|
Name |
Accession |
Description |
Interval |
E-value |
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-604 |
0e+00 |
|
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: 892.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 6 TRIAIVSSDRCKPKKCRQECKKSCPVVKTGKLCIEVTVGSKLAFISEELCIGCGICVKKCPFEAIQIINLPRDLEKDTTH 85
Cdd:COG1245 2 MRIAVVDRDRCQPKKCNYECIKYCPVNRTGKEAIEIDEDDGKPVISEELCIGCGICVKKCPFDAISIVNLPEELEEDPVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 86 RYGANTFKLHRLPVPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPDWQEILTHFRGSELQNYFTRILEDNLK 165
Cdd:COG1245 82 RYGENGFRLYGLPVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKRFRGTELQDYFKKLANGEIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 166 AIIKPQYVDHIPRAVKGNVGEVLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSS 245
Cdd:COG1245 162 VAHKPQYVDLIPKVFKGTVRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 246 YLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCLYGKPGAYGVVTLPFSVREGINIFLAGFVPTENLRFR 325
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILYGEPGVYGVVSKPKSVRVGINQYLDGYLPEENVRIR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 326 DESLTFKVAETPQESAEEIqsyaRYKYPTMTKTQGNFRLRVSEGEFTDSQIIVMLGENGTGKTTFIRMLAGLLKPDdtEG 405
Cdd:COG1245 322 DEPIEFEVHAPRREKEEET----LVEYPDLTKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPD--EG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 406 pdrEIP-EFNVSYKPQKISPKFQNSVRHLLHQKIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGK 484
Cdd:COG1245 396 ---EVDeDLKISYKPQYISPDYDGTVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 485 PADIYLIDEPSAYLDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIVYEGQPSIDCTANCPQSLLSGMNLF 564
Cdd:COG1245 473 DADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGVHGHASGPMDMREGMNRF 552
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 22328793 565 LSHLNITFRRDPTNFRPRINKLESTKDREQKSAGSYYYLD 604
Cdd:COG1245 553 LKELGITFRRDEETGRPRINKPGSYLDREQKERGEYYYYE 592
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-604 |
0e+00 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 872.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 6 TRIAIVSSDRCKPKKCRQECKKSCPVVKTGKLCIEVTVGSKLAFISEELCIGCGICVKKCPFEAIQIINLPRDLEKDTTH 85
Cdd:PRK13409 2 MRIAVVDYDRCQPKKCNYECIKYCPVVRTGEETIEIDEDDGKPVISEELCIGCGICVKKCPFDAISIVNLPEELEEEPVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 86 RYGANTFKLHRLPVPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPDWQEILTHFRGSELQNYFTRILEDNLK 165
Cdd:PRK13409 82 RYGVNGFKLYGLPIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRFRGTELQNYFKKLYNGEIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 166 AIIKPQYVDHIPRAVKGNVGEVLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSS 245
Cdd:PRK13409 162 VVHKPQYVDLIPKVFKGKVRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 246 YLDVKQRLKAAQVVRSLLRpNSYVIVVEHDLSVLDYLSDFICCLYGKPGAYGVVTLPFSVREGINIFLAGFVPTENLRFR 325
Cdd:PRK13409 242 YLDIRQRLNVARLIRELAE-GKYVLVVEHDLAVLDYLADNVHIAYGEPGAYGVVSKPKGVRVGINEYLKGYLPEENMRIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 326 DESLTFKVAETPQESAEEIQSyaryKYPTMTKTQGNFRLRVSEGEFTDSQIIVMLGENGTGKTTFIRMLAGLLKPDdtEG 405
Cdd:PRK13409 321 PEPIEFEERPPRDESERETLV----EYPDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPD--EG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 406 -PDREIpefNVSYKPQKISPKFQNSVRHLLhQKIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGK 484
Cdd:PRK13409 395 eVDPEL---KISYKPQYIKPDYDGTVEDLL-RSITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 485 PADIYLIDEPSAYLDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIVYEGQPSIDCTANCPQSLLSGMNLF 564
Cdd:PRK13409 471 DADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGEPGKHGHASGPMDMREGMNRF 550
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 22328793 565 LSHLNITFRRDPTNFRPRINKLESTKDREQKSAGSYYYLD 604
Cdd:PRK13409 551 LKELGITFRRDEETGRPRVNKPGSYLDREQKERGEYYYAD 590
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
78-332 |
1.05e-169 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 482.64 E-value: 1.05e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 78 DLEKDTTHRYGANTFKLHRLPVPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPDWQEILTHFRGSELQNYFT 157
Cdd:cd03236 1 ELEDEPVHRYGPNSFKLHRLPVPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 158 RILEDNLKAIIKPQYVDHIPRAVKGNVGEVLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEI 237
Cdd:cd03236 81 KLLEGDVKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 238 YMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCLYGKPGAYGVVTLPFSVREGINIFLAGFV 317
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPGAYGVVTLPKSVREGINEFLDGYL 240
|
250
....*....|....*
gi 22328793 318 PTENLRFRDESLTFK 332
Cdd:cd03236 241 PTENMRFREESIEFE 255
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
350-598 |
5.60e-154 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 442.23 E-value: 5.60e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 350 YKYPTMTKTQGNFRLRVSEGEFTDSQIIVMLGENGTGKTTFIRMLAGLLKPDDTegpDREIPEFNVSYKPQKISPKFQNS 429
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG---DIEIELDTVSYKPQYIKADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 430 VRHLLHQKIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKV 509
Cdd:cd03237 78 VRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 510 IKRFILHAKKTAFVVEHDFIMATYLADRVIVYEGQPSIDCTANCPQSLLSGMNLFLSHLNITFRRDPTNFRPRINKLEST 589
Cdd:cd03237 158 IRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVANPPQSLRSGMNRFLKNLDITFRRDPETGRPRINKLGSV 237
|
....*....
gi 22328793 590 KDREQKSAG 598
Cdd:cd03237 238 KDREQKESG 246
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
351-573 |
6.25e-72 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 229.00 E-value: 6.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 351 KYPTMTKTQGNFRLRVSEGEFTDSQIIVMLGENGTGKTTFIRMLAGLLKPddtEGPDREIPEFNVSYKPQKISpkfqnsv 430
Cdd:cd03222 2 LYPDCVKRYGVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIP---NGDNDEWDGITPVYKPQYID------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 431 rhllhqkirdsymhpqfmsdvmkplqieqlmdqevvnLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVI 510
Cdd:cd03222 72 -------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 511 KRFILHAKKTAFVVEHDFIMATYLADRVIVYEGQPSIDCTANCPQSLLSGMNLFLSHLNITFR 573
Cdd:cd03222 115 RRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYLITFR 177
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
101-314 |
2.62e-45 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 160.65 E-value: 2.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRftsppdwqeilthfrgselqnyftrILEDNLKAIIKPQYvdhIPRAV 180
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD-------------------------IEIELDTVSYKPQY---IKADY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 181 KGNVGEVLDQKDERDK-----KAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKA 255
Cdd:cd03237 75 EGTVRDLLSSITKDFYthpyfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 256 AQVVRSL-LRPNSYVIVVEHDLSVLDYLSDFICCLYGKPGAYGVVTLPFSVREGINIFLA 314
Cdd:cd03237 155 SKVIRRFaENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVANPPQSLRSGMNRFLK 214
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
79-321 |
1.32e-44 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 156.58 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 79 LEKDTTHRYGaNTFKLHRLPVPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFtsppDWqeilthfrgselqnyftr 158
Cdd:cd03222 2 LYPDCVKRYG-VFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND----EW------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 159 ileDNLKAIIKPQYVDhipravkgnvgevldqkderdkkaelcadlelnqvidrdvenLSGGELQRFAIAVVAIQNAEIY 238
Cdd:cd03222 59 ---DGITPVYKPQYID------------------------------------------LSGGELQRVAIAAALLRNATFY 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 239 MFDEPSSYLDVKQRLKAAQVVRSLLRPNS-YVIVVEHDLSVLDYLSDFICCLYGKPGAYGVVTLPFSVREGINIFLAGFV 317
Cdd:cd03222 94 LFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYL 173
|
....
gi 22328793 318 PTEN 321
Cdd:cd03222 174 ITFR 177
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
362-580 |
1.31e-37 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 139.81 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 362 FRLRVSEgeftDSQIIVMLGENGTGKTTFIRMLAGLLKPD----DTEGPDREIPEF------------------NVSYKP 419
Cdd:cd03236 18 HRLPVPR----EGQVLGLVGPNGIGKSTALKILAGKLKPNlgkfDDPPDWDEILDEfrgselqnyftkllegdvKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 420 QKIS--PK-FQNSVRHLLHQKIRDSymhpqFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSA 496
Cdd:cd03236 94 QYVDliPKaVKGKVGELLKKKDERG-----KLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 497 YLDSEQRIVASKVIKRFILHaKKTAFVVEHDFIMATYLADRVIVYEGQPSIDCTANCPQSLLSGMNLFLSHL----NITF 572
Cdd:cd03236 169 YLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLYGEPGAYGVVTLPKSVREGINEFLDGYlpteNMRF 247
|
....*...
gi 22328793 573 RRDPTNFR 580
Cdd:cd03236 248 REESIEFE 255
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
101-544 |
7.56e-32 |
|
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: 129.64 E-value: 7.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGkLKPNLGRFTSppdwqEILthFRGSELQNYFTRILEDNLKAIikPQYVDH--IPR 178
Cdd:COG1123 30 APGETVALVGESGSGKSTLALALMG-LLPHGGRISG-----EVL--LDGRDLLELSEALRGRRIGMV--FQDPMTqlNPV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 179 AVKGNVGEVLDQ----KDERDKKA-ELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRL 253
Cdd:COG1123 100 TVGDQIAEALENlglsRAEARARVlELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 254 KAAQVVRSLLR-PNSYVIVVEHDLSVLDYLSDFICCLYGkpgayGVVTLPFSVREginIFLAgfvPTENLRFRDESLTFK 332
Cdd:COG1123 180 EILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDD-----GRIVEDGPPEE---ILAA---PQALAAVPRLGAARG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 333 VAETPQESAEEI-------QSYARYKYPTMTKTQG-NFRLRvsEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDD-- 402
Cdd:COG1123 249 RAAPAAAAAEPLlevrnlsKRYPVRGKGGVRAVDDvSLTLR--RGE-----TLGLVGESGSGKSTLARLLLGLLRPTSgs 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 403 --------TEGPDREIPEFnvsykPQKISPKFQNSVRHLL-HQKIRDSYMHPQFMSDVMKPLQ----IEQLMDQ-----E 464
Cdd:COG1123 322 ilfdgkdlTKLSRRSLREL-----RRRVQMVFQDPYSSLNpRMTVGDIIAEPLRLHGLLSRAErrerVAELLERvglppD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 465 VVN-----LSGGELQRV----ALTLclgKPaDIYLIDEP-SAyLD-SEQRIVAsKVIKRfiLHAK--KTAFVVEHDFIMA 531
Cdd:COG1123 397 LADrypheLSGGQRQRVaiarALAL---EP-KLLILDEPtSA-LDvSVQAQIL-NLLRD--LQRElgLTYLFISHDLAVV 468
|
490
....*....|....
gi 22328793 532 TYLADRVIV-YEGQ 544
Cdd:COG1123 469 RYIADRVAVmYDGR 482
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
360-540 |
1.74e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 101.43 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 360 GNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPddTEGP----DREIPEFN-------VSYKPQKiSPKFQN 428
Cdd:COG4619 17 SPVSLTLEAGEC-----VAITGPSGSGKSTLLRALADLDPP--TSGEiyldGKPLSAMPppewrrqVAYVPQE-PALWGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 SVR-HLLH-QKIRDSYMHPQFMSDVMKPLQI-EQLMDQEVVNLSGGELQRVAL--TLCLGKpaDIYLIDEPSAYLDSEQR 503
Cdd:COG4619 89 TVRdNLPFpFQLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALirALLLQP--DVLLLDEPTSALDPENT 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 22328793 504 IVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIV 540
Cdd:COG4619 167 RRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLT 203
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
101-289 |
1.00e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 99.46 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPN------LGRFTSPPDWQEILTH----FRGSELQNYFTRILED------NL 164
Cdd:cd03225 25 KKGEFVLIVGPNGSGKSTLLRLLNGLLGPTsgevlvDGKDLTKLSLKELRRKvglvFQNPDDQFFGPTVEEEvafgleNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 165 KaiikpqyvdhipravkgnvgevLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPS 244
Cdd:cd03225 105 G----------------------LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22328793 245 SYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCL 289
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
81-542 |
3.27e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGAN------TFKLHrlpvprPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPDW------QEILTHFR 148
Cdd:COG0488 2 ENLSKSFGGRpllddvSLSIN------PGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigylpQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 149 GSELQNYFT------RILEDNLKAIIKPQYVDHIPRAvkgnVGEVLDQKDERD------KKAELCADLELNQVI-DRDVE 215
Cdd:COG0488 76 LTVLDTVLDgdaelrALEAELEELEAKLAEPDEDLER----LAELQEEFEALGgweaeaRAEEILSGLGFPEEDlDRPVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 216 NLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVK------QRLKAaqvvrsllRPNSyVIVVEHDLSVLDYLSDFICCL 289
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLEsiewleEFLKN--------YPGT-VLVVSHDRYFLDRVATRILEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 290 -YGK----PGAYgvvtlpfsvreginiflAGFVPTENLRFRDESLTFKVAetpQESAEEIQSYAR---YKYPTMTKTQ-- 359
Cdd:COG0488 223 dRGKltlyPGNY-----------------SAYLEQRAERLEQEAAAYAKQ---QKKIAKEEEFIRrfrAKARKAKQAQsr 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 360 ----------------GNFRLRVSEGE---------------FTDSQI-------------IVMLGENGTGKTTFIRMLA 395
Cdd:COG0488 283 ikaleklereepprrdKTVEIRFPPPErlgkkvleleglsksYGDKTLlddlslridrgdrIGLIGPNGAGKSTLLKLLA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 396 GLLKPDD---TEGP---------DREipEFNVSYKP----QKISPKFQN-SVRHLLHqkirdsymhpQFM---SDVMKPl 455
Cdd:COG0488 363 GELEPDSgtvKLGEtvkigyfdqHQE--ELDPDKTVldelRDGAPGGTEqEVRGYLG----------RFLfsgDDAFKP- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 456 qieqlmdqeVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDseqriVASK-VIKRFILHAKKTAFVVEHD--FIMAt 532
Cdd:COG0488 430 ---------VGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD-----IETLeALEEALDDFPGTVLLVSHDryFLDR- 494
|
570
....*....|
gi 22328793 533 yLADRVIVYE 542
Cdd:COG0488 495 -VATRILEFE 503
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
361-542 |
3.40e-23 |
|
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: 96.16 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPddTEGpdreipefNVSYKPQKISPKFqnsvRHLLHQKIrd 440
Cdd:cd00267 17 NVSLTLKAGEIV-----ALVGPNGSGKSTLLRAIAGLLKP--TSG--------EILIDGKDIAKLP----LEELRRRI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 441 SYMhPQfmsdvmkplqieqlmdqevvnLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFILHaKKT 520
Cdd:cd00267 76 GYV-PQ---------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRT 132
|
170 180
....*....|....*....|..
gi 22328793 521 AFVVEHDFIMATYLADRVIVYE 542
Cdd:cd00267 133 VIIVTHDPELAELAADRVIVLK 154
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
361-540 |
8.95e-23 |
|
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: 96.55 E-value: 8.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDDTegpDREIPEFNVSYKPQK---ISPKFQNsvrHLL--H 435
Cdd:cd03301 18 DLNLDIADGEF-----VVLLGPSGCGKTTTLRMIAGLEEPTSG---RIYIGGRDVTDLPPKdrdIAMVFQN---YALypH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 436 QKIRDSYMHP------------QFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQR 503
Cdd:cd03301 87 MTVYDNIAFGlklrkvpkdeidERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 22328793 504 IVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIV 540
Cdd:cd03301 167 VQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAV 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
70-284 |
1.40e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 96.67 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 70 IQIINLprdlekdtTHRYGANT------FKLhrlpvpRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeI 143
Cdd:COG1131 1 IEVRGL--------TKRYGDKTaldgvsLTV------EPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVR-------V 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 144 LTHFRGSELQNYFTRI--------LEDNLKAIikpQYVDHIpRAVKGnvgevLDQKDERDKKAELCADLELNQVIDRDVE 215
Cdd:COG1131 60 LGEDVARDPAEVRRRIgyvpqepaLYPDLTVR---ENLRFF-ARLYG-----LPRKEARERIDELLELFGLTDAADRKVG 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 216 NLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSD 284
Cdd:COG1131 131 TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCD 199
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
349-540 |
2.00e-22 |
|
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: 95.61 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 349 RYKYPTMTKTQG-NFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPddTEG----PDREIPEFNVSYKPQKIS 423
Cdd:cd03225 6 SFSYPDGARPALdDISLTIKKGEF-----VLIVGPNGSGKSTLLRLLNGLLGP--TSGevlvDGKDLTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 424 PKFQNSVRHLLHQKIRD-------SYMHPQF-----MSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLI 491
Cdd:cd03225 79 LVFQNPDDQFFGPTVEEevafgleNLGLPEEeieerVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22328793 492 DEPSAYLDSEQRIVASKVIKRfiLHAK-KTAFVVEHDFIMATYLADRVIV 540
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKK--LKAEgKTIIIVTHDLDLLLELADRVIV 206
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
81-276 |
2.24e-22 |
|
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: 94.42 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGaNTFKLHRLPV-PRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEIltHFRGSELQNYFTRI 159
Cdd:cd03214 3 ENLSVGYG-GRTVLDDLSLsIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSG---------EI--LLDGKDLASLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 160 LEDNLkAIIkPQyvdhipravkgnvgeVLDQkderdkkaelcadLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYM 239
Cdd:cd03214 71 LARKI-AYV-PQ---------------ALEL-------------LGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190
....*....|....*....|....*....|....*...
