGGSQVVILDEP 966
Cdd:PLN03140 968 VTVRESLIYSAFLR-LPKEVSKEEKmmfvDEVMELVELDNlKDAIvglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
....*
gi 768000599 967 TAGVD 971
Cdd:PLN03140 1047 TSGLD 1051
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
791-1014 |
2.35e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 791 DPKVLVEEAPPGLSpgvsVRSLEKRFPG---------SPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPS 861
Cdd:PRK15134 264 DPVPLPEPASPLLD----VEQLQVAFPIrkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 862 GGSAF---ILGHDVRSSMAAIRPHLGVCPQ--YNVLFDMLTVDEHVWFYGRL--KGLSAAVVGPEQDRLLQDVGLvskqS 934
Cdd:PRK15134 340 GEIWFdgqPLHNLNRRQLLPVRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGL----D 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 935 VQTRH-----LSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTL--ILSTHHLDEAELLGDR 1007
Cdd:PRK15134 416 PETRHrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQ 495
|
....*..
gi 768000599 1008 VAVVAGG 1014
Cdd:PRK15134 496 VIVLRQG 502
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
839-1017 |
2.65e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 839 FL-GHNGAGKTTTLSILSGLFPPSGGSAFILGHDVrssmAAIRPHlgvcpQYNVLFDMLTVDehVWFYGRLKGLSAAVVG 917
Cdd:PRK10522 353 FLiGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV----TAEQPE-----DYRKLFSAVFTD--FHLFDQLLGPEGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 918 PEQ-DRLLQDVGLVSKQSVQ-----TRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKY-RE-GR 989
Cdd:PRK10522 422 PALvEKWLERLKMAHKLELEdgrisNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLlQEmGK 501
|
170 180
....*....|....*....|....*...
gi 768000599 990 TLILSTHHlDEAELLGDRVAVVAGGRLC 1017
Cdd:PRK10522 502 TIFAISHD-DHYFIHADRLLEMRNGQLS 528
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
938-996 |
2.86e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 51.24 E-value: 2.86e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 938 RHLSGGMQRKLSVAIAF---VGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRT-LILSTH 996
Cdd:pfam13304 235 FELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
819-996 |
3.09e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 819 SPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFIlgHDVRSSMAAiRPHLG-VCPQYNVLFDMlT 897
Cdd:PRK13541 11 IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIA-KPYCTyIGHNLGLKLEM-T 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 898 VDEHVWFYGRLKGLSAAVVGPEQDRLLQDvgLVSKQSVQtrhLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRG 977
Cdd:PRK13541 87 VFENLKFWSEIYNSAETLYAAIHYFKLHD--LLDEKCYS---LSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
170 180
....*....|....*....|
gi 768000599 978 IWELL-LKYREGRTLILSTH 996
Cdd:PRK13541 162 LNNLIvMKANSGGIVLLSSH 181
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
834-1004 |
3.15e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 834 GHITAFLGHNGAGKTTTLSILSGLFPP---SGGSAFILGHDVRSSMAAIrphLGVCPQYNVLFDMLTVDEHVWFYGRLKg 910
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQRS---IGYVQQQDLHLPTSTVRESLRFSAYLR- 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 911 LSAAVVGPEQDRLLQDV-GLVSKQS-------VQTRHLSGGMQRKLSVAIAFVGGSQVVI-LDEPTAGVDPASRRGIWEL 981
Cdd:TIGR00956 865 QPKSVSKSEKMEYVEEViKLLEMESyadavvgVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKL 944
|
170 180
....*....|....*....|...
gi 768000599 982 LLKYREGRTLILSTHHLDEAELL 1004
Cdd:TIGR00956 945 MRKLADHGQAILCTIHQPSAILF 967
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
830-997 |
3.75e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.53 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 830 DFYQGhITAFLGHNGAGKTTTLS----ILSGLFPPSGGSAFILGHDVR--SSMAAIRPHLGVCP--QYNVL--FDMLtvd 899
Cdd:cd03240 19 EFFSP-LTLIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLIRegEVRAQVKLAFENANgkKYTITrsLAIL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 900 ehvwfygrlkgLSAAVVGPEQDR--LLQDVGLvskqsvqtrhLSGGMQRKLSVAI------AFVGGSQVVILDEPTAGVD 971
Cdd:cd03240 95 -----------ENVIFCHQGESNwpLLDMRGR----------CSGGEKVLASLIIrlalaeTFGSNCGILALDEPTTNLD 153
|
170 180
....*....|....*....|....*....