gi 22328793 240 FDEPSSYLDVKQRLKAAQVVRSLLR-PNSYVIVVEHDL 276
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDL 158
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
101-276 |
2.51e-22 |
|
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: 96.65 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEILthFRGSELQNYftriledNLKAIIK-----PQyvdH 175
Cdd:COG1120 25 PPGEVTALLGPNGSGKSTLLRALAGLLKPSSG---------EVL--LDGRDLASL-------SRRELARriayvPQ---E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 176 IPRAVKGNVGEV-----------LDQKDERDKKA--ELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDE 242
Cdd:COG1120 84 PPAPFGLTVRELvalgryphlglFGRPSAEDREAveEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190
....*....|....*....|....*....|....*
gi 22328793 243 PSSYLDVKQRLKAAQVVRSLLRPNSY-VIVVEHDL 276
Cdd:COG1120 164 PTSHLDLAHQLEVLELLRRLARERGRtVVMVLHDL 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
81-289 |
4.35e-22 |
|
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: 93.08 E-value: 4.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANTFkLHRLPV-PRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSELQNYFTRI 159
Cdd:cd00267 3 ENLSFRYGGRTA-LDNVSLtLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL-----------IDGKDIAKLPLEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 160 LEDNLkaIIKPQyvdhipravkgnvgevldqkderdkkaelcadlelnqvidrdvenLSGGELQRFAIAVVAIQNAEIYM 239
Cdd:cd00267 71 LRRRI--GYVPQ---------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22328793 240 FDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCL 289
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
70-284 |
5.03e-22 |
|
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: 95.31 E-value: 5.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 70 IQIINLprdlekdtTHRYGAN------TFKLhrlpvpRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEI 143
Cdd:COG4555 2 IEVENL--------SKKYGKVpalkdvSFTA------KDGEITGLLGPNGAGKTTLLRMLAGLLKPDSG---------SI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 144 LTHFRGSELQNYFTR----ILEDNlkaiikpqyvDHIP--RAVKGNV---GEVLDQKDERDKK--AELCADLELNQVIDR 212
Cdd:COG4555 59 LIDGEDVRKEPREARrqigVLPDE----------RGLYdrLTVRENIryfAELYGLFDEELKKriEELIELLGLEEFLDR 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 213 DVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSD 284
Cdd:COG4555 129 RVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCD 200
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
370-540 |
7.59e-22 |
|
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: 94.92 E-value: 7.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 370 EFTDSQIIVMLGENGTGKTTFIRMLAGLLKPD------DTEGPDREIPEF--NVSYKPQKI-SPKFqNSVR-HL-----L 434
Cdd:COG4555 23 TAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDsgsiliDGEDVRKEPREArrQIGVLPDERgLYDR-LTVReNIryfaeL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 435 HQKIRDSYmhPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDseqrIVASKVIKRFI 514
Cdd:COG4555 102 YGLFDEEL--KKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD----VMARRLLREIL 175
|
170 180
....*....|....*....|....*....
gi 22328793 515 LHAK---KTAFVVEHDFIMATYLADRVIV 540
Cdd:COG4555 176 RALKkegKTVLFSSHIMQEVEALCDRVVI 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
364-540 |
1.77e-21 |
|
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: 92.11 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPDDTE----GPDREipefnvSYKPQKISpkfqnsvrhllhQKIr 439
Cdd:cd03214 20 LSIEAGEIV-----GILGPNGAGKSTLLKTLAGLLKPSSGEilldGKDLA------SLSPKELA------------RKI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 440 dSYMhPQfmsdVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFILHAKK 519
Cdd:cd03214 76 -AYV-PQ----ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGK 149
|
170 180
....*....|....*....|.
gi 22328793 520 TAFVVEHDFIMATYLADRVIV 540
Cdd:cd03214 150 TVVMVLHDLNLAARYADRVIL 170
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
364-540 |
4.92e-21 |
|
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: 92.80 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPD------DtegpDREIPEFN-------VSYKPQKISPKFQNSV 430
Cdd:COG1120 22 LSLPPGEVT-----ALLGPNGSGKSTLLRALAGLLKPSsgevllD----GRDLASLSrrelarrIAYVPQEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 431 RHLL------HQKI--RDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQ 502
Cdd:COG1120 93 RELValgrypHLGLfgRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAH 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 22328793 503 RIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIV 540
Cdd:COG1120 173 QLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVL 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
349-540 |
5.03e-21 |
|
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: 92.01 E-value: 5.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 349 RYKYPTMTKTQGNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPddTEG----PDREIPEFNVSYKPQKISP 424
Cdd:COG1122 7 SFSYPGGTPALDDVSLSIEKGEF-----VAIIGPNGSGKSTLLRLLNGLLKP--TSGevlvDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 425 KFQN--------SVRH-----LLHQKIRDSYMHpQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVAL--TLCLgKPaDIY 489
Cdd:COG1122 80 VFQNpddqlfapTVEEdvafgPENLGLPREEIR-ERVEEALELVGLEHLADRPPHELSGGQKQRVAIagVLAM-EP-EVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22328793 490 LIDEPSAYLDSEQRIVASKVIKRfiLHAKKTAFV-VEHDFIMATYLADRVIV 540
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKR--LNKEGKTVIiVTHDLDLVAELADRVIV 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
360-540 |
7.95e-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: 91.63 E-value: 7.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 360 GNFRLRVSEGEFTDSQIIVMLGENGTGKTTFIRMLAGLLKPDD----TEGPD-REIP--EFNVSYKPQKIS--PK---FQ 427
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSgkilLNGKDiTNLPpeKRDISYVPQNYAlfPHmtvYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 428 NSVRHLLHQKIRDSYMHPQFMsDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVAS 507
Cdd:cd03299 91 NIAYGLKKRKVDKKEIERKVL-EIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190
....*....|....*....|....*....|...
gi 22328793 508 KVIKRFILHAKKTAFVVEHDFIMATYLADRVIV 540
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAI 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
364-540 |
3.99e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 89.76 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPD----DTEGPDREIPEFNVSYKPQK--ISPKFQNSVRHLL--- 434
Cdd:COG1121 27 LTIPPGEFV-----AIVGPNGAGKSTLLKAILGLLPPTsgtvRLFGKPPRRARRRIGYVPQRaeVDWDFPITVRDVVlmg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 435 ---------------HQKIRDsymhpqfmsdVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLD 499
Cdd:COG1121 102 rygrrglfrrpsradREAVDE----------ALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22328793 500 --SEQRIVAskVIKRfiLHAK-KTAFVVEHDFIMATYLADRVIV 540
Cdd:COG1121 172 aaTEEALYE--LLRE--LRREgKTILVVTHDLGAVREYFDRVLL 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
364-539 |
4.90e-20 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 88.74 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFTdsQIIvmlGENGTGKTTFIRMLAGLLKPddTEG-------PDREIPEfNVSYKPQK--ISPKFQNSVRHL- 433
Cdd:cd03235 20 FEVKPGEFL--AIV---GPNGAGKSTLLKAILGLLKP--TSGsirvfgkPLEKERK-RIGYVPQRrsIDRDFPISVRDVv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 434 ---------LHQKIRDSYMHpqfmsDVMKPLQ---IEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLD-- 499
Cdd:cd03235 92 lmglyghkgLFRRLSKADKA-----KVDEALErvgLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDpk 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22328793 500 SEQRIVAskVIKRfiLHAK-KTAFVVEHDFIMATYLADRVI 539
Cdd:cd03235 167 TQEDIYE--LLRE--LRREgMTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
350-539 |
5.73e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 88.47 E-value: 5.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 350 YKYPTMTKTQGNFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDDTE----GPDREIPEF--NVSYKPQkiS 423
Cdd:cd03226 7 FSYKKGTEILDDLSLDLYAGE-----IIALTGKNGAGKTTLAKILAGLIKESSGSillnGKPIKAKERrkSIGYVMQ--D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 424 PKFQ---NSVRHLLHQKIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVAL--TLCLGKpaDIYLIDEPSAYL 498
Cdd:cd03226 80 VDYQlftDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIaaALLSGK--DLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22328793 499 DSEQRIVASKVIKRfILHAKKTAFVVEHDFIMATYLADRVI 539
Cdd:cd03226 158 DYKNMERVGELIRE-LAAQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
81-286 |
6.19e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 88.47 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANTFKLHRLPVP-RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPDWqeilthfrgselqnyftRI 159
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDlYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP-----------------IK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 160 LEDNLKAI-IKPQYVDHI--PRAVKGNVGEVLDQKDERDKKAE-LCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNA 235
Cdd:cd03226 66 AKERRKSIgYVMQDVDYQlfTDSVREELLLGLKELDAGNEQAEtVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22328793 236 EIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFI 286
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
102-287 |
9.30e-20 |
|
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: 87.97 E-value: 9.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFtsppdwqeiltHFRGSELQNYFTRIlednlkaiikpQYV---DHIPR 178
Cdd:cd03235 24 PGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI-----------RVFGKPLEKERKRI-----------GYVpqrRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 179 AVKGNVGEVL-------------DQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSS 245
Cdd:cd03235 82 DFPISVRDVVlmglyghkglfrrLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22328793 246 YLDVKQRLKAAQVVRSLLRPNSYVIVVEHDL-SVLDYLSDFIC 287
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLgLVLEYFDRVLL 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
361-540 |
1.18e-19 |
|
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: 86.86 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPDDTE----GPDREIPEFNVSYKPQKISPKFQNS--VRHLl 434
Cdd:cd03229 18 DVSLNIEAGEIV-----ALLGPSGSGKSTLLRCIAGLEEPDSGSilidGEDLTDLEDELPPLRRRIGMVFQDFalFPHL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 435 hqKIRDSYMHPqfmsdvmkplqieqlmdqevvnLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRfi 514
Cdd:cd03229 92 --TVLENIALG----------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKS-- 145
|
170 180
....*....|....*....|....*...
gi 22328793 515 LHAK--KTAFVVEHDFIMATYLADRVIV 540
Cdd:cd03229 146 LQAQlgITVVLVTHDLDEAARLADRVVV 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
361-540 |
2.14e-19 |
|
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: 86.80 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKP-------DDTEGPDREIPEFNVSYKPQKIS--PK---FQN 428
Cdd:cd03259 18 DLSLTVEPGEFL-----ALLGPSGCGKTTLLRLIAGLERPdsgeiliDGRDVTGVPPERRNIGMVFQDYAlfPHltvAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 -----SVRHLLHQKIRDSymhpqfMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQR 503
Cdd:cd03259 93 iafglKLRGVPKAEIRAR------VRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 22328793 504 IVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIV 540
Cdd:cd03259 167 EELREELKELQRELGITTIYVTHDQEEALALADRIAV 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
361-540 |
2.42e-19 |
|
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: 85.53 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDdtEGpdrEIPEFNVSYKPQKISPKfqnsvrhllhQKIrd 440
Cdd:cd03230 18 DISLTVEKGE-----IYGLLGPNGAGKTTLIKIILGLLKPD--SG---EIKVLGKDIKKEPEEVK----------RRI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 441 SYM--HPQFMSDvMKPLqieqlmdqEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDseqrIVASKVIKRFILHAK 518
Cdd:cd03230 76 GYLpeEPSLYEN-LTVR--------ENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLD----PESRREFWELLRELK 142
|
170 180
....*....|....*....|....*
gi 22328793 519 ---KTAFVVEHDFIMATYLADRVIV 540
Cdd:cd03230 143 kegKTILLSSHILEEAERLCDRVAI 167
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
101-245 |
7.72e-19 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 83.47 E-value: 7.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEILthFRGSELQNYFTRILEDNLKAIikPQYVDHIPRA- 179
Cdd:pfam00005 9 NPGEILALVGPNGAGKSTLLKLIAGLLSPTEG---------TIL--LDGQDLTDDERKSLRKEIGYV--FQDPQLFPRLt 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328793 180 VKGNVGEVLD----QKDERDKKAElcADLE-------LNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSS 245
Cdd:pfam00005 76 VRENLRLGLLlkglSKREKDARAE--EALEklglgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
100-277 |
1.84e-18 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 85.25 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 100 PRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSELQNyFTRILEDNLKAIIKPQYVDHIPRA 179
Cdd:TIGR03873 24 APPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVD-----------LAGVDLHG-LSRRARARRVALVEQDSDTAVPLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 180 VKGNV--GEV-------LDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVK 250
Cdd:TIGR03873 92 VRDVValGRIphrslwaGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVR 171
|
170 180
....*....|....*....|....*..
gi 22328793 251 QRLKAAQVVRSLLRPNSYVIVVEHDLS 277
Cdd:TIGR03873 172 AQLETLALVRELAATGVTVVAALHDLN 198
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
356-540 |
2.67e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 84.34 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 356 TKTQGNFR------LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPddTEG--------PDREIPEF--NVSYKP 419
Cdd:COG1131 7 TKRYGDKTaldgvsLTVEPGE-----IFGLLGPNGAGKTTTIRMLLGLLRP--TSGevrvlgedVARDPAEVrrRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 420 QKIS--PKFqnSVR-HL-LHQKIR--DSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDE 493
Cdd:COG1131 80 QEPAlyPDL--TVReNLrFFARLYglPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22328793 494 PSAYLDSEQRivasKVIKRFILHAK---KTAFVVEHdfIM--ATYLADRVIV 540
Cdd:COG1131 158 PTSGLDPEAR----RELWELLRELAaegKTVLLSTH--YLeeAERLCDRVAI 203
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
81-284 |
2.91e-18 |
|
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: 84.47 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGAntfKLHRLPVPR-------PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSELQ 153
Cdd:COG1124 5 RNLSVSYGQ---GGRRVPVLKdvslevaPGESFGLVGESGSGKSTLLRALAGLERPWSGEVT-----------FDGRPVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 154 NYFTRileDNLKAIikpQYV--DhiPRAV---KGNVGEVLDQ------KDERDKK-AELCADLELN-QVIDRDVENLSGG 220
Cdd:COG1124 71 RRRRK---AFRRRV---QMVfqD--PYASlhpRHTVDRILAEplrihgLPDREERiAELLEQVGLPpSFLDRYPHQLSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 221 ELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRlkaAQVVRsLL------RPNSYVIvVEHDLSVLDYLSD 284
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQ---AEILN-LLkdlreeRGLTYLF-VSHDLAVVAHLCD 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
101-297 |
3.70e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 83.99 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSELQNYFTRIlednlkAIIkPQYVDhIPRAV 180
Cdd:COG1121 30 PPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVR-----------LFGKPPRRARRRI------GYV-PQRAE-VDWDF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 181 KGNVGEVLDQ-------------KDERDKKAELCADLELNQVIDRDVENLSGGELQR--FAIAVVaiQNAEIYMFDEPSS 245
Cdd:COG1121 91 PITVRDVVLMgrygrrglfrrpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRvlLARALA--QDPDLLLLDEPFA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22328793 246 YLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCLYGKPGAYG 297
Cdd:COG1121 169 GVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHG 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
361-543 |
4.16e-18 |
|
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: 82.05 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFTdsqIIVmlGENGTGKTTFIRMLAGLLKPddTEG----PDREIPEFNVSYKPQKISPKFQNSvrHLLHQ 436
Cdd:cd03228 20 DVSLTIKPGEKV---AIV--GPSGSGKSTLLKLLLRLYDP--TSGeiliDGVDLRDLDLESLRKNIAYVPQDP--FLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 437 KIRDsymhpqfmsdvmkplqieqlmdqevvN-LSGGELQRVALTLCLGKPADIYLIDEPSAYLD--SEQRIVasKVIKRf 513
Cdd:cd03228 91 TIRE--------------------------NiLSGGQRQRIAIARALLRDPPILILDEATSALDpeTEALIL--EALRA- 141
|
170 180 190
....*....|....*....|....*....|
gi 22328793 514 iLHAKKTAFVVEHDFIMATyLADRVIVYEG 543
Cdd:cd03228 142 -LAKGKTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
364-539 |
5.47e-18 |
|
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: 82.92 E-value: 5.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPddTEGP----DREIPEFN----VSYKPQKISPKFQNSvrHLL- 434
Cdd:cd03255 25 LSIEKGEFV-----AIVGPSGSGKSTLLNILGGLDRP--TSGEvrvdGTDISKLSekelAAFRRRHIGFVFQSF--NLLp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 435 HQKIRDSYMHPQFMSDVMKP------------LQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQ 502
Cdd:cd03255 96 DLTALENVELPLLLAGVPKKerreraeellerVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSET 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 22328793 503 RIVASKVIKRFILHAKKTAFVVEHDFIMATYlADRVI 539
Cdd:cd03255 176 GKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRII 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
87-276 |
7.16e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.52 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 87 YGANTFkLHRLPVPRP-GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSELQNYFTRILEDNLK 165
Cdd:PRK11231 12 YGTKRI-LNDLSLSLPtGKITALIGPNGCGKSTLLKCFARLLTPQSGTVF-----------LGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 166 AIikPQyVDHIPRAVKgnVGEV--------------LDQKDERdKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVA 231
Cdd:PRK11231 80 LL--PQ-HHLTPEGIT--VRELvaygrspwlslwgrLSAEDNA-RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22328793 232 IQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDL 276
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDL 198
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
357-545 |
1.86e-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: 81.57 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 357 KTQGNFRLRVSegeFT-DSQIIVMLGENGTGKTTFIRMLAGLLKPD-------DTEGPDREIpefNVSYKPQ--KISPKF 426
Cdd:cd03297 8 KRLPDFTLKID---FDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDggtivlnGTVLFDSRK---KINLPPQqrKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 427 QN-------SVRHLL--------HQKIRDSymhPQFMSDVMkplQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLI 491
Cdd:cd03297 82 QQyalfphlNVRENLafglkrkrNREDRIS---VDELLDLL---GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 492 DEPSAYLDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIVYE-GQP 545
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEdGRL 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
91-291 |
2.12e-17 |
|
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: 81.40 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 91 TFKLHRLPVP---------RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSELQNYFTRILE 161
Cdd:cd03257 10 SFPTGGGSVKalddvsfsiKKGETLGLVGESGSGKSTLARAILGLLKPTSGSII-----------FDGKDLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 162 DNLKAIikpQYVDHIPRA-------VKGNVGEVL--DQKDERDKKAELCADLELNQV-IDRDVEN-----LSGGELQRFA 226
Cdd:cd03257 79 IRRKEI---QMVFQDPMSslnprmtIGEQIAEPLriHGKLSKKEARKEAVLLLLVGVgLPEEVLNrypheLSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 227 IAVVAIQNAEIYMFDEPSSYLDVkqrLKAAQVVRsLLR-----PNSYVIVVEHDLSVLDYLSDFICCLYG 291
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDV---SVQAQILD-LLKklqeeLGLTLLFITHDLGVVAKIADRVAVMYA 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
361-540 |
2.83e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 83.58 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPddTEGpdrEIpEFN---VSYKPqkisPK-------FQN-- 428
Cdd:COG3839 21 DIDLDIEDGEF-----LVLLGPSGCGKSTLLRMIAGLEDP--TSG---EI-LIGgrdVTDLP----PKdrniamvFQSya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 -----SVR-----HL---------LHQKIRDsymhpqfmsdVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIY 489
Cdd:COG3839 86 lyphmTVYeniafPLklrkvpkaeIDRRVRE----------AAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22328793 490 LIDEPSAYLDSEQRIVASKVIKRfiLHAK-KTAFV-VEHDFIMATYLADRVIV 540
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKR--LHRRlGTTTIyVTHDQVEAMTLADRIAV 206
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
101-280 |
4.60e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 84.42 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT---------SPPDWQEILT------H-FRGSelqnyftriLEDNL 164
Cdd:COG4988 361 PPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdlDPASWRRQIAwvpqnpYlFAGT---------IRENL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 165 kAIIKPQYVDH-IPRAVKgNVGevLDqkderdkkaELCADLE--LNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFD 241
Cdd:COG4988 432 -RLGRPDASDEeLEAALE-AAG--LD---------EFVAALPdgLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLD 498
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22328793 242 EPSSYLDVKQrlkAAQVVRSL--LRPNSYVIVVEHDLSVLD 280
Cdd:COG4988 499 EPTAHLDAET---EAEILQALrrLAKGRTVILITHRLALLA 536
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
361-539 |
5.93e-17 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 79.58 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDDTEG--PDREIPEFN----VSYKPQKISPKFQN------ 428
Cdd:TIGR03608 16 DLNLTIEKGKM-----YAIIGESGSGKSTLLNIIGLLEKFDSGQVylNGQETPPLNskkaSKFRREKLGYLFQNfalien 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 -SVRH-----LLHQKIRDSYMHpQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQ 502
Cdd:TIGR03608 91 eTVEEnldlgLKYKKLSKKEKR-EKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKN 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 22328793 503 RivaSKVIKRF--ILHAKKTAFVVEHDFIMATyLADRVI 539
Cdd:TIGR03608 170 R---DEVLDLLleLNDEGKTIIIVTHDPEVAK-QADRVI 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
361-496 |
5.98e-17 |
|
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: 78.07 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKP-------DDTEGPDREIPEF--NVSYKPQKISPK-----F 426
Cdd:pfam00005 3 NVSLTLNPGE-----ILALVGPNGAGKSTLLKLIAGLLSPtegtillDGQDLTDDERKSLrkEIGYVFQDPQLFprltvR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328793 427 QNSVRHLLHQKIRDSYMHPQfMSDVMKPLQIEQLMDQEVVN----LSGGELQRVALTLCLGKPADIYLIDEPSA 496
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDAR-AEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
101-289 |
1.48e-16 |
|
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: 79.30 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSElqnyftrILEDNLKAIIK-----PQYVDH 175
Cdd:COG1122 25 EKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL-----------VDGKD-------ITKKNLRELRRkvglvFQNPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 176 -IpraVKGNVGE-V--------LDqKDERDKKA-ELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPS 244
Cdd:COG1122 87 qL---FAPTVEEdVafgpenlgLP-REEIRERVeEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22328793 245 SYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCL 289
Cdd:COG1122 163 AGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVL 207
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
350-540 |
2.12e-16 |
|
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: 82.50 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 350 YKYPTMTKTQGNFRLRVSEGEFTdsqIIVmlGENGTGKTTFIRMLAGLLKPDdtEG-------PDREIPEF----NVSYK 418
Cdd:COG4988 344 FSYPGGRPALDGLSLTIPPGERV---ALV--GPSGAGKSTLLNLLLGFLPPY--SGsilingvDLSDLDPAswrrQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 419 PQKisPK-FQNSVR------------HLLHQKIRDSYMHpQFmsdvmkplqIEQL---MDQEV----VNLSGGELQRVAL 478
Cdd:COG4988 417 PQN--PYlFAGTIRenlrlgrpdasdEELEAALEAAGLD-EF---------VAALpdgLDTPLgeggRGLSGGQAQRLAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328793 479 TLCLGKPADIYLIDEPSAYLD--SEQRIVASkvIKRfiLHAKKTAFVVEHDfIMATYLADRVIV 540
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDaeTEAEILQA--LRR--LAKGRTVILITHR-LALLAQADRILV 543
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
350-543 |
3.04e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 79.26 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 350 YKYPTMTKTQ-GNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPddTEGP----DREIPEFNVSYKPQKISP 424
Cdd:PRK13632 15 FSYPNSENNAlKNVSFEINEGEY-----VAILGHNGSGKSTISKILTGLLKP--QSGEikidGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 425 KFQN--------SVRH-----LLHQKIRDSYMhPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLI 491
Cdd:PRK13632 88 IFQNpdnqfigaTVEDdiafgLENKKVPPKKM-KDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22328793 492 DEPSAYLDSEqrivASKVIKRFILH----AKKTAFVVEHDFIMATyLADRVIVYEG 543
Cdd:PRK13632 167 DESTSMLDPK----GKREIKKIMVDlrktRKKTLISITHDMDEAI-LADKVIVFSE 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
102-287 |
3.16e-16 |
|
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: 77.72 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGselqnyftRILEDNLKAIIKPQYVDHI----- 176
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIV-----------LNG--------TVLFDSRKKINLPPQQRKIglvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 177 -----PR-AVKGNVG---EVLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYL 247
Cdd:cd03297 83 qyalfPHlNVRENLAfglKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22328793 248 DVKQRLKAAQVVRSLL-RPNSYVIVVEHDLSVLDYLSDFIC 287
Cdd:cd03297 163 DRALRLQLLPELKQIKkNLNIPVIFVTHDLSEAEYLADRIV 203
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
361-545 |
5.85e-16 |
|
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: 77.13 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDDTE---------GPDREIpefnvSYKPQK---------- 421
Cdd:cd03293 22 DISLSVEEGEF-----VALVGPSGCGKSTLLRIIAGLERPTSGEvlvdgepvtGPGPDR-----GYVFQQdallpwltvl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 422 ----ISPKFQNS--------VRHLLH----QKIRDSYmhpqfmsdvmkPLQieqlmdqevvnLSGGELQRVALTLCL-GK 484
Cdd:cd03293 92 dnvaLGLELQGVpkaearerAEELLElvglSGFENAY-----------PHQ-----------LSGGMRQRVALARALaVD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 485 PaDIYLIDEPSAYLDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIVYEGQP 545
Cdd:cd03293 150 P-DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARP 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
349-543 |
1.19e-15 |
|
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: 76.09 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 349 RYKYPTM-TKTQGNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDD----TEGPD-REIPEF----NVSYK 418
Cdd:cd03245 9 SFSYPNQeIPALDNVSLTIRAGEK-----VAIIGRVGSGKSTLLKLLAGLYKPTSgsvlLDGTDiRQLDPAdlrrNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 419 PQKIspkfqnsvrHLLHQKIRDSY-MHPQFMSD--VMKPLQIEQL----------MDQEV----VNLSGGELQRVALT-L 480
Cdd:cd03245 84 PQDV---------TLFYGTLRDNItLGAPLADDerILRAAELAGVtdfvnkhpngLDLQIgergRGLSGGQRQAVALArA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 481 CLGKPAdIYLIDEPSAYLD--SEQRIVasKVIKRFILHakKTAFVVEHDFIMATyLADRVIVYEG 543
Cdd:cd03245 155 LLNDPP-ILLLDEPTSAMDmnSEERLK--ERLRQLLGD--KTLIIITHRPSLLD-LVDRIIVMDS 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
70-286 |
1.70e-15 |
|
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: 74.74 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 70 IQIINLprdlekdtTHRYGANT------FKLhrlpvpRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEI 143
Cdd:cd03230 1 IEVRNL--------SKRYGKKTalddisLTV------EKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG---------EI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 144 lthfrgselqnyftRILEDNLKAIikpqyvdhiPRAVKGNVGEVLDQkderdkkAELCADLELNQVIDrdvenLSGGELQ 223
Cdd:cd03230 58 --------------KVLGKDIKKE---------PEEVKRRIGYLPEE-------PSLYENLTVRENLK-----LSGGMKQ 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 224 RFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFI 286
Cdd:cd03230 103 RLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRV 165
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
361-544 |
1.86e-15 |
|
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: 73.64 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDdtEGPDREIPEFNVSYKPQkispkfqnsvrhllhqkird 440
Cdd:cd03221 18 DISLTINPGD-----RIGLVGRNGAGKSTLLKLIAGELEPD--EGIVTWGSTVKIGYFEQ-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 441 symhpqfmsdvmkplqieqlmdqevvnLSGGELQRVALTLCLGKPADIYLIDEPSAYLDseqrIVASKVIKRFILHAKKT 520
Cdd:cd03221 71 ---------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD----LESIEALEEALKEYPGT 119
|
170 180
....*....|....*....|....
gi 22328793 521 AFVVEHDFIMATYLADRVIVYEGQ 544
Cdd:cd03221 120 VILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
81-280 |
1.97e-15 |
|
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: 73.64 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANT------FKLHrlpvprPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPDwqeilthfrgselqn 154
Cdd:cd03221 4 ENLSKTYGGKLllkdisLTIN------PGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 155 yftrilednlkaiIKPQYVDHipravkgnvgevldqkderdkkaelcadlelnqvidrdvenLSGGELQRFAIAVVAIQN 234
Cdd:cd03221 63 -------------VKIGYFEQ-----------------------------------------LSGGEKMRLALAKLLLEN 88
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22328793 235 AEIYMFDEPSSYLDVKQRlkaAQVVRSLLRPNSYVIVVEHDLSVLD 280
Cdd:cd03221 89 PNLLLLDEPTNHLDLESI---EALEEALKEYPGTVILVSHDRYFLD 131
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
361-540 |
2.24e-15 |
|
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: 79.49 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPddTEG-------PDREI-PEF---NVSYKPQKIspkfqns 429
Cdd:COG2274 493 NISLTIKPGER-----VAIVGRSGSGKSTLLKLLLGLYEP--TSGrilidgiDLRQIdPASlrrQIGVVLQDV------- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 430 vrHLLHQKIRD--SYMHPQF-MSDVMKPLQ-------IEQL---MDQEV----VNLSGGELQRVALTLCLGKPADIYLID 492
Cdd:COG2274 559 --FLFSGTIREniTLGDPDAtDEEIIEAARlaglhdfIEALpmgYDTVVgeggSNLSGGQRQRLAIARALLRNPRILILD 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22328793 493 EPSAYLD--SEQRIVASkvIKRFIlhAKKTAFVVEHDfiMAT-YLADRVIV 540
Cdd:COG2274 637 EATSALDaeTEAIILEN--LRRLL--KGRTVIIIAHR--LSTiRLADRIIV 681
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
103-322 |
2.91e-15 |
|
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: 75.45 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------TSPPDWQEIlthfrGSELQNY--FTRI-LEDNLKAIIKPQ 171
Cdd:cd03299 25 GDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngkditNLPPEKRDI-----SYVPQNYalFPHMtVYKNIAYGLKKR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 172 YVDhipravkgnvgevldqKDERDKKA-ELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVK 250
Cdd:cd03299 100 KVD----------------KKEIERKVlEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328793 251 QRLKAAQVVRSLLRPNSY-VIVVEHDLSVLDYLSDFICCLY-GKPGAYGVVTLPFSvrEGINIFLAGFVPTENL 322
Cdd:cd03299 164 TKEKLREELKKIRKEFGVtVLHVTHDFEEAWALADKVAIMLnGKLIQVGKPEEVFK--KPKNEFVAEFLGFNNI 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
373-540 |
3.61e-15 |
|
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: 74.71 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 373 DSQIIVMLGENGTGKTTFIRMLAGLLKPDDTEGpdrEIPEFNVSYKPQKISPK--FQNSVRHL---------------LH 435
Cdd:cd03266 30 PGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA---TVDGFDVVKEPAEARRRlgFVSDSTGLydrltarenleyfagLY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 436 QKIRDSYMhpQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDseqrIVASKVIKRFIL 515
Cdd:cd03266 107 GLKGDELT--ARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD----VMATRALREFIR 180
|
170 180
....*....|....*....|....*...
gi 22328793 516 HAK---KTAFVVEHDFIMATYLADRVIV 540
Cdd:cd03266 181 QLRalgKCILFSTHIMQEVERLCDRVVV 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
81-281 |
4.29e-15 |
|
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: 74.45 E-value: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANTFKLHRLPVP----RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEI-------LTHFRG 149
Cdd:cd03255 4 KNLSKTYGGGGEKVQALKGVslsiEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV--DGTDIsklsekeLAAFRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 150 SEL----QNY-----FTriLEDNlkaIIKPQYVDHIPRavkgnvgevldqKDERDKKAELCADLELNQVIDRDVENLSGG 220
Cdd:cd03255 82 RHIgfvfQSFnllpdLT--ALEN---VELPLLLAGVPK------------KERRERAEELLERVGLGDRLNHYPSELSGG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22328793 221 ELQRFAIAVVAIQNAEIYMFDEPSSYLDVkqrlKAAQVVRSLLRP-----NSYVIVVEHDLSVLDY 281
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDS----ETGKEVMELLRElnkeaGTTIVVVTHDPELAEY 206
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
101-292 |
4.39e-15 |
|
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: 74.78 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFtsppdwqeiltHFRGSEL-----------------QNyfTRILE-- 161
Cdd:cd03219 24 RPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-----------LFDGEDItglppheiarlgigrtfQI--PRLFPel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 162 ---DNLKAiikpqyVDHIPRAVKGNVGEVLDQKDERDKKAELCAD-LELNQVIDRDVENLSGGELQRFAIAVVAIQNAEI 237
Cdd:cd03219 91 tvlENVMV------AAQARTGSGLLLARARREEREARERAEELLErVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22328793 238 YMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCL-YGK 292
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLdQGR 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
105-277 |
8.54e-15 |
|
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: 73.38 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 105 VLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSElqnyfTRILEDNLKAIIK--PQYVDHIPRAvkg 182
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPSSGTIR-----------IDGQD-----VLKQPQKLRRRIGylPQEFGVYPNF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 183 NVGEVLD---------QKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRL 253
Cdd:cd03264 88 TVREFLDyiawlkgipSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERI 167
|
170 180
....*....|....*....|....*..