gi 768000599 972 PASRRGIWELLLKYREG---RTLILSTHH 997
Cdd:cd03240 154 EENIEESLAEIIEERKSqknFQLIVITHD 182
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
776-999 |
1.22e-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: 50.29 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 776 GPRPPKSPAPCPTP----LDPKVLVEEAPPGLSpgVSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTL 851
Cdd:TIGR01271 1185 EPRPSGGGGKYQLStvlvIENPHAQKCWPSGGQ--MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLL 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 852 SILSGLFPpSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFD----------MLTVDEHVWFYGRLKGLSAAVvgpEQ 920
Cdd:TIGR01271 1263 SALLRLLS-TEGEIQIDGVSWNSvTLQTWRKAFGVIPQKVFIFSgtfrknldpyEQWSDEEIWKVAEEVGLKSVI---EQ 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 921 -----DRLLQDVGLVskqsvqtrhLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILST 995
Cdd:TIGR01271 1339 fpdklDFVLVDGGYV---------LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSE 1409
|
....
gi 768000599 996 HHLD 999
Cdd:TIGR01271 1410 HRVE 1413
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
800-971 |
1.48e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 800 PPG--LSPGVSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRS-SM 876
Cdd:PLN03130 1229 PPGwpSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGL 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 877 AAIRPHLGVCPQYNVLF------DMLTVDEH----VWfygrlKGLSAAvvgpeqdrLLQDV------GLVSKQSVQTRHL 940
Cdd:PLN03130 1309 MDLRKVLGIIPQAPVLFsgtvrfNLDPFNEHndadLW-----ESLERA--------HLKDVirrnslGLDAEVSEAGENF 1375
|
170 180 190
....*....|....*....|....*....|.
gi 768000599 941 SGGMQRKLSVAIAFVGGSQVVILDEPTAGVD 971
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
833-1003 |
2.23e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.21 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 833 QGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFIlghdvrssmaairphlgvcpqynvlfdmltvdehvwfygrlkgls 912
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 913 aaVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL-------LKY 985
Cdd:smart00382 36 --IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLKS 113
|
170 180
....*....|....*....|.
gi 768000599 986 REGRTLILSTHH---LDEAEL 1003
Cdd:smart00382 114 EKNLTVILTTNDekdLGPALL 134
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
822-1002 |
2.40e-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: 49.52 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 822 PALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSafiLGHDVRSSMaairphlgvCPQY----------NV 891
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK---IKHSGRISF---------SPQTswimpgtikdNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 892 LFDmLTVDEHvwfygRLKGLSAA-------VVGPEQDRLLQDVGLVSkqsvqtrhLSGGMQRKLSVAIAFVGGSQVVILD 964
Cdd:TIGR01271 508 IFG-LSYDEY-----RYTSVIKAcqleediALFPEKDKTVLGEGGIT--------LSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768000599 965 EPTAGVDPASRRGIWE-LLLKYREGRTLILST---HHLDEAE 1002
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFEsCLCKLMSNKTRILVTsklEHLKKAD 615
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
824-1022 |
3.47e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.51 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAfilGHDVRSS-------MAAIRPH-----LGVCPQYNV 891
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPR---GARVTGDvtlngepLAAIDAPrlarlRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 892 LFDMLTVDEHVwFYGRLKGLSAAVVGPEQDRLLQDVGL-------VSKQSVQTrhLSGGMQRKLSVAIAF---------V 955
Cdd:PRK13547 94 PAFAFSAREIV-LLGRYPHARRAGALTHRDGEIAWQALalagataLVGRDVTT--LSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768000599 956 GGSQVVILDEPTAGVDPASRRGIWELLLKY-REGRTLILS-THHLDEAELLGDRVAVVAGGRLCCCGSP 1022
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAiVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
816-1002 |
4.25e-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: 47.16 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 816 FPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGsafILGHDVRSSMaairphlgvCPQY------ 889
Cdd:cd03291 45 LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG---KIKHSGRISF---------SSQFswimpg 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 890 ----NVLFDmLTVDEHvwfygRLKGLSAA-------VVGPEQDRLLQDVGLVSkqsvqtrhLSGGMQRKLSVAIAFVGGS 958
Cdd:cd03291 113 tikeNIIFG-VSYDEY-----RYKSVVKAcqleediTKFPEKDNTVLGEGGIT--------LSGGQRARISLARAVYKDA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768000599 959 QVVILDEPTAGVDPASRRGIWE-LLLKYREGRTLILST---HHLDEAE 1002
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKEIFEsCVCKLMANKTRILVTskmEHLKKAD 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
923-1016 |
5.39e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 923 LLQDVGL---VSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHH 997
Cdd:PRK11022 134 LLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLleLQQKENMALVLITHD 213
|
90
....*....|....*....