gi 22328793 254 KaaqvVRSLLR---PNSYVIVVEHDLS 277
Cdd:cd03264 168 R----FRNLLSelgEDRIVILSTHIVE 190
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
352-540 |
1.42e-14 |
|
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: 76.56 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 352 YPTMTKTQGNFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDDTEGP--DREIPEFN-------VSYKPQKi 422
Cdd:TIGR02857 331 YPGRRPALRPVSFTVPPGE-----RVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvnGVPLADADadswrdqIAWVPQH- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 423 sPK-FQNSVR------------HLLHQKIRDSYMHpQFMSDVmkPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIY 489
Cdd:TIGR02857 405 -PFlFAGTIAenirlarpdasdAEIREALERAGLD-EFVAAL--PQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22328793 490 LIDEPSAYLD--SEQRIVASkvIKRfiLHAKKTAFVVEHDfIMATYLADRVIV 540
Cdd:TIGR02857 481 LLDEPTAHLDaeTEAEVLEA--LRA--LAQGRTVLLVTHR-LALAALADRIVV 528
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
91-277 |
1.58e-14 |
|
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: 72.95 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 91 TFKLHRlpvprpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT-----SPPdwQEIlthfrGSELQNYFTRilEDNLK 165
Cdd:cd03220 42 SFEVPR------GERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTvrgrvSSL--LGL-----GGGFNPELTG--RENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 166 AiikpqyvdhipravkgnVGEVLD-QKDERDKKAELCADL-ELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEP 243
Cdd:cd03220 107 L-----------------NGRLLGlSRKEIDEKIDEIIEFsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190
....*....|....*....|....*....|....
gi 22328793 244 SSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLS 277
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
101-544 |
1.66e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.21 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLG---------RFTSPPD---------WQEILthfrgseLQNYFTrILEd 162
Cdd:COG1129 28 RPGEVHALLGENGAGKSTLMKILSGVYQPDSGeilldgepvRFRSPRDaqaagiaiiHQELN-------LVPNLS-VAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 163 NLkaiikpqYVDHIPRAvkgnvGEVLDQKDERDKKAELCADLELNqvID--RDVENLSGGELQRFAIAVVAIQNAEIYMF 240
Cdd:COG1129 99 NI-------FLGREPRR-----GGLIDWRAMRRRARELLARLGLD--IDpdTPVGDLSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 241 DEPSSYLDVK--QRLKAaqVVRSLLRPNSYVIVVEHDLS-VLDyLSDFICCLygkpgaygvvtlpfsvREGINIflagfv 317
Cdd:COG1129 165 DEPTASLTERevERLFR--IIRRLKAQGVAIIYISHRLDeVFE-IADRVTVL----------------RDGRLV------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 318 ptenlrfrdesLTFKVAETPQESA------EEIQSYarykYPTMTKTQGNFRLRVS----EGEFTDSQIIVMLGE----- 382
Cdd:COG1129 220 -----------GTGPVAELTEDELvrlmvgRELEDL----FPKRAAAPGEVVLEVEglsvGGVVRDVSFSVRAGEilgia 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 383 --NGTGKTTFIRMLAGLLKPDdtEGpdreipEFNVSYKPQKI-SPkfQNSVRH--------------LLHQKIRD----- 440
Cdd:COG1129 285 glVGAGRTELARALFGADPAD--SG------EIRLDGKPVRIrSP--RDAIRAgiayvpedrkgeglVLDLSIREnitla 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 441 ---SYMHPQFMS---------DVMKPLQIE-QLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDseqriVAS 507
Cdd:COG1129 355 sldRLSRGGLLDrrreralaeEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID-----VGA 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 22328793 508 KV-IKRFI--LHAKKTAFVV---EHDFIMAtyLADRVIV-YEGQ 544
Cdd:COG1129 430 KAeIYRLIreLAAEGKAVIVissELPELLG--LSDRILVmREGR 471
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
364-544 |
1.69e-14 |
|
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: 73.24 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFTdsQIIvmlGENGTGKTTFIRMLAGLLKPD---------DTEG-PDREIPEFNVSYKPQKISPkFQN-SVR- 431
Cdd:cd03219 21 FSVRPGEIH--GLI---GPNGAGKTTLFNLISGFLRPTsgsvlfdgeDITGlPPHEIARLGIGRTFQIPRL-FPElTVLe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 432 -----HLLHQK-----IRDSYMHPQFMSDVMKPLQ---IEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYL 498
Cdd:cd03219 95 nvmvaAQARTGsglllARARREEREARERAEELLErvgLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22328793 499 DSEQRIVASKVIKRfiLHAKKTAFV-VEHD--FIMAtyLADRVIV-YEGQ 544
Cdd:cd03219 175 NPEETEELAELIRE--LRERGITVLlVEHDmdVVMS--LADRVTVlDQGR 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
361-527 |
1.92e-14 |
|
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: 72.51 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPD------DTEGPDREIPEF--NVSYKPQKISPKFQNSVR- 431
Cdd:COG4133 20 GLSFTLAAGE-----ALALTGPNGSGKTTLLRILAGLLPPSagevlwNGEPIRDAREDYrrRLAYLGHADGLKPELTVRe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 432 HL-LHQKIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVI 510
Cdd:COG4133 95 NLrFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELI 174
|
170
....*....|....*..
gi 22328793 511 KRFiLHAKKTAFVVEHD 527
Cdd:COG4133 175 AAH-LARGGAVLLTTHQ 190
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
101-289 |
3.05e-14 |
|
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: 70.87 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEILthFRGSELQNYftrILEDNLKAIIkpqYVDHIPRAV 180
Cdd:cd03228 26 KPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSG---------EIL--IDGVDLRDL---DLESLRKNIA---YVPQDPFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 181 KGNVGEVLdqkderdkkaelcadlelnqvidrdvenLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQrlkAAQVVR 260
Cdd:cd03228 89 SGTIRENI----------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET---EALILE 137
|
170 180 190
....*....|....*....|....*....|.
gi 22328793 261 SL--LRPNSYVIVVEHDLSVLDyLSDFICCL 289
Cdd:cd03228 138 ALraLAKGKTVIVIAHRLSTIR-DADRIIVL 167
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
70-287 |
3.87e-14 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 71.77 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 70 IQIINLprdlekdtTHRYGANTFK-LHRLPVP-RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeILTHF 147
Cdd:cd03263 1 LQIRNL--------TKTYKKGTKPaVDDLSLNvYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY-------INGYS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 148 RGSELQNYFTRI--------LEDNLKAIikpqyvDHI---PRaVKGnvgevLDQKDERDKKAELCADLELNQVIDRDVEN 216
Cdd:cd03263 66 IRTDRKAARQSLgycpqfdaLFDELTVR------EHLrfyAR-LKG-----LPKSEIKEEVELLLRVLGLTDKANKRART 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 217 LSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSlLRPNSYVIVVEHDLSVLDYLSDFIC 287
Cdd:cd03263 134 LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIA 203
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
101-289 |
4.38e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPD----------WQEILTHFRGSELQNYFTrilednLKAIIKP 170
Cdd:PRK09536 27 REGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraaSRRVASVPQDTSLSFEFD------VRQVVEM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 171 QYVDHIPRavkgnvgevLDQKDERDKKA--ELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLD 248
Cdd:PRK09536 101 GRTPHRSR---------FDTWTETDRAAveRAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22328793 249 VKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCL 289
Cdd:PRK09536 172 INHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLL 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
101-279 |
4.68e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 70.73 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPDwqeilthfrgselqnyftrilednlkaiIKPQYV---DHIP 177
Cdd:NF040873 16 PAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------------------------ARVAYVpqrSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 178 RAVKGNVGEV----------LDQKDERDKKAELCADLE---LNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPS 244
Cdd:NF040873 68 DSLPLTVRDLvamgrwarrgLWRRLTRDDRAAVDDALErvgLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*
gi 22328793 245 SYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVL 279
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
364-544 |
4.95e-14 |
|
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: 71.77 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPD---------DTEGPDREIpefnVSYKPQKISPKFQNSVRHL- 433
Cdd:cd03257 26 FSIKKGE-----TLGLVGESGSGKSTLARAILGLLKPTsgsiifdgkDLLKLSRRL----RKIRRKEIQMVFQDPMSSLn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 434 -LHqKIRDSYMHP---QFMSDVMKPLQIEQLMDQEVVN------------LSGGELQRV--ALTLCLgKPaDIYLIDEPS 495
Cdd:cd03257 97 pRM-TIGEQIAEPlriHGKLSKKEARKEAVLLLLVGVGlpeevlnrypheLSGGQRQRVaiARALAL-NP-KLLIADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 496 AYLDseqriVASKV-IKRFILHAKK---TAFV-VEHDFIMATYLADRVIV-YEGQ 544
Cdd:cd03257 174 SALD-----VSVQAqILDLLKKLQEelgLTLLfITHDLGVVAKIADRVAVmYAGK 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
81-277 |
5.52e-14 |
|
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: 71.40 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANTFKLH-RLPVPrPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR-FTSPPDWQEILTHFRGSEL--QNYf 156
Cdd:cd03259 4 KGLSKTYGSVRALDDlSLTVE-PGEFLALLGPSGCGKTTLLRLIAGLERPDSGEiLIDGRDVTGVPPERRNIGMvfQDY- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 157 trILEDNLkaiikpqyvdhiprAVKGNVGEVL-----DQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVA 231
Cdd:cd03259 82 --ALFPHL--------------TVAENIAFGLklrgvPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22328793 232 IQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSY-VIVVEHDLS 277
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGItTIYVTHDQE 192
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
101-280 |
6.25e-14 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 74.80 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT---------SPPDWQEIL------TH-FRGSelqnyftriLEDNL 164
Cdd:COG4987 359 PPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdlDEDDLRRRIavvpqrPHlFDTT---------LRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 165 KaIIKPQyvdhiprAVKGNVGEVLDQkderdkkAELCADLE-----LNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYM 239
Cdd:COG4987 430 R-LARPD-------ATDEELWAALER-------VGLGDWLAalpdgLDTWLGEGGRRLSGGERRRLALARALLRDAPILL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22328793 240 FDEPSSYLDvkqRLKAAQVVRSLLR--PNSYVIVVEHDLSVLD 280
Cdd:COG4987 495 LDEPTEGLD---AATEQALLADLLEalAGRTVLLITHRLAGLE 534
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
364-540 |
6.33e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKP---------DDTEGPDREIPEFNVSYKPQKISPKFQNSVRHLL 434
Cdd:PRK09536 24 LSVREGSL-----VGLVGPNGAGKTTLLRAINGTLTPtagtvlvagDDVEALSARAASRRVASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 435 H-----QKIRDSYMHPQFMSDV---MKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVA 506
Cdd:PRK09536 99 EmgrtpHRSRFDTWTETDRAAVeraMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRT 178
|
170 180 190
....*....|....*....|....*....|....
gi 22328793 507 SKVIKRFIlHAKKTAFVVEHDFIMATYLADRVIV 540
Cdd:PRK09536 179 LELVRRLV-DDGKTAVAAIHDLDLAARYCDELVL 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
102-280 |
6.37e-14 |
|
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: 70.97 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdWQEILTHFRGSElqnYFTRILednlkaiikpqYVDHIPrAVK 181
Cdd:COG4133 27 AGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL----WNGEPIRDARED---YRRRLA-----------YLGHAD-GLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 182 GN--VGEVLD-------QKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQR 252
Cdd:COG4133 88 PEltVRENLRfwaalygLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180
....*....|....*....|....*...
gi 22328793 253 LKAAQVVRSLLRPNSYVIVVEHDLSVLD 280
Cdd:COG4133 168 ALLAELIAAHLARGGAVLLTTHQPLELA 195
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
376-540 |
7.82e-14 |
|
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: 70.68 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 376 IIVMLGENGTGKTTFIRMLAGLLKP----------DDTEGPD--REIpefnVSYKPQKISPKFQNSVRHLLH-----QKI 438
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPssgtiridgqDVLKQPQklRRR----IGYLPQEFGVYPNFTVREFLDyiawlKGI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 439 RDSYMHPQfMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCL-GKPaDIYLIDEPSAYLDSEQRIVASKVIKRfiLHA 517
Cdd:cd03264 103 PSKEVKAR-VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALvGDP-SILIVDEPTAGLDPEERIRFRNLLSE--LGE 178
|
170 180
....*....|....*....|...
gi 22328793 518 KKTAFVVEHDFIMATYLADRVIV 540
Cdd:cd03264 179 DRIVILSTHIVEDVESLCNQVAV 201
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
361-543 |
8.10e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 8.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLlkPDDTEGpDREIPEFNVSYKPQK---ISPKFQnsvrhllhqk 437
Cdd:PRK11000 21 DINLDIHEGEF-----VVFVGPSGCGKSTLLRMIAGL--EDITSG-DLFIGEKRMNDVPPAergVGMVFQ---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 438 irdSY-MHPQF-----MSDVMK------------------PLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDE 493
Cdd:PRK11000 83 ---SYaLYPHLsvaenMSFGLKlagakkeeinqrvnqvaeVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22328793 494 PSAYLDS----EQRIVASKVIKRFilhaKKTAFVVEHDFIMATYLADRVIVYEG 543
Cdd:PRK11000 160 PLSNLDAalrvQMRIEISRLHKRL----GRTMIYVTHDQVEAMTLADKIVVLDA 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
361-545 |
8.17e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 71.66 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPddTEGpdreipefNVSYKPQKISPK-------FQN----- 428
Cdd:COG1116 29 DVSLTVAAGEF-----VALVGPSGCGKSTLLRLIAGLEKP--TSG--------EVLVDGKPVTGPgpdrgvvFQEpallp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 --SVRH--LLHQKIRDsymhpqfmsdvMKPLQIEQLMDQ--EVVNL-----------SGGELQRVAL--TLCLgKPaDIY 489
Cdd:COG1116 94 wlTVLDnvALGLELRG-----------VPKAERRERAREllELVGLagfedayphqlSGGMRQRVAIarALAN-DP-EVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22328793 490 LIDEP-SAyLDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIVYEGQP 545
Cdd:COG1116 161 LMDEPfGA-LDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARP 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
355-540 |
8.27e-14 |
|
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: 71.22 E-value: 8.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 355 MTKTQGNFR------LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPD-------DTEGPDREIPEFNVSYKpqk 421
Cdd:cd03296 8 VSKRFGDFValddvsLDIPSGE-----LVALLGPSGSGKTTLLRLIAGLERPDsgtilfgGEDATDVPVQERNVGFV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 422 ispkFQNSV--RHL-------LHQKIRDSYMHP------QFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPA 486
Cdd:cd03296 80 ----FQHYAlfRHMtvfdnvaFGLRVKPRSERPpeaeirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22328793 487 DIYLIDEPSAYLDSEQRivasKVIKRFI--LHAKK--TAFVVEHDFIMATYLADRVIV 540
Cdd:cd03296 156 KVLLLDEPFGALDAKVR----KELRRWLrrLHDELhvTTVFVTHDQEEALEVADRVVV 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
101-276 |
8.32e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 71.73 E-value: 8.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR---FTSPpdwqeiLTHFRGSELqnyfTRILednlkAIIkPQY----- 172
Cdd:PRK13548 26 RPGEVVAILGPNGAGKSTLLRALSGELSPDSGEvrlNGRP------LADWSPAEL----ARRR-----AVL-PQHsslsf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 173 ---VDHI-----------PRAVKGNVGEVLDQKDerdkkaelCADLElnqviDRDVENLSGGELQRFAIAVVAIQNAE-- 236
Cdd:PRK13548 90 pftVEEVvamgraphglsRAEDDALVAAALAQVD--------LAHLA-----GRDYPQLSGGEQQRVQLARVLAQLWEpd 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22328793 237 ----IYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSY-VIVVEHDL 276
Cdd:PRK13548 157 gpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLaVIVVLHDL 201
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
103-545 |
1.04e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.68 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGklkpnLGRFtsPPDWQEILTHFRGSELQNYFTRI----------------------- 159
Cdd:TIGR03269 26 GEVLGILGRSGAGKSVLMHVLRG-----MDQY--EPTSGRIIYHVALCEKCGYVERPskvgepcpvcggtlepeevdfwn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 160 LEDNLKAIIKPQYVDHIPRA--------VKGNVGEVLDQ-----KDERDKKAELCADLELNQVIDRDVENLSGGELQRFA 226
Cdd:TIGR03269 99 LSDKLRRRIRKRIAIMLQRTfalygddtVLDNVLEALEEigyegKEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 227 IAVVAIQNAEIYMFDEPSSYLDVKqrlkAAQVVRSLLRP-----NSYVIVVEHDLSVLDYLSDFICCLygKPGAYGVVTL 301
Cdd:TIGR03269 179 LARQLAKEPFLFLADEPTGTLDPQ----TAKLVHNALEEavkasGISMVLTSHWPEVIEDLSDKAIWL--ENGEIKEEGT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 302 PFSVregINIFLAGFVPTENlrfrdesltfkvaETPQESAEEI---QSYARYKYPT---MTKTQGNFRLRVSEGEftdsq 375
Cdd:TIGR03269 253 PDEV---VAVFMEGVSEVEK-------------ECEVEVGEPIikvRNVSKRYISVdrgVVKAVDNVSLEVKEGE----- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 376 IIVMLGENGTGKTTFIRMLAGLLKPddTEGpdreipEFNVSYKPQKI---SPKFQNSVRH-----LLHQKIrDSYMHPQF 447
Cdd:TIGR03269 312 IFGIVGTSGAGKTTLSKIIAGVLEP--TSG------EVNVRVGDEWVdmtKPGPDGRGRAkryigILHQEY-DLYPHRTV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 448 MSDVMKPLQIE-------------------------QLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQ 502
Cdd:TIGR03269 383 LDNLTEAIGLElpdelarmkavitlkmvgfdeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPIT 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 22328793 503 RIvaskVIKRFILHAKK----TAFVVEHDFIMATYLADRV-------IVYEGQP 545
Cdd:TIGR03269 463 KV----DVTHSILKAREemeqTFIIVSHDMDFVLDVCDRAalmrdgkIVKIGDP 512
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
375-543 |
1.27e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.20 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 375 QIIVMLGENGTGKTTFIRMLAGLLKP----------DDTEGPDREIPEfNVSYKPQK-ISPKfQNSVRHL---------- 433
Cdd:PRK11231 29 KITALIGPNGCGKSTLLKCFARLLTPqsgtvflgdkPISMLSSRQLAR-RLALLPQHhLTPE-GITVRELvaygrspwls 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 434 ----LHQKIRdsymhpQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKV 509
Cdd:PRK11231 107 lwgrLSAEDN------ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRL 180
|
170 180 190
....*....|....*....|....*....|....*
gi 22328793 510 IKRfiLHAK-KTAFVVEHDFIMATYLADRVIVYEG 543
Cdd:PRK11231 181 MRE--LNTQgKTVVTVLHDLNQASRYCDHLVVLAN 213
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
81-284 |
1.35e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.11 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGAN------TFKLHrlpvprPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEILTHFRGSELQN 154
Cdd:PRK11701 10 RGLTKLYGPRkgcrdvSFDLY------PGEVLGIVGESGSGKTTLLNALSARLAPDAG---------EVHYRMRDGQLRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 155 YFTrILEDNLKAIIKPQ--YVDHIPR-----AVK--GNVGEVL------DQKDERDKKAELCADLELNQV-IDRDVENLS 218
Cdd:PRK11701 75 LYA-LSEAERRRLLRTEwgFVHQHPRdglrmQVSagGNIGERLmavgarHYGDIRATAGDWLERVEIDAArIDDLPTTFS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328793 219 GGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRP-NSYVIVVEHDLSVLDYLSD 284
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAH 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
364-540 |
1.48e-13 |
|
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: 70.60 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPD-------DTEGPDREIPEFnvsykPQKISPKFQN---SV--R 431
Cdd:COG1124 26 LEVAPGE-----SFGLVGESGSGKSTLLRALAGLERPWsgevtfdGRPVTRRRRKAF-----RRRVQMVFQDpyaSLhpR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 432 HLLHQKIRDSYMHpQFMSDVMKplQIEQLMDQevVNL------------SGGELQRVAL--TLCLgKPaDIYLIDEPSAY 497
Cdd:COG1124 96 HTVDRILAEPLRI-HGLPDREE--RIAELLEQ--VGLppsfldryphqlSGGQRQRVAIarALIL-EP-ELLLLDEPTSA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22328793 498 LD-SEQ-RIVAskVIKRFILHAKKTAFVVEHDFIMATYLADRVIV 540
Cdd:COG1124 169 LDvSVQaEILN--LLKDLREERGLTYLFVSHDLAVVAHLCDRVAV 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
364-539 |
1.68e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.18 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPddTEGPDREIPEFNVSYKPQKIS--PKFQNSV----------- 430
Cdd:NF040873 13 LTIPAGSLT-----AVVGPNGSGKSTLLKVLAGVLRP--TSGTVRRAGGARVAYVPQRSEvpDSLPLTVrdlvamgrwar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 431 RHLLHQKIRDSYMhpqFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVI 510
Cdd:NF040873 86 RGLWRRLTRDDRA---AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALL 162
|
170 180 190
....*....|....*....|....*....|
gi 22328793 511 KRfiLHAKKTAFV-VEHDFIMATyLADRVI 539
Cdd:NF040873 163 AE--EHARGATVVvVTHDLELVR-RADPCV 189
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
325-540 |
1.78e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 70.44 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 325 RDESLTFKVAETPQESAEEIQSYARYKYPTMTKTQGnFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPddTE 404
Cdd:cd03267 4 SNLSKSYRVYSKEPGLIGSLKSLFKRKYREVEALKG-ISFTIEKGE-----IVGFIGPNGAGKTTTLKILSGLLQP--TS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 405 GpdreipEFNVS-YKPQKISPKFQNSVRHLLHQK--------IRDSYMHPQFMSDVMKP------------LQIEQLMDQ 463
Cdd:cd03267 76 G------EVRVAgLVPWKRRKKFLRRIGVVFGQKtqlwwdlpVIDSFYLLAAIYDLPPArfkkrldelselLDLEELLDT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 464 EVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDseqrIVASKVIKRFILHAKK----TAFVVEHDFIMATYLADRVI 539
Cdd:cd03267 150 PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD----VVAQENIRNFLKEYNRergtTVLLTSHYMKDIEALARRVL 225
|
.
gi 22328793 540 V 540
Cdd:cd03267 226 V 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
101-279 |
3.02e-13 |
|
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: 72.94 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT---------SPPDW--------QEILThFRGSelqnyftriLEDN 163
Cdd:COG2274 499 KPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqiDPASLrrqigvvlQDVFL-FSGT---------IREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 164 LkAIIKPQY-VDHIPRAVKgnvgevldqkderdkKAELCADLE-----LNQVIDRDVENLSGGELQRFAIAVVAIQNAEI 237
Cdd:COG2274 569 I-TLGDPDAtDEEIIEAAR---------------LAGLHDFIEalpmgYDTVVGEGGSNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22328793 238 YMFDEPSSYLDVKQRlkaAQVVRSL--LRPNSYVIVVEHDLSVL 279
Cdd:COG2274 633 LILDEATSALDAETE---AIILENLrrLLKGRTVIIIAHRLSTI 673
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
357-542 |
4.45e-13 |
|
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: 70.91 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 357 KTQGNFRLRVSEgEFTDSQIIVMLGENGTGKTTFIRMLAGLLKPDDTE-------------GPDREIPEFNVSYKPQKIS 423
Cdd:TIGR02142 7 KRLGDFSLDADF-TLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEivlngrtlfdsrkGIFLPPEKRRIGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 424 PKFQNSVRHLL---HQKIRDSYMHPQFMSdVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDS 500
Cdd:TIGR02142 86 LFPHLSVRGNLrygMKRARPSERRISFER-VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 22328793 501 EQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIVYE 542
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLE 206
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
364-540 |
4.68e-13 |
|
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: 67.07 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDDTEgpdreipefnVSYKPQKISPkfqNSVRHLLHQKIrdsYM 443
Cdd:cd03216 21 LSVRRGE-----VHALLGENGAGKSTLMKILSGLYKPDSGE----------ILVDGKEVSF---ASPRDARRAGI---AM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 444 HPQfmsdvmkplqieqlmdqevvnLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRfiLHAKKTAFV 523
Cdd:cd03216 80 VYQ---------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRR--LRAQGVAVI 136
|
170 180
....*....|....*....|
gi 22328793 524 -VEHDF--IMAtyLADRVIV 540
Cdd:cd03216 137 fISHRLdeVFE--IADRVTV 154
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
102-286 |
5.24e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 68.55 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT--------SPPDWQEILTHFRGS----------ELQNYFTRILedN 163
Cdd:cd03266 30 PGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgfdvvkEPAEARRRLGFVSDStglydrltarENLEYFAGLY--G 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 164 LKaiikpqyvdhiPRAVKGNVGEVLDQkderdkkaelcadLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEP 243
Cdd:cd03266 108 LK-----------GDELTARLEELADR-------------LGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22328793 244 SSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFI 286
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRV 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
364-544 |
5.45e-13 |
|
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: 71.47 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLL-KPDDTEGP----DREIPEFNVSYKPQKISPKFQN--------SV 430
Cdd:COG1123 27 LTIAPGET-----VALVGESGSGKSTLALALMGLLpHGGRISGEvlldGRDLLELSEALRGRRIGMVFQDpmtqlnpvTV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 431 RHLLHQKIRDSYMHPQFM----SDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVA 506
Cdd:COG1123 102 GDQIAEALENLGLSRAEArarvLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEI 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 22328793 507 SKVIKRFILHAKKTAFVVEHDFIMATYLADRVIV-YEGQ 544
Cdd:COG1123 182 LDLLRELQRERGTTVLLITHDLGVVAEIADRVVVmDDGR 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
102-294 |
6.07e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.27 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT---SPPDW---------QEILTHFRGSELQNYFTRILEDnlkaiik 169
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgKPLDYskrgllalrQQVATVFQDPEQQIFYTDIDSD------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 170 pqyvdhIPRAVKgNVGEVLDQKDERDKKAELCADLElnQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDV 249
Cdd:PRK13638 99 ------IAFSLR-NLGVPEAEITRRVDEALTLVDAQ--HFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22328793 250 KQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCL-------YGKPG 294
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLrqgqiltHGAPG 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
101-289 |
6.50e-13 |
|
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: 67.34 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSELQNYftrilEDNLKAIIKpqyvdhiprav 180
Cdd:cd03247 26 KQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-----------LDGVPVSDL-----EKALSSLIS----------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 181 kgnvgeVLDQKderdkkAELCADLELNQVIDRdvenLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVR 260
Cdd:cd03247 79 ------VLNQR------PYLFDTTLRNNLGRR----FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIF 142
|
170 180
....*....|....*....|....*....
gi 22328793 261 SLLRpNSYVIVVEHDLSVLDYLsDFICCL 289
Cdd:cd03247 143 EVLK-DKTLIWITHHLTGIEHM-DKILFL 169
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
82-291 |
7.17e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.05 E-value: 7.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 82 DTTHRYGANTFK------LHRLPVPRP-GQVLGLVGTNGIGKSTALKILagklkpnlGRFTSPPDWQEILTHFRGSELQN 154
Cdd:PRK10575 9 DTTFALRNVSFRvpgrtlLHPLSLTFPaGKVTGLIGHNGSGKSTLLKML--------GRHQPPSEGEILLDAQPLESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 155 -YFTRilednlKAIIKPQyvdHIPRAVKGNVGEVLD-------------QKDERDKKAELCADLELNQVIDRDVENLSGG 220
Cdd:PRK10575 81 kAFAR------KVAYLPQ---QLPAAEGMTVRELVAigrypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 221 ELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSY-VIVVEHDLSVLDYLSDFICCLYG 291
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLtVIAVLHDINMAARYCDYLVALRG 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
364-544 |
7.80e-13 |
|
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: 68.47 E-value: 7.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDD----------TEGPDREIPEFnvsykPQKISPKFQN----- 428
Cdd:COG1127 26 LDVPRGE-----ILAIIGGSGSGKSVLLKLIIGLLRPDSgeilvdgqdiTGLSEKELYEL-----RRRIGMLFQGgalfd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 --SVR-----------HLLHQKIRDSymhpqfmsdVMKPLQ------IEQLMDQEvvnLSGGELQRVAL--TLCLgKPaD 487
Cdd:COG1127 96 slTVFenvafplrehtDLSEAEIREL---------VLEKLElvglpgAADKMPSE---LSGGMRKRVALarALAL-DP-E 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 488 IYLIDEPSAYLDseqrIVASKVIKRFILHAKK----TAFVVEHDFIMATYLADRVIV-YEGQ 544
Cdd:COG1127 162 ILLYDEPTAGLD----PITSAVIDELIRELRDelglTSVVVTHDLDSAFAIADRVAVlADGK 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
101-281 |
9.74e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 67.76 E-value: 9.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT---------SPPDwqeiLTHFRGSEL----QNY-----FTriLED 162
Cdd:COG1136 32 EAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdisslSERE----LARLRRRHIgfvfQFFnllpeLT--ALE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 163 NlkaIIKPQYVDHIPRAvkgnvgevldqkdERDKKA-ELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFD 241
Cdd:COG1136 106 N---VALPLLLAGVSRK-------------ERRERArELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILAD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22328793 242 EPSSYLDVKQrlkAAQVVRSLLRPNSY----VIVVEHDLSVLDY 281
Cdd:COG1136 170 EPTGNLDSKT---GEEVLELLRELNRElgttIVMVTHDPELAAR 210
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
361-546 |
1.58e-12 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 68.23 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDDTE----GPDREIPEfNVSYKPQKISPKFQN-------- 428
Cdd:TIGR04520 20 NVSLSIEKGEF-----VAIIGHNGSGKSTLAKLLNGLLLPTSGKvtvdGLDTLDEE-NLWEIRKKVGMVFQNpdnqfvga 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 SVRH----------LLHQKIRdsymhpQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVAL--TLCLgKPaDIYLIDEPSA 496
Cdd:TIGR04520 94 TVEDdvafglenlgVPREEMR------KRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIagVLAM-RP-DIIILDEATS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 497 YLDSEQRIVASKVIKRfiLHAK--KTAFVVEHDFIMATyLADRVIV-------YEGQPS 546
Cdd:TIGR04520 166 MLDPKGRKEVLETIRK--LNKEegITVISITHDMEEAV-LADRVIVmnkgkivAEGTPR 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
364-539 |
1.64e-12 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 67.38 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDD----------TEGPDRE------------------IPEFNV 415
Cdd:COG1136 29 LSIEAGEF-----VAIVGPSGSGKSTLLNILGGLDRPTSgevlidgqdiSSLSERElarlrrrhigfvfqffnlLPELTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 416 sykpqkispkFQNsVRH-LLHQKIRDSYMHPQFMsDVMKPLQIEQLMDQEVVNLSGGELQRV----ALtlcLGKPAdIYL 490
Cdd:COG1136 104 ----------LEN-VALpLLLAGVSRKERRERAR-ELLERVGLGDRLDHRPSQLSGGQQQRVaiarAL---VNRPK-LIL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22328793 491 IDEPSAYLDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYlADRVI 539
Cdd:COG1136 168 ADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVI 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
77-284 |
1.65e-12 |
|
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: 66.06 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 77 RDLEKDTTHRYGANTFKLHrlpVPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSELQ--N 154
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLN---IEA-GEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL-----------IDGEDLTdlE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 155 YFTRILEDNLKAII-KPQYVDHipRAVKGNVGEVLdqkderdkkaelcadlelnqvidrdvenlSGGELQRFAIAVVAIQ 233
Cdd:cd03229 69 DELPPLRRRIGMVFqDFALFPH--LTVLENIALGL-----------------------------SGGQQQRVALARALAM 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22328793 234 NAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSY-VIVVEHDLSVLDYLSD 284
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGItVVLVTHDLDEAARLAD 169
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
101-276 |
1.75e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.56 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGkLKPNLGRF----TSPPDW--QEiLTHFRGselqnYFTrilEDNLKAIIKP--QY 172
Cdd:COG4138 20 NAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEIllngRPLSDWsaAE-LARHRA-----YLS---QQQSPPFAMPvfQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 173 VD-HIPR-AVKGNVGEVLdqkderdkkAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQ-------NAEIYMFDEP 243
Cdd:COG4138 90 LAlHQPAgASSEAVEQLL---------AQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|...