gi 768000599 998 LDEAELLGDRVAVVAGGRL 1016
Cdd:PRK11022 214 LALVAEAAHKIIVMYAGQV 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
807-999 |
1.06e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.00 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 807 VSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPpSGGSAFILGHDVRS-SMAAIRPHLGV 885
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQYNVLFDMLT----------VDEHVWFYGRLKGLSAAVVG-PEQ-DRLLQDVGLVskqsvqtrhLSGGMQRKLSVAIA 953
Cdd:cd03289 82 IPQKVFIFSGTFrknldpygkwSDEEIWKVAEEVGLKSVIEQfPGQlDFVLVDGGCV---------LSHGHKQLMCLARS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 768000599 954 FVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLD 999
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
814-1000 |
1.79e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 814 KRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAfilghDVRSSMAAIRPHLGVCPQynvlf 893
Cdd:PRK13545 30 RSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSGLNGQ----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 894 dmLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQ--DVGLVSKQSVQTrhLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVD 971
Cdd:PRK13545 100 --LTGIENIELKGLMMGLTKEKIKEIIPEIIEfaDIGKFIYQPVKT--YSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190
....*....|....*....|....*....|
gi 768000599 972 PASRRGIWELLLKYRE-GRTLILSTHHLDE 1000
Cdd:PRK13545 176 QTFTKKCLDKMNEFKEqGKTIFFISHSLSQ 205
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
824-997 |
2.82e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 43.30 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFYQG---HITaflGHNGAGKTTTLSILSGLFPPSGGsafilghdvrssmaairpHLGVCPQYNVLFdmltVDE 900
Cdd:cd03223 17 LKDLSFEIKPGdrlLIT---GPSGTGKSSLFRALAGLWPWGSG------------------RIGMPEGEDLLF----LPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 901 HVWFY-GRLKglsAAVVGPEQDRLlqdvglvskqsvqtrhlSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIW 979
Cdd:cd03223 72 RPYLPlGTLR---EQLIYPWDDVL-----------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....*...
gi 768000599 980 ELLLKyrEGRTLILSTHH 997
Cdd:cd03223 132 QLLKE--LGITVISVGHR 147
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
821-1001 |
4.15e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 821 QPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSS---MAAIRPHLGV------------ 885
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRGSgetIWDIKKHIGYvssslhldyrvs 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 886 CPQYNVL----FDMLtvdehvwfygrlkGLSAAVvgPEQDRLLQD-----VGLVSKQSVQTRH-LSGGMQRKLSVAIAFV 955
Cdd:PRK10938 353 TSVRNVIlsgfFDSI-------------GIYQAV--SDRQQKLAQqwldiLGIDKRTADAPFHsLSWGQQRLALIVRALV 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 768000599 956 GGSQVVILDEPTAGVDPASR---RGIWELLLkyREGRT-LILSTHHLDEA 1001
Cdd:PRK10938 418 KHPTLLILDEPLQGLDPLNRqlvRRFVDVLI--SEGETqLLFVSHHAEDA 465
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
818-998 |
4.29e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 43.47 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 818 GSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTL-SILSGLFPPSG----GSAFILGHDVRSSMAAIRPHLGVCPQYNVL 892
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwSNKNESEPSFEATRSRNRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 893 FDMlTVDEHVWFYG-----RLKGLS-AAVVGPEQDRL-LQDVGLVSKQSVqtrHLSGGMQRKLSVAIAFVGGSQVVILDE 965
Cdd:cd03290 91 LNA-TVEENITFGSpfnkqRYKAVTdACSLQPDIDLLpFGDQTEIGERGI---NLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 768000599 966 PTAGV-----DPASRRGIWELLLKyrEGRTLILSTHHL 998
Cdd:cd03290 167 PFSALdihlsDHLMQEGILKFLQD--DKRTLVLVTHKL 202
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
921-1041 |
4.60e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 921 DRL--LQDVGL----VSKQSvqtRHLSGG-MQRklsVAIAFVGGSQVV----ILDEPTAGVDPASRRGIWELLLKYRE-G 988
Cdd:TIGR00630 467 ERLgfLIDVGLdylsLSRAA---GTLSGGeAQR---IRLATQIGSGLTgvlyVLDEPSIGLHQRDNRRLINTLKRLRDlG 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 989 RTLILSTHHlDEAELLGDRV------AVVAGGRLCCCGSP------------LFLR----------RHLGSGYYLTLVKA 1040
Cdd:TIGR00630 541 NTLIVVEHD-EDTIRAADYVidigpgAGEHGGEVVASGTPeeilanpdsltgQYLSgrkkievpaeRRPGNGKFLTLKGA 619
|
.
gi 768000599 1041 R 1041
Cdd:TIGR00630 620 R 620
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
824-996 |
4.95e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.22 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 824 LRGLSLDFyQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAF------------------------ILG---------- 869
Cdd:COG3593 14 IKDLSIEL-SDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFdeedfylgddpdlpeieieltfgsLLSrllrlllkee 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 870 --HDVRSSMAAIRPHLGvcpqyNVLFDMLT-VDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLV--SKQSVQTRHLSGGM 944
Cdd:COG3593 93 dkEELEEALEELNEELK-----EALKALNElLSEYLKELLDGLDLELELSLDELEDLLKSLSLRieDGKELPLDRLGSGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 945 QRKLSVAIAFV-------GGSQVVILDEPTAGVDPASRRGIWELLLKYREGRT-LILSTH 996
Cdd:COG3593 168 QRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNqVIITTH 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
940-1015 |
5.91e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.31 E-value: 5.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768000599 940 LSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELL--LKYREGRTLILSTHHLDEAELLGDRVAVVAGGR 1015
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
777-1027 |
6.41e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.77 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 777 PRPPKSPAPcpTPLDPKVLVEEappglspGVSVRSLEkrfpGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSG 856
Cdd:PTZ00243 1293 PASPTSAAP--HPVQAGSLVFE-------GVQMRYRE----GLPL-VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMR 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 857 LFPPSGGSAFILGHDVRS-SMAAIRPHLGVCPQYNVLFDMlTVDEHVWFYgrLKGLSAAVVgpeqdRLLQDVGL---VSK 932
Cdd:PTZ00243 1359 MVEVCGGEIRVNGREIGAyGLRELRRQFSMIPQDPVLFDG-TVRQNVDPF--LEASSAEVW-----AALELVGLrerVAS 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 933 QS--VQTRHLSGGM-----QRKL-SVAIAFVG-GSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAEL 1003
Cdd:PTZ00243 1431 ESegIDSRVLEGGSnysvgQRQLmCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQ 1510
|
250 260
....*....|....*....|....*.