gi 22328793 244 SSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDL 276
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQGITVVMSSHDL 193
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
81-289 |
1.80e-12 |
|
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: 67.05 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANTFKLHRLPVPRP-GQVLGLVGTNGIGKSTALKILAGKLKPNLGrfTSPPDWQEiLTHFRGSELQnYFTR- 158
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISaGEFVFLVGPSGAGKSTLLKLIYKEELPTSG--TIRVNGQD-VSDLRGRAIP-YLRRk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 159 ---ILEDNL---------KAIIKPQYVDHIPRAVKGNVGEVLDQKDERDKKAELCADLelnqvidrdvenlSGGELQRFA 226
Cdd:cd03292 80 igvVFQDFRllpdrnvyeNVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAEL-------------SGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 227 IAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCL 289
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
351-540 |
2.05e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.96 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 351 KYPTMTKTQGNFRLRVSEGeftdsQIIVMLGENGTGKTTFIRMLAGLlkPDDTEGPDReipeFN------VSYKPQKISP 424
Cdd:PRK10851 10 KSFGRTQVLNDISLDIPSG-----QMVALLGPSGSGKTTLLRIIAGL--EHQTSGHIR----FHgtdvsrLHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 425 KFQNSV--RHL------------LHQKIR-DSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIY 489
Cdd:PRK10851 79 VFQHYAlfRHMtvfdniafgltvLPRRERpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 490 LIDEPSAYLDSEQRivasKVIKRFI--LHA--KKTAFVVEHDFIMATYLADRVIV 540
Cdd:PRK10851 159 LLDEPFGALDAQVR----KELRRWLrqLHEelKFTSVFVTHDQEEAMEVADRVVV 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
101-292 |
2.26e-12 |
|
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: 67.14 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEIlTHFRGSELQNYFTRI--------LEDNLkaiikpqy 172
Cdd:cd03261 24 RRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI--DGEDI-SGLSEAELYRLRRRMgmlfqsgaLFDSL-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 173 vdhiprAVKGNVGEVLDQ-----KDERDKKAELCADL-ELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSY 246
Cdd:cd03261 93 ------TVFENVAFPLREhtrlsEEEIREIVLEKLEAvGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22328793 247 LDVKQRLKAAQVVRSLLR-PNSYVIVVEHDLSVLDYLSDFICCLYGK 292
Cdd:cd03261 167 LDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDG 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
352-546 |
2.40e-12 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 66.94 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 352 YPTMTKTQGNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPD--DTEGPDREIPEFNVSYKPQ---KISPKF 426
Cdd:TIGR02315 11 YPNGKQALKNINLNINPGEF-----VAIIGPSGAGKSTLLRCINRLVEPSsgSILLEGTDITKLRGKKLRKlrrRIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 427 QN-------SV-RHLLHQkiRDSYMHP------QFM-SDVMKPLQ------IEQLMDQEVVNLSGGELQRVALTLCLGKP 485
Cdd:TIGR02315 86 QHynlierlTVlENVLHG--RLGYKPTwrsllgRFSeEDKERALSalervgLADKAYQRADQLSGGQQQRVAIARALAQQ 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328793 486 ADIYLIDEPSAYLDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRV-------IVYEGQPS 546
Cdd:TIGR02315 164 PDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIvglkageIVFDGAPS 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
101-276 |
2.84e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 67.06 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT---------SPpdWQeiLTHFRG-----SELQNYFTrILEdnlka 166
Cdd:COG4559 25 RPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngrplaawSP--WE--LARRRAvlpqhSSLAFPFT-VEE----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 167 II---------KPQYVDHIPRavkgnvgEVLDQKDerdkkaelCADLElnqviDRDVENLSGGELQRFAIAVVAIQ---- 233
Cdd:COG4559 95 VValgraphgsSAAQDRQIVR-------EALALVG--------LAHLA-----GRSYQTLSGGEQQRVQLARVLAQlwep 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22328793 234 --NAEIYMF-DEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDL 276
Cdd:COG4559 155 vdGGPRWLFlDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDL 200
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
351-544 |
2.88e-12 |
|
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: 66.94 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 351 KYPTMTKTQGNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDDTE----GPD-REIPEF----NVSYKPQK 421
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEF-----LVLIGPSGSGKTTTMKMINRLIEPTSGEifidGEDiREQDPVelrrKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 422 IS--PKF---QN--SVRHLLH---QKIRDSYMhpQFMSDVmkPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLI 491
Cdd:cd03295 84 IGlfPHMtveENiaLVPKLLKwpkEKIRERAD--ELLALV--GLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22328793 492 DEPSAYLDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADR-VIVYEGQ 544
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRiAIMKNGE 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
356-540 |
3.47e-12 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 68.20 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 356 TKTQGNFRLRVSEgEFTDSQIIVMLGENGTGKTTFIRMLAGLLKPD------------DTEGpdreipefNVSYKPQK-- 421
Cdd:COG4148 8 RLRRGGFTLDVDF-TLPGRGVTALFGPSGSGKTTLLRAIAGLERPDsgrirlggevlqDSAR--------GIFLPPHRrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 422 ISPKFQN-------SVRHLL---HQKIRDSYMHPQFmSDVMKPLQIEQLMDQEVVNLSGGELQRVAL--TLcLGKPaDIY 489
Cdd:COG4148 79 IGYVFQEarlfphlSVRGNLlygRKRAPRAERRISF-DEVVELLGIGHLLDRRPATLSGGERQRVAIgrAL-LSSP-RLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 490 LIDEPSAYLDseqriVASK---------VIKRF---ILHakktafvVEHDFIMATYLADRVIV 540
Cdd:COG4148 156 LMDEPLAALD-----LARKaeilpylerLRDELdipILY-------VSHSLDEVARLADHVVL 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
350-563 |
4.16e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.93 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 350 YKYPTMTKTQGNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDDTEGPDREIPEFNVSYKP---QKISPKF 426
Cdd:PRK13644 9 YSYPDGTPALENINLVIKKGEY-----IGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgirKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 427 QNSVRHLLHQKI-RDSYMHPQFMsdVMKPLQIEQLMDQEVV-------------NLSGGELQRVALTLCLGKPADIYLID 492
Cdd:PRK13644 84 QNPETQFVGRTVeEDLAFGPENL--CLPPIEIRKRVDRALAeiglekyrhrspkTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 493 EPSAYLDSEQRIVASKVIKRfiLHAK-KTAFVVEHDfIMATYLADRVIVYE-GQPSIDCTancPQSLLSGMNL 563
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKK--LHEKgKTIVYITHN-LEELHDADRIIVMDrGKIVLEGE---PENVLSDVSL 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
361-545 |
4.24e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 65.95 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDD----------TE-GPDREIPEFNVSYKP-----QKISP 424
Cdd:TIGR01184 3 GVNLTIQQGEF-----ISLIGHSGCGKSTLLNLISGLAQPTSggvilegkqiTEpGPDRMVVFQNYSLLPwltvrENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 425 KFqNSVRHLLHQKIRDsymhpQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRI 504
Cdd:TIGR01184 78 AV-DRVLPDLSKSERR-----AIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22328793 505 VASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIVYEGQP 545
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGP 192
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
101-279 |
4.52e-12 |
|
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: 68.85 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT---------SPPDWQEILTH-------FRGSELQNyftrilednl 164
Cdd:TIGR02857 346 PPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladaDADSWRDQIAWvpqhpflFAGTIAEN---------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 165 kaiikpqyvdhIPRAVKGNVGEVLDQKDERDKKAELCADLE--LNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDE 242
Cdd:TIGR02857 416 -----------IRLARPDASDAEIREALERAGLDEFVAALPqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
170 180 190
....*....|....*....|....*....|....*....
gi 22328793 243 PSSYLDvkqRLKAAQVVRSL--LRPNSYVIVVEHDLSVL 279
Cdd:TIGR02857 485 PTAHLD---AETEAEVLEALraLAQGRTVLLVTHRLALA 520
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
350-546 |
4.65e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.96 E-value: 4.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 350 YKYPTMTK-TQGNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPD--DTEGPDREIPEFNVSYKPQKISPKF 426
Cdd:PRK13635 13 FRYPDAATyALKDVSFSVYEGEW-----VAIVGHNGSGKSTLAKLLNGLLLPEagTITVGGMVLSEETVWDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 427 QN--------SVRH-----LLHQKIRDSYMHPQfMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDE 493
Cdd:PRK13635 88 QNpdnqfvgaTVQDdvafgLENIGVPREEMVER-VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 494 PSAYLDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYlADRVIVY-------EGQPS 546
Cdd:PRK13635 167 ATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMnkgeileEGTPE 225
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
364-540 |
4.74e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.56 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLlkpDDTEGPDREIPEFNVSykpqKISPK-------FQN-------S 429
Cdd:PRK11650 25 LDVADGEF-----IVLVGPSGCGKSTLLRMVAGL---ERITSGEIWIGGRVVN----ELEPAdrdiamvFQNyalyphmS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 430 VRH-----LlhqKIRDsymhpqfMS---------DVMKPLQIEQLMDQEVVNLSGGELQRVAltlcLG-----KPAdIYL 490
Cdd:PRK11650 93 VREnmaygL---KIRG-------MPkaeieervaEAARILELEPLLDRKPRELSGGQRQRVA----MGraivrEPA-VFL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22328793 491 IDEPSAYLDSEQRiVASKV-IKRfiLHA--KKTAFVVEHDFIMATYLADRVIV 540
Cdd:PRK11650 158 FDEPLSNLDAKLR-VQMRLeIQR--LHRrlKTTSLYVTHDQVEAMTLADRVVV 207
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
81-297 |
5.67e-12 |
|
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: 65.38 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANT------FKLHRlpvprpGQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEIltHFRGSELQ- 153
Cdd:cd03269 4 ENVTKRFGRVTalddisFSVEK------GEIFGLLGPNGAGKTTTIRMILGIILPDSG---------EV--LFDGKPLDi 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 154 ---NYFTRILEDN---LKAIIKPQYVdHIPRaVKGnvgevLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAI 227
Cdd:cd03269 67 aarNRIGYLPEERglyPKMKVIDQLV-YLAQ-LKG-----LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 228 AVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCLY-GKPGAYG 297
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNkGRAVLYG 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
361-544 |
8.48e-12 |
|
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: 64.83 E-value: 8.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPddTEG----------PDREIPEFNVSYKPQK------ISP 424
Cdd:cd03263 20 DLSLNVYKGE-----IFGLLGHNGAGKTTTLKMLTGELRP--TSGtayingysirTDRKAARQSLGYCPQFdalfdeLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 425 ----KFQNSVRHLLHQKIRDSymhpqfMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDS 500
Cdd:cd03263 93 rehlRFYARLKGLPKSEIKEE------VELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22328793 501 EQRivasKVIKRFILHAKK--TAFVVEHDFIMATYLADRV-IVYEGQ 544
Cdd:cd03263 167 ASR----RAIWDLILEVRKgrSIILTTHSMDEAEALCDRIaIMSDGK 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
102-274 |
9.34e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.51 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPDwqeilthfrGSELQNYFTRIlednlkaiikpQYVDHiPRAVK 181
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---------DIDDPDVAEAC-----------HYLGH-RNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 182 GN--VGEVLD------QKDERDKKAELCAdLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVK-QR 252
Cdd:PRK13539 86 PAltVAENLEfwaaflGGEELDIAAALEA-VGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAaVA 164
|
170 180
....*....|....*....|..
gi 22328793 253 LKAAqVVRSLLRPNSYVIVVEH 274
Cdd:PRK13539 165 LFAE-LIRAHLAQGGIVIAATH 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
102-543 |
9.44e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAG---------KLKPNL--GRFTSPPDWQEILThFRG------SELQNYFTRILEDNL 164
Cdd:TIGR03719 30 PGAKIGVLGLNGAGKSTLLRIMAGvdkdfngeaRPQPGIkvGYLPQEPQLDPTKT-VREnveegvAEIKDALDRFNEISA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 165 K---------AIIKPQyvdhipravkGNVGEVLDQKD--ERDKKAELCAD-LELNQViDRDVENLSGGELQRFAIAVVAI 232
Cdd:TIGR03719 109 KyaepdadfdKLAAEQ----------AELQEIIDAADawDLDSQLEIAMDaLRCPPW-DADVTKLSGGERRRVALCRLLL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 233 QNAEIYMFDEPSSYLDvkqrlkaAQVV----RSLLRPNSYVIVVEHDLSVLDYLSDFICCL---YGKP--GAYgvvtlpf 303
Cdd:TIGR03719 178 SKPDMLLLDEPTNHLD-------AESVawleRHLQEYPGTVVAVTHDRYFLDNVAGWILELdrgRGIPweGNY------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 304 svreginiflAGFVPTENLRF----RDESLTFKVAETPQE------SAEEIQSYARY-KYPTMTKTQGNFRLRVSE---- 368
Cdd:TIGR03719 244 ----------SSWLEQKQKRLeqeeKEESARQKTLKRELEwvrqspKGRQAKSKARLaRYEELLSQEFQKRNETAEiyip 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 369 -GE---------------FTD-------------SQIIVMLGENGTGKTTFIRMLAGLLKPDdtEGPDREIPEFNVSYKP 419
Cdd:TIGR03719 314 pGPrlgdkvieaenltkaFGDklliddlsfklppGGIVGVIGPNGAGKSTLFRMITGQEQPD--SGTIEIGETVKLAYVD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 420 Q---KISPKfqNSVrhllHQKIRDSYmhpqfmsDVMKPLQIE------------QLMDQE--VVNLSGGELQRVALTLCL 482
Cdd:TIGR03719 392 QsrdALDPN--KTV----WEEISGGL-------DIIKLGKREipsrayvgrfnfKGSDQQkkVGQLSGGERNRVHLAKTL 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 483 GKPADIYLIDEPSAYLDSEqrivASKVIKRFILHAKKTAFVVEHDfimaTYLADRV----IVYEG 543
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVE----TLRALEEALLNFAGCAVVISHD----RWFLDRIathiLAFEG 515
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
102-527 |
1.18e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.50 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPDWQEILTHFRGSELQ----NYFT------RILEDNLKaIIKPQ 171
Cdd:PRK10636 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPqpalEYVIdgdreyRQLEAQLH-DANER 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 172 YVDHIPRAVKGNVgEVLDQKDERDKKAELCADLELNQV-IDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDvk 250
Cdd:PRK10636 105 NDGHAIATIHGKL-DAIDAWTIRSRAASLLHGLGFSNEqLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD-- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 251 qrLKAAQVVRSLLRpnSY---VIVVEHDLSVLDYLSDFICCLYgkpgaygvvtlpfsvREGINIFLAGFVPTENLRFRDE 327
Cdd:PRK10636 182 --LDAVIWLEKWLK--SYqgtLILISHDRDFLDPIVDKIIHIE---------------QQSLFEYTGNYSSFEVQRATRL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 328 SLTFKVAETPQESAEEIQSYA-RYKYPTMTKTQGNFRLR------------------------------------VSEGe 370
Cdd:PRK10636 243 AQQQAMYESQQERVAHLQSYIdRFRAKATKAKQAQSRIKmlermeliapahvdnpfhfsfrapeslpnpllkmekVSAG- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 371 FTDSQI-------------IVMLGENGTGKTTFIRMLAGLLKPDDTE-GPDREI-----PEFNVSYKPQKISPkFQNSVR 431
Cdd:PRK10636 322 YGDRIIldsiklnlvpgsrIGLLGRNGAGKSTLIKLLAGELAPVSGEiGLAKGIklgyfAQHQLEFLRADESP-LQHLAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 432 ---HLLHQKIRDSYMHPQFMSDVMKplqieqlmdQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASK 508
Cdd:PRK10636 401 lapQELEQKLRDYLGGFGFQGDKVT---------EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE 471
|
490
....*....|....*....
gi 22328793 509 VIKRFilhaKKTAFVVEHD 527
Cdd:PRK10636 472 ALIDF----EGALVVVSHD 486
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
371-542 |
1.48e-11 |
|
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: 64.05 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 371 FTDSQIIVMLGENGTGKTTFIRMLAGLLKPDD----TEGPDREIPEfnVSYKPqkISPKFQ--NSVRHL---------LH 435
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSgrvlINGVDVTAAP--PADRP--VSMLFQenNLFAHLtveqnvglgLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 436 QKIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFIL 515
Cdd:cd03298 97 PGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176
|
170 180
....*....|....*....|....*..
gi 22328793 516 HAKKTAFVVEHDFIMATYLADRVIVYE 542
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLD 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
349-540 |
1.85e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 65.14 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 349 RYKYPTMTKTQGNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDD----TEGpdREIPEFNVSYKPQKISP 424
Cdd:PRK13650 13 KYKEDQEKYTLNDVSFHVKQGEW-----LSIIGHNGSGKSTTVRLIDGLLEAESgqiiIDG--DLLTEENVWDIRHKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 425 KFQNSVRHLLHQKIRDSYM---------HPQFMSDVMKPLQIEQLMD---QEVVNLSGGELQRVALTLCLGKPADIYLID 492
Cdd:PRK13650 86 VFQNPDNQFVGATVEDDVAfglenkgipHEEMKERVNEALELVGMQDfkeREPARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22328793 493 EPSAYLDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATyLADRVIV 540
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLV 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
352-542 |
1.97e-11 |
|
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: 63.97 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 352 YPTMTKTQGNFRLRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPddTEG------------PDREIPefnvsYKP 419
Cdd:cd03292 10 YPNGTAALDGINISISAGEFV-----FLVGPSGAGKSTLLKLIYKEELP--TSGtirvngqdvsdlRGRAIP-----YLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 420 QKISPKFQNSvRHLLHQKIRDSYMHPQFMSD---------VMKPLQIEQLMDQE---VVNLSGGELQRVALTLCLGKPAD 487
Cdd:cd03292 78 RKIGVVFQDF-RLLPDRNVYENVAFALEVTGvppreirkrVPAALELVGLSHKHralPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 488 IYLIDEPSAYLDSEQRIVASKVIKRFILhAKKTAFVVEHDFIMATYLADRVIVYE 542
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALE 210
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
101-276 |
2.03e-11 |
|
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: 66.62 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT--SPPDWQeilthFRGSELQ----------NYFTRILEDNLkAII 168
Cdd:TIGR02868 359 PPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldGVPVSS-----LDQDEVRrrvsvcaqdaHLFDTTVRENL-RLA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 169 KPQYVDHipravkgNVGEVLdqkdERDKKAELCADLE--LNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSY 246
Cdd:TIGR02868 433 RPDATDE-------ELWAAL----ERVGLADWLRALPdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180 190
....*....|....*....|....*....|..