gi 768000599 1004 LgDRVAVVAGGRLCCCGSP--LFLRR 1027
Cdd:PTZ00243 1511 Y-DKIIVMDHGAVAEMGSPreLVMNR 1535
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
828-1012 |
8.16e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 828 SLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGG---SAFilGHDVRSSMAAIRPHLGVCPQYNVLfDMLTVDEHVwf 904
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqSQF--SHITRLSFEQLQKLVSDEWQRNNT-DMLSPGEDD-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 905 ygrlKGLSAAVVGPEQ-------DRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRG 977
Cdd:PRK10938 98 ----TGRTTAEIIQDEvkdparcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 768000599 978 IWELLLK-YREGRTLILSTHHLDEAELLGDRVAVVA 1012
Cdd:PRK10938 174 LAELLASlHQSGITLVLVLNRFDEIPDFVQFAGVLA 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
833-1013 |
8.66e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.00 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 833 QGHITAFLGHNGAGKTTTLSILSGLF---------PPS--------GGSAF------ILGHDVRSSMAairphlgvcPQY 889
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkpnlgdydeEPSwdevlkrfRGTELqdyfkkLANGEIKVAHK---------PQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 890 nvlFDML-------------TVDEHvwfyGRLKGLSaavvgpeqDRLlqDVGLVSKQSVqtRHLSGG-MQRkLSVAIAFV 955
Cdd:COG1245 169 ---VDLIpkvfkgtvrelleKVDER----GKLDELA--------EKL--GLENILDRDI--SELSGGeLQR-VAIAAALL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768000599 956 GGSQVVILDEPTAGVDPASR----RGIWELLlkyREGRTLILSTHHLDEAELLGDRVAVVAG 1013
Cdd:COG1245 229 RDADFYFFDEPSSYLDIYQRlnvaRLIRELA---EEGKYVLVVEHDLAILDYLADYVHILYG 287
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
802-1040 |
1.57e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.20 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 802 GLSPGVSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDV-RSSMAAIR 880
Cdd:cd03288 15 GLGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 881 PHLGVCPQYNVLF----------DMLTVDEHVWF---YGRLKGLSAAVVGpeqdrllqdvGLVSKQSVQTRHLSGGMQRK 947
Cdd:cd03288 95 SRLSIILQDPILFsgsirfnldpECKCTDDRLWEaleIAQLKNMVKSLPG----------GLDAVVTEGGENFSVGQRQL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 948 LSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAeLLGDRVAVVAGGRLCCCGSPLFLRR 1027
Cdd:cd03288 165 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTI-LDADLVLVLSRGILVECDTPENLLA 243
|
250
....*....|...
gi 768000599 1028 HlGSGYYLTLVKA 1040
Cdd:cd03288 244 Q-EDGVFASLVRT 255
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
834-1008 |
1.58e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 834 GHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHdvrSSMAAIR---PHLGVcPQYNVLFD-----------MLTVD 899
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN---WQLAWVNqetPALPQ-PALEYVIDgdreyrqleaqLHDAN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 900 EH------VWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQ-TRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDP 972
Cdd:PRK10636 103 ERndghaiATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 768000599 973 ASRrgIW-ELLLKYREGrTLILSTHHLDEAELLGDRV 1008
Cdd:PRK10636 183 DAV--IWlEKWLKSYQG-TLILISHDRDFLDPIVDKI 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
832-971 |
3.41e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.08 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 832 YQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFIlghDVRSSMAairphlgvcPQY-NVLFDMlTVDEHV-------- 902
Cdd:COG1245 364 REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE---DLKISYK---------PQYiSPDYDG-TVEEFLrsantddf 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000599 903 ---WFYGRlkglsaaVVGPEQ-DRLLQdvglvskQSVqtRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVD 971
Cdd:COG1245 431 gssYYKTE-------IIKPLGlEKLLD-------KNV--KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
102-689 |