gi 22328793 247 LDVKqrlKAAQVVRSLLRPNS--YVIVVEHDL 276
Cdd:TIGR02868 502 LDAE---TADELLEDLLAALSgrTVVLITHHL 530
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
364-544 |
2.21e-11 |
|
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: 64.06 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDDTE----GPDReipeFNVSYKPQKISPK-----FQN------ 428
Cdd:cd03261 21 LDVRRGE-----ILAIIGPSGSGKSTLLRLIVGLLRPDSGEvlidGEDI----SGLSEAELYRLRRrmgmlFQSgalfds 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 -SVR---------H--LLHQKIRDSymhpqfmsdVMKPLQ------IEQLMDQEvvnLSGGELQRVAL--TLCLgKPaDI 488
Cdd:cd03261 92 lTVFenvafplreHtrLSEEEIREI---------VLEKLEavglrgAEDLYPAE---LSGGMKKRVALarALAL-DP-EL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 489 YLIDEPSAYLDSeqriVASKVIKRFILHAKK----TAFVVEHDFIMATYLADRVIV-YEGQ 544
Cdd:cd03261 158 LLYDEPTAGLDP----IASGVIDDLIRSLKKelglTSIMVTHDLDTAFAIADRIAVlYDGK 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
355-545 |
2.25e-11 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 63.93 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 355 MTKTQGNFR------LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDDTE----GPD-----REIPEfNVSYKP 419
Cdd:cd03265 6 LVKKYGDFEavrgvsFRVRRGE-----IFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaGHDvvrepREVRR-RIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 420 QKIS-----PKFQNSvrhLLHQKIrdsYMHP-----QFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIY 489
Cdd:cd03265 80 QDLSvddelTGWENL---YIHARL---YGVPgaerrERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 490 LIDEPSAYLDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRV-------IVYEGQP 545
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVaiidhgrIIAEGTP 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
101-286 |
2.43e-11 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 63.54 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeILTHFRGSELQNYFTRILednlkaiIKPQY--VD---- 174
Cdd:cd03265 24 RRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-------VAGHDVVREPREVRRRIG-------IVFQDlsVDdelt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 175 -----HIPRAVKGNVGEVLDQKDErdkkaELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDV 249
Cdd:cd03265 90 gwenlYIHARLYGVPGAERRERID-----ELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 22328793 250 KQRLKAAQVVRSLLR-PNSYVIVVEHDLSVLDYLSDFI 286
Cdd:cd03265 165 QTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRV 202
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
375-531 |
2.93e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.98 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 375 QIIVMLGENGTGKTTFIRMLAGLLKPDdtEGPDREIPEFNVSYKPQKIS--PKFQNSVRH--LLHQKIRDSYMHPqfmsd 450
Cdd:PRK09544 31 KILTLLGPNGAGKSTLVRVVLGLVAPD--EGVIKRNGKLRIGYVPQKLYldTTLPLTVNRflRLRPGTKKEDILP----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 451 VMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFILHAKKTAFVVEHD--F 528
Cdd:PRK09544 104 ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDlhL 183
|
...
gi 22328793 529 IMA 531
Cdd:PRK09544 184 VMA 186
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
101-546 |
2.97e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPDWQEILTHFRGSELQnyfTRILEDNLKAI-----IKPQYVDH 175
Cdd:PRK09700 29 YPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG---IGIIYQELSVIdeltvLENLYIGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 176 IP-RAVKGNvgEVLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLK 254
Cdd:PRK09700 106 HLtKKVCGV--NIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 255 AAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCLygKPGAYGVVTLPFSVR-EGINIFLAGfvptENLRFRDESLTFKV 333
Cdd:PRK09700 184 LFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVM--KDGSSVCSGMVSDVSnDDIVRLMVG----RELQNRFNAMKENV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 334 AETPQESAEEIQSYARYKYptmtKTQGNFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDDTE----GPD-- 407
Cdd:PRK09700 258 SNLAHETVFEVRNVTSRDR----KKVRDISFSVCRGE-----ILGFAGLVGSGRTELMNCLFGVDKRAGGEirlnGKDis 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 408 -------------------RE---IPEF----NVSYKPQKISPKFQNSVrHLLHQKirdsyMHPQFMSDVMKPLQIE-QL 460
Cdd:PRK09700 329 prspldavkkgmayitesrRDngfFPNFsiaqNMAISRSLKDGGYKGAM-GLFHEV-----DEQRTAENQRELLALKcHS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 461 MDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIkRFILHAKKTAFVVEHDF--IMAtyLADRV 538
Cdd:PRK09700 403 VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVM-RQLADDGKVILMVSSELpeIIT--VCDRI 479
|
....*....
gi 22328793 539 IVY-EGQPS 546
Cdd:PRK09700 480 AVFcEGRLT 488
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
101-276 |
3.07e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.80 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGkLKPNLG--RFTSPPdwqeiLTHFRGSELQNYFTRILEDNLKAIIKP--QYVD-H 175
Cdd:PRK03695 20 RAGEILHLVGPNGAGKSTLLARMAG-LLPGSGsiQFAGQP-----LEAWSAAELARHRAYLSQQQTPPFAMPvfQYLTlH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 176 IP-RAVKGNVGEVLDqkderdkkaELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQ-------NAEIYMFDEPSSYL 247
Cdd:PRK03695 94 QPdKTRTEAVASALN---------EVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSL 164
|
170 180
....*....|....*....|....*....
gi 22328793 248 DVKQRLKAAQVVRSLLRPNSYVIVVEHDL 276
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQGIAVVMSSHDL 193
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
361-540 |
3.11e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 65.12 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDdtEGP----DREI----PE-------------F------ 413
Cdd:COG3842 23 DVSLSIEPGEF-----VALLGPSGCGKTTLLRMIAGFETPD--SGRilldGRDVtglpPEkrnvgmvfqdyalFphltva 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 414 -NVSY--KPQKISPKFQNS-VRHLLHQkirdsymhpqfmsdvmkpLQIEQLMDQEVVNLSGGELQRVAL--TLCLgKPaD 487
Cdd:COG3842 96 eNVAFglRMRGVPKAEIRArVAELLEL------------------VGLEGLADRYPHQLSGGQQQRVALarALAP-EP-R 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 488 IYLIDEP-SAyLDSEQRIVASKVIKRfILHAKKTAFV-VEHDFIMATYLADRVIV 540
Cdd:COG3842 156 VLLLDEPlSA-LDAKLREEMREELRR-LQRELGITFIyVTHDQEEALALADRIAV 208
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
210-297 |
3.16e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 62.34 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 210 IDRDVENLSGGELQRFAIAVVAIQNAE--IYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYlSDFIC 287
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWII 159
|
90
....*....|
gi 22328793 288 CLYGKPGAYG 297
Cdd:cd03238 160 DFGPGSGKSG 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
101-544 |
3.19e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGkLKPNlgrftspPDWQ-EIltHFRGSELQNYFTRILEDNLKAIIKpQYVDHIPR- 178
Cdd:TIGR02633 25 RPGECVGLCGENGAGKSTLMKILSG-VYPH-------GTWDgEI--YWSGSPLKASNIRDTERAGIVIIH-QELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 179 AVKGNV---------GEVLDQKDERDKKAELCADLELNQVID-RDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLD 248
Cdd:TIGR02633 94 SVAENIflgneitlpGGRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 249 VKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICClygkpgaygvvtlpfsVREGINIflaGFVPTENLRfRDES 328
Cdd:TIGR02633 174 EKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICV----------------IRDGQHV---ATKDMSTMS-EDDI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 329 LTFKVAE--------TPQESAEEIqsyARYKYPTMTKTQGNFRLRVSEGEFT--DSQIIVMLGENGTGKTTFIRMLAGLL 398
Cdd:TIGR02633 234 ITMMVGReitslyphEPHEIGDVI---LEARNLTCWDVINPHRKRVDDVSFSlrRGEILGVAGLVGAGRTELVQALFGAY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 399 ------------KPDDTEGPDREI-------PEfnvSYKPQKISPKF---QN---SVRHLLHQKIR-DSYMHPQFMSDVM 452
Cdd:TIGR02633 311 pgkfegnvfingKPVDIRNPAQAIragiamvPE---DRKRHGIVPILgvgKNitlSVLKSFCFKMRiDAAAELQIIGSAI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 453 KPLQIEQLM-DQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIkrFILHAKKTAF-VVEHDFIM 530
Cdd:TIGR02633 388 QRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLI--NQLAQEGVAIiVVSSELAE 465
|
490
....*....|....*
gi 22328793 531 ATYLADRVIV-YEGQ 544
Cdd:TIGR02633 466 VLGLSDRVLViGEGK 480
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
91-277 |
3.39e-11 |
|
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: 63.26 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 91 TFKLHrlpvprPGQVLGLVGTNGIGKSTALKILAgklkpnlgRFTSPPDWQEILThfrGSELQNYFTRILEDNLKAIIK- 169
Cdd:cd03248 34 SFTLH------PGEVTALVGPSGSGKSTVVALLE--------NFYQPQGGQVLLD---GKPISQYEHKYLHSKVSLVGQe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 170 PQYvdhIPRAVKGNVGEVLDQK-DERDKKAELCAD-----LELNQVIDRDVEN----LSGGELQRFAIAVVAIQNAEIYM 239
Cdd:cd03248 97 PVL---FARSLQDNIAYGLQSCsFECVKEAAQKAHahsfiSELASGYDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 22328793 240 FDEPSSYLDVKQRLKAAQVVRSLLRPNSyVIVVEHDLS 277
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPERRT-VLVIAHRLS 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
364-554 |
4.45e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.54 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDDTE-----GPDREIPEfnvsykpqKISPKFQNSvRHLLHQKI 438
Cdd:PRK11247 33 LHIPAGQF-----VAVVGRSGCGKSTLLRLLAGLETPSAGEllagtAPLAEARE--------DTRLMFQDA-RLLPWKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 439 RDSY---MHPQFMSDVMKPLQIEQLMDQEV---VNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKR 512
Cdd:PRK11247 99 IDNVglgLKGQWRDAALQALAAVGLADRANewpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIES 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22328793 513 FILHAKKTAFVVEHDFIMATYLADRVIVYE-GQPSIDCTANCP 554
Cdd:PRK11247 179 LWQQHGFTVLLVTHDVSEAVAMADRVLLIEeGKIGLDLTVDLP 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
81-275 |
4.90e-11 |
|
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: 62.66 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGaNTFKLHRLPVPRP-GQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------TSPPDWQEILTHFrgse 151
Cdd:cd03301 4 ENVTKRFG-NVTALDDLNLDIAdGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtDLPPKDRDIAMVF---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 152 lQNYftrilednlkaIIKPQYvdhiprAVKGNVGEVLDQ----KDERDKKAELCAD-LELNQVIDRDVENLSGGELQRFA 226
Cdd:cd03301 79 -QNY-----------ALYPHM------TVYDNIAFGLKLrkvpKDEIDERVREVAElLQIEHLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22328793 227 IAVVAIQNAEIYMFDEPSSYLDVKQRLKA-AQVVRSLLRPNSYVIVVEHD 275
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMrAELKRLQQRLGTTTIYVTHD 190
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
103-276 |
5.18e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.47 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqeilthfrgsELQNYFTRILEDNLKAI-----IKPQYVDH-- 175
Cdd:PRK13632 35 GEYVAILGHNGSGKSTISKILTGLLKPQSG------------------EIKIDGITISKENLKEIrkkigIIFQNPDNqf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 176 IPRAVKGNVG-----EVLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVK 250
Cdd:PRK13632 97 IGATVEDDIAfglenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180
....*....|....*....|....*..
gi 22328793 251 QRLKAAQVVRSLLRPNS-YVIVVEHDL 276
Cdd:PRK13632 177 GKREIKKIMVDLRKTRKkTLISITHDM 203
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
9-72 |
6.13e-11 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 58.52 E-value: 6.13e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328793 9 AIVSSDRCKpkKCRqECKKSCPVvktgklcIEVTVGSKLAFISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG4231 17 YVIDEDKCT--GCG-ACVKVCPA-------DAIEEGDGKAVIDPDLCIGCGSCVQVCPVDAIKL 70
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
361-504 |
7.31e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.87 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRvsegeftDSQIIVMLGENGTGKTTFIRMLAGLLKpddTEGP----DREIPEFNVSYKPQKISPKFQNSvrHLLHQ 436
Cdd:PRK11174 370 NFTLP-------AGQRIALVGPSGAGKTSLLNALLGFLP---YQGSlkinGIELRELDPESWRKHLSWVGQNP--QLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 437 KIRDSYM--HPQfMSDVmkplQIEQLMDQEVVN--------------------LSGGELQRVALTLCLGKPADIYLIDEP 494
Cdd:PRK11174 438 TLRDNVLlgNPD-ASDE----QLQQALENAWVSeflpllpqgldtpigdqaagLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170
....*....|..
gi 22328793 495 SAYLD--SEQRI 504
Cdd:PRK11174 513 TASLDahSEQLV 524
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
364-546 |
7.65e-11 |
|
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: 62.07 E-value: 7.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKP----------DDTEGPDREIPEFNVSYKPQ--KIspkFQN-SV 430
Cdd:cd03224 21 LTVPEGE-----IVALLGRNGAGKTTLLKTIMGLLPPrsgsirfdgrDITGLPPHERARAGIGYVPEgrRI---FPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 431 RHLLH---QKIRDSymHPQFMSDVMKPL--QIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLdseqriv 505
Cdd:cd03224 93 EENLLlgaYARRRA--KRKARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL------- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22328793 506 ASKVIKRFI-----LHAKKTA-FVVEHDFIMATYLADRV-------IVYEGQPS 546
Cdd:cd03224 164 APKIVEEIFeaireLRDEGVTiLLVEQNARFALEIADRAyvlergrVVLEGTAA 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
379-540 |
9.27e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.90 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 379 MLGENGTGKTTFIRMLAGLLKPDDTEGPDREIPEFNVSYKP-----QKISPKFQNSVRHLLHQKIRDSYM---------H 444
Cdd:PRK13640 38 LIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTvwdirEKVGIVFQNPDNQFVGATVGDDVAfglenravpR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 445 PQFMS---DVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFILHAKKTA 521
Cdd:PRK13640 118 PEMIKivrDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTV 197
|
170
....*....|....*....
gi 22328793 522 FVVEHDFIMATyLADRVIV 540
Cdd:PRK13640 198 ISITHDIDEAN-MADQVLV 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
364-543 |
9.75e-11 |
|
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: 61.72 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFTdsqIIVmlGENGTGKTTFIRMLAGLLKPddTEGpDREIPEfNVSYKPQkiSPKFQN-SVRhllhQKIR-DS 441
Cdd:cd03250 26 LEVPKGELV---AIV--GPVGSGKSSLLSALLGELEK--LSG-SVSVPG-SIAYVSQ--EPWIQNgTIR----ENILfGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 442 YMHPQFMSDVMKPLQ----IEQLMDQ---EV----VNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEqriVASKVI 510
Cdd:cd03250 91 PFDEERYEKVIKACAlepdLEILPDGdltEIgekgINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH---VGRHIF 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 22328793 511 KRFILHA---KKTAFVVEH--DFIMAtylADRVIVYEG 543
Cdd:cd03250 168 ENCILGLllnNKTRILVTHqlQLLPH---ADQIVVLDN 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
344-551 |
1.08e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.70 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 344 IQSYARYKYPTMTKTQG------NFRLRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPDD----TEGpdREIPEF 413
Cdd:PRK10253 2 TESVARLRGEQLTLGYGkytvaeNLTVEIPDGHFT-----AIIGPNGCGKSTLLRTLSRLMTPAHghvwLDG--EHIQHY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 414 NVSYKPQKISPKFQN-------SVRHLLhqkIRDSYMH-PQF----------MSDVMKPLQIEQLMDQEVVNLSGGELQR 475
Cdd:PRK10253 75 ASKEVARRIGLLAQNattpgdiTVQELV---ARGRYPHqPLFtrwrkedeeaVTKAMQATGITHLADQSVDTLSGGQRQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 476 VALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLA-------DRVIVYEGQPSID 548
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYAshlialrEGKIVAQGAPKEI 231
|
...
gi 22328793 549 CTA 551
Cdd:PRK10253 232 VTA 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
379-595 |
1.09e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.87 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 379 MLGENGTGKTTFIRMLAGLLKPddTEGpDREIPEFNVSYKP---------QKISPKFQNSVRHLLHQKI-RDSYMHPQ-F 447
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKP--TTG-TVTVDDITITHKTkdkyirpvrKRIGMVFQFPESQLFEDTVeREIIFGPKnF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 448 MSDVMK------PLQIE-----QLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFILH 516
Cdd:PRK13646 115 KMNLDEvknyahRLLMDlgfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 517 AKKTAFVVEHDFIMATYLADRVIVY-EGQPSIDCTancPQSLLSGMNLFLS-HLNItfrrdptnfrPRINKLEstKDREQ 594
Cdd:PRK13646 195 ENKTIILVSHDMNEVARYADEVIVMkEGSIVSQTS---PKELFKDKKKLADwHIGL----------PEIVQLQ--YDFEQ 259
|
.