3.53e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 42.17 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 102 VSRLLADARTVLGGASAHRTLAGLGKLIATLRAARSTAQPQPTKQSpleppmlDVAELLTSLLRTESLGLAL-------- 173
Cdd:COG3321 783 VEALLADGVRVFLEVGPGPVLTGLVRQCLAAAGDAVVLPSLRRGED-------ELAQLLTALAQLWVAGVPVdwsalypg 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 174 --------------GQAQEPLHSLLEAAEDLAQELLALRSLVELRALLQRPRGTSGPLELLSEALCSVRGPSSTVGPSLN 239
Cdd:COG3321 856 rgrrrvplptypfqREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVAL 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 240 WYEASDLMELVGQEPESALPDSSLSPACSELIGALDSHPLSRLLWRRLKPLILGKLLFAPDTPFTRKLMAQVNRTFEELT 319
Cdd:COG3321 936 AAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAA 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 320 LLRDVREVWEMLGPRIFTFMNDSSNVAMLQRLLQMQDEGRRQPRPGGRDHMEALRSFLDPGSGGYSWQDAHADVGHLVGT 399
Cdd:COG3321 1016 AAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAAL 1095
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 400 LGRVTECLSLDKLEAAPSEAALVSRALQLLAEHRFWAGVVFLGPEDSSDPTEHPTPDLGPGHVRIKIRMDIDVVTRTNKI 479
Cdd:COG3321 1096 ALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLL 1175
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 480 RDRFWDPGPAADPLTDLRYVWGGFVYLQDLVERAAVRVLSGANPRAGLYLQQMPyPCYVDDVFLRVLSRSLPLFLTLAWI 559
Cdd:COG3321 1176 ALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAA-AAALALLALAAAAAAVAALAAAAAA 1254
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 560 YSVTLTVKAVVREKETRLRDTMRAMGLSRAVLWLGWFLSCLGPFLLSAALLVLVLKLGDILPYSHPGVVFLFLAAFAVAT 639
Cdd:COG3321 1255 LLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALA 1334
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 768000599 640 VTQSFLLSAFFSRANLAAACGGLAYFSLYLPYVLCVAWRDRLPAGGRVAA 689
Cdd:COG3321 1335 AAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
922-1020 |
3.89e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.70 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 922 RLLQDVG---LVSKQSVQTrhLSGG-MQRklsVAIAFVGGSQVV----ILDEPTAGVDPASRRGIWELLLKYRE-GRTLI 992
Cdd:cd03270 119 GFLVDVGlgyLTLSRSAPT--LSGGeAQR---IRLATQIGSGLTgvlyVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVL 193
|
90 100 110
....*....|....*....|....*....|....
gi 768000599 993 LSTHHLDeAELLGDRV------AVVAGGRLCCCG 1020
Cdd:cd03270 194 VVEHDED-TIRAADHVidigpgAGVHGGEIVAQG 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
791-1016 |
4.59e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 791 DPKVLVEEAPPGLSPGVSVRSLEKR---FPGSPQpALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFi 867
Cdd:PLN03073 490 DPDYKFEFPTPDDRPGPPIISFSDAsfgYPGGPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 868 lghdvRSsmAAIRphLGVCPQYNVlfDMLTVDEHVWFYgrlkgLSAAVVG-PEQdRL---LQDVGLVSKQSVQTRH-LSG 942
Cdd:PLN03073 568 -----RS--AKVR--MAVFSQHHV--DGLDLSSNPLLY-----MMRCFPGvPEQ-KLrahLGSFGVTGNLALQPMYtLSG 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768000599 943 GMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELlgDRVAVVAGGRL 1016
Cdd:PLN03073 631 GQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSV--DELWVVSEGKV 702
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
891-999 |
8.51e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.91 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000599 891 VLfDMlTVDEHVWFYGRLKGLSAAVvgpeqdRLLQDVGL---VSKQSVQTrhLSGG-MQR-KLSVAIAF-VGGSQVVILD 964
Cdd:cd03271 128 VL-DM-TVEEALEFFENIPKIARKL------QTLCDVGLgyiKLGQPATT--LSGGeAQRiKLAKELSKrSTGKTLYILD 197
|
90 100 110
....*....|....*....|....*....|....*.
gi 768000599 965 EPTAGVDPASRRGIWELLLKYRE-GRTLILSTHHLD 999
Cdd:cd03271 198 EPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLD 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
833-860 |
9.32e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.56 E-value: 9.32e-03
10 20
....*....|....*....|....*...
gi 768000599 833 QGHITAFLGHNGAGKTTTLSILSGLFPP 860
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIP 125
|
|
| |