gi 22328793 595 K 595
Cdd:PRK13646 260 K 260
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
101-279 |
1.13e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.02 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRftsppdwqeILTHFR-------GSELQNYFTriLEDNLKAIikpqyv 173
Cdd:COG1134 50 ERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR---------VEVNGRvsallelGAGFHPELT--GRENIYLN------ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 174 dhipravkgnvGEVLD-QKDERDKKAELCADL-ELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQ 251
Cdd:COG1134 113 -----------GRLLGlSRKEIDEKFDEIVEFaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAF 181
|
170 180
....*....|....*....|....*...
gi 22328793 252 RLKAAQVVRSLLRPNSYVIVVEHDLSVL 279
Cdd:COG1134 182 QKKCLARIRELRESGRTVIFVSHSMGAV 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
81-303 |
1.16e-10 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 61.72 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANTFKLH-----RLPVPrPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSELQNY 155
Cdd:cd03293 4 RNVSKTYGGGGGAVTalediSLSVE-EGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVL-----------VDGEPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 156 FTRIL----EDNLkaiikpqyvdhIP-RAVKGNVGEVLDQKDERDKKAELCADLELNQVIDRDVEN-----LSGGELQRF 225
Cdd:cd03293 72 GPDRGyvfqQDAL-----------LPwLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENayphqLSGGMRQRV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 226 AIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLR-PNSYVIVVEHDLSVLDYLSDFICCLYGKPGAY-GVVTLPF 303
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWReTGKTVLLVTHDIDEAVFLADRVVVLSARPGRIvAEVEVDL 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
101-287 |
1.25e-10 |
|
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: 64.05 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FTSPPDWQEILThfRGSELQNYFTRILednlkAIIKPQYVDHIPR 178
Cdd:TIGR03269 308 KEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTK--PGPDGRGRAKRYI-----GILHQEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 179 AVKGNVGEV--LDQKDE---------------RDKKAElcadlelnQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFD 241
Cdd:TIGR03269 381 TVLDNLTEAigLELPDElarmkavitlkmvgfDEEKAE--------EILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22328793 242 EPSSYLDVKQRLKAAQ-VVRSLLRPNSYVIVVEHDlsvLDYLSDfIC 287
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHD---MDFVLD-VC 495
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
101-286 |
1.71e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 61.62 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAG--KLKPNLGrftsppdwqEILthFRGselQNyftrILEdnlkaiIKP-------- 170
Cdd:COG0396 24 KPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSG---------SIL--LDG---ED----ILE------LSPderaragi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 171 ----QYVDHIP---------RAVKGNVGEVLDQKDERDKKAELCADLELNQ-VIDRDV-ENLSGGELQRFAIAVVAIQNA 235
Cdd:COG0396 80 flafQYPVEIPgvsvsnflrTALNARRGEELSAREFLKLLKEKMKELGLDEdFLDRYVnEGFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22328793 236 EIYMFDEPSSYLDVkQRLKA-AQVVRSLLRPNSYVIVVEHDLSVLDYLS-DFI 286
Cdd:COG0396 160 KLAILDETDSGLDI-DALRIvAEGVNKLRSPDRGILIITHYQRILDYIKpDFV 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
81-277 |
1.95e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 61.69 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANT-FKLHRLPVPRP-GQVLGLVGTNGIGKSTALKILAGKLKPNLGRF------TSPPDWQEILTHFrGSEL 152
Cdd:PRK13648 11 KNVSFQYQSDAsFTLKDVSFNIPkGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFEKLRKHI-GIVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 153 QNyftrilEDNlkaiikpQYVDHIpraVKGNVGEVLDQ-----KDERDKKAELCADLELNQVIDRDVENLSGGELQRFAI 227
Cdd:PRK13648 90 QN------PDN-------QFVGSI---VKYDVAFGLENhavpyDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22328793 228 AVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIV-VEHDLS 277
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIIsITHDLS 204
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
82-284 |
2.24e-10 |
|
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: 61.74 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 82 DTTHRYGANTF--KLHRLPV-------PRPGQVLGLVGTNGIGKSTALKILAGKLKPNLG--RFTSPPdwqeiLTHFRGS 150
Cdd:TIGR02769 7 DVTHTYRTGGLfgAKQRAPVltnvslsIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGtvSFRGQD-----LYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 151 ELQNyFTR----ILEDNLKAIiKPQyvdhipRAVKGNVGE------VLDQKDERDKKAELCADLEL-NQVIDRDVENLSG 219
Cdd:TIGR02769 82 QRRA-FRRdvqlVFQDSPSAV-NPR------MTVRQIIGEplrhltSLDESEQKARIAELLDMVGLrSEDADKLPRQLSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328793 220 GELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPN--SYVIVVeHDLSVLDYLSD 284
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFgtAYLFIT-HDLRLVQSFCQ 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
103-290 |
2.48e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.03 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT---------SPPDWQEILthfrgSELQnyftRILEDNLKA------- 166
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgmKDDEWRAVR-----SDIQ----MIFQDPLASlnprmti 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 167 ---IIKP--QYVDHIPRAvkgnvgEVLDQKDERDKKAELcadleLNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFD 241
Cdd:PRK15079 118 geiIAEPlrTYHPKLSRQ------EVKDRVKAMMLKVGL-----LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22328793 242 EPSSYLDVKQRlkaAQVV---RSLLRPNSY-VIVVEHDLSVLDYLSDFICCLY 290
Cdd:PRK15079 187 EPVSALDVSIQ---AQVVnllQQLQREMGLsLIFIAHDLAVVKHISDRVLVMY 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
101-290 |
2.86e-10 |
|
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: 60.23 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAG--KLKPNLGRftsppdwqeILthFRGSELQNyftriLEDNLKA----IIKPQYvd 174
Cdd:cd03217 24 KKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGE---------IL--FKGEDITD-----LPPEERArlgiFLAFQY-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 175 hiPRAVKG-NVGEVLdqkderdkkaelcadlelnqvidRDV-ENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQR 252
Cdd:cd03217 86 --PPEIPGvKNADFL-----------------------RYVnEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 22328793 253 LKAAQVVRSLLRPNSYVIVVEHDLSVLDYL-SDFICCLY 290
Cdd:cd03217 141 RLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLY 179
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
103-274 |
3.37e-10 |
|
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: 60.36 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLkPNLGRFT----------SPPDWQEILTHFRGSE-LQNYFTriLEDNLK--AIIK 169
Cdd:cd03234 33 GQVMAILGSSGSGKTTLLDAISGRV-EGGGTTSgqilfngqprKPDQFQKCVAYVRQDDiLLPGLT--VRETLTytAILR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 170 PQYvdHIPRAVKGNVGEVLDQKDerdkkaelCADLelnQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDV 249
Cdd:cd03234 110 LPR--KSSDAIRKKRVEDVLLRD--------LALT---RIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180
....*....|....*....|....*
gi 22328793 250 KQRLKAAQVVRSLLRPNSYVIVVEH 274
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIH 201
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
101-344 |
3.51e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.16 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR----------FTSPPDWQEIL-THFRGSELQnYFTRILEDNLKaiIK 169
Cdd:PRK13644 26 KKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKvlvsgidtgdFSKLQGIRKLVgIVFQNPETQ-FVGRTVEEDLA--FG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 170 PQYVDHIPRAVKGNVGEVLdqkderdkkaelcADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDV 249
Cdd:PRK13644 103 PENLCLPPIEIRKRVDRAL-------------AEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 250 KQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCLYGKPGAYGVvtlPFSVREGINIFLAGFVP------TENLR 323
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE---PENVLSDVSLQTLGLTPpslielAENLK 246
|
250 260
....*....|....*....|.
gi 22328793 324 FRDESLTFKVAETPQESAEEI 344
Cdd:PRK13644 247 MHGVVIPWENTSSPSSFAEEI 267
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
361-540 |
3.58e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 62.87 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFTdsqIIVmlGENGTGKTTFIRMLAGLLKPddTEGP----DREIPEFNVSYKPQKISPKFQNSvrHLLHQ 436
Cdd:COG1132 358 DISLTIPPGETV---ALV--GPSGSGKSTLVNLLLRFYDP--TSGRilidGVDIRDLTLESLRRQIGVVPQDT--FLFSG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 437 KIRD--SYMHPQF-MSDVMKPLQ-------IEQL---MDQEV----VNLSGGELQRVAL--TLClgKPADIYLIDEPSAY 497
Cdd:COG1132 429 TIREniRYGRPDAtDEEVEEAAKaaqahefIEALpdgYDTVVgergVNLSGGQRQRIAIarALL--KDPPILILDEATSA 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22328793 498 LD--SEQRIVASkvIKRfiLHAKKTAFVVEHDF--IMAtylADRVIV 540
Cdd:COG1132 507 LDteTEALIQEA--LER--LMKGRTTIVIAHRLstIRN---ADRILV 546
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
352-546 |
3.64e-10 |
|
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: 60.66 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 352 YPTMTKTQGNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPddTEGpdreipefNVSYKPQKI---SPKFQN 428
Cdd:cd03256 10 YPNGKKALKDVSLSINPGEF-----VALIGPSGAGKSTLLRCLNGLVEP--TSG--------SVLIDGTDInklKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 SVRH---LLHQKI---------------RDSYMHP-----QFMSDVMKPLQIEQLMD--------QEVVNLSGGELQRVA 477
Cdd:cd03256 75 QLRRqigMIFQQFnlierlsvlenvlsgRLGRRSTwrslfGLFPKEEKQRALAALERvglldkayQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328793 478 LTLCLGKPADIYLIDEPSAYLDSE-QRIVASkVIKRFILHAKKTAFVVEHDFIMATYLADRV-------IVYEGQPS 546
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPAsSRQVMD-LLKRINREEGITVIVSLHQVDLAREYADRIvglkdgrIVFDGPPA 230
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
9-72 |
3.72e-10 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 56.28 E-value: 3.72e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328793 9 AIVSSDRCKpkKCRQeCKKSCPVvktgkLCIEVTVGSklAFISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG2768 6 PYVDEEKCI--GCGA-CVKVCPV-----GAISIEDGK--AVIDPEKCIGCGACIEVCPVGAIKI 59
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
101-277 |
4.42e-10 |
|
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: 60.19 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------TSPPDWqeiLTHFRGSELQN--YFTRILEDNLkAIIKP 170
Cdd:cd03252 26 KPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaLADPAW---LRRQVGVVLQEnvLFNRSIRDNI-ALADP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 171 QYVDHipravkgNVGEVLDQKDERDKKAELcaDLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVK 250
Cdd:cd03252 102 GMSME-------RVIEAAKLAGAHDFISEL--PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180
....*....|....*....|....*..
gi 22328793 251 QRLKAAQVVRSLLRpNSYVIVVEHDLS 277
Cdd:cd03252 173 SEHAIMRNMHDICA-GRTVIIIAHRLS 198
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
84-276 |
4.88e-10 |
|
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: 58.59 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 84 THRYGAN------TFKLhrlpvpRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEILthfrgselqnyft 157
Cdd:cd03216 7 TKRFGGVkaldgvSLSV------RRGEVHALLGENGAGKSTLMKILSGLYKPDSG---------EIL------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 158 rilednlkaiikpqyvdhipraVKGNVGEVLDQKDERDKKAELcadlelnqvidrdVENLSGGELQRFAIAVVAIQNAEI 237
Cdd:cd03216 59 ----------------------VDGKEVSFASPRDARRAGIAM-------------VYQLSVGERQMVEIARALARNARL 103
|
170 180 190
....*....|....*....|....*....|....*....
gi 22328793 238 YMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDL 276
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRL 142
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
103-274 |
4.90e-10 |
|
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: 59.43 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPdwqEILTHFRGSELQNYFTRILEDNLKAIIKPQYVDHIPRAVKG 182
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---GPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 183 nvgevldqkdeRDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSL 262
Cdd:cd03231 103 -----------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170
....*....|..
gi 22328793 263 LRPNSYVIVVEH 274
Cdd:cd03231 172 CARGGMVVLTTH 183
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
87-297 |
5.87e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.39 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 87 YGANTFKlHRLPVPRP-GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFtsppdWQEilthfrGSELQNYFTR------- 158
Cdd:PRK10253 17 YGKYTVA-ENLTVEIPdGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-----WLD------GEHIQHYASKevarrig 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 159 ILEDN--------LKAIIKPQYVDHIPRAVKGnvgevldQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVV 230
Cdd:PRK10253 85 LLAQNattpgditVQELVARGRYPHQPLFTRW-------RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 231 AIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVI-VVEHDLS-VLDYLSDFICCLYGKPGAYG 297
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLaAVLHDLNqACRYASHLIALREGKIVAQG 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
79-284 |
9.08e-10 |
|
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: 60.51 E-value: 9.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 79 LEKDTTHRYGANTFKLhRLPVPRPGqVLGLVGTNGIGKSTALKILAGKLKPNLGRFtsppdwqeiltHFRGselqnyftR 158
Cdd:TIGR02142 1 LSARFSKRLGDFSLDA-DFTLPGQG-VTAIFGRSGSGKTTLIRLIAGLTRPDEGEI-----------VLNG--------R 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 159 ILEDNLKAIIKPQ------YVDHIPR-----AVKGNVGEVL---DQKDERDKKAELCADLELNQVIDRDVENLSGGELQR 224
Cdd:TIGR02142 60 TLFDSRKGIFLPPekrrigYVFQEARlfphlSVRGNLRYGMkraRPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 225 FAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRP-NSYVIVVEHDLSVLDYLSD 284
Cdd:TIGR02142 140 VAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLAD 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
381-543 |
1.07e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 61.23 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 381 GENGTGKTTFIRMLAGLLKPDDteGpdrEI---PEFNVSYKPQkiSPKF--QNSVRHL----------LHQKIRDSYMHP 445
Cdd:COG0488 31 GRNGAGKSTLLKILAGELEPDS--G---EVsipKGLRIGYLPQ--EPPLddDLTVLDTvldgdaelraLEAELEELEAKL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 446 QFMSDVMKPL-----------------QIEQLM----------DQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYL 498
Cdd:COG0488 104 AEPDEDLERLaelqeefealggweaeaRAEEILsglgfpeedlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22328793 499 DSEqrivaskVIK---RFILHAKKTAFVVEHD--FI--MATYLAD----RVIVYEG 543
Cdd:COG0488 184 DLE-------SIEwleEFLKNYPGTVLVVSHDryFLdrVATRILEldrgKLTLYPG 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
101-279 |
1.15e-09 |
|
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: 59.12 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdWQEI-LTHFRGSELQNYFTRI----LEDNLkaiIKPQYVdh 175
Cdd:cd03256 25 NPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL----IDGTdINKLKGKALRQLRRQIgmifQQFNL---IERLSV-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 176 IPRAVKGNVGEV--------LDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYL 247
Cdd:cd03256 96 LENVLSGRLGRRstwrslfgLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASL 175
|
170 180 190
....*....|....*....|....*....|..
gi 22328793 248 DVkqrlKAAQVVRSLLRPnsyvIVVEHDLSVL 279
Cdd:cd03256 176 DP----ASSRQVMDLLKR----INREEGITVI 199
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
375-544 |
1.24e-09 |
|
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: 58.73 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 375 QIIVMLGENGTGKTTFIRMLAGLLK-----PDDTE----GPDREIPEFNVSYKPQKISPKFQN------SVRH--LLHQK 437
Cdd:cd03260 27 EITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEvlldGKDIYDLDVDVLELRRRVGMVFQKpnpfpgSIYDnvAYGLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 438 IRDSYMHPQFMSDVMKPLQIEQLMDqEVVN------LSGGELQRVALTLCLGKPADIYLIDEPSAYLDSeqriVASKVIK 511
Cdd:cd03260 107 LHGIKLKEELDERVEEALRKAALWD-EVKDrlhalgLSGGQQQRLCLARALANEPEVLLLDEPTSALDP----ISTAKIE 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 22328793 512 RFILHAKK--TAFVVEHDFIMATYLADRVIV-YEGQ 544
Cdd:cd03260 182 ELIAELKKeyTIVIVTHNMQQAARVADRTAFlLNGR 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
84-247 |
1.27e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.81 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 84 THRYG---AN---TFKLhrlpvpRPGQVLGLVGTNGIGKSTALKILAGKLKPNLG---------RFTSPPD--------- 139
Cdd:COG3845 12 TKRFGgvvANddvSLTV------RPGEIHALLGENGAGKSTLMKILYGLYQPDSGeilidgkpvRIRSPRDaialgigmv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 140 WQeiltHFRgseLQNYFTrILEdNLkaIIkpqyvdhiprAVKGNVGEVLDQKDERDKKAELCADLELNQVIDRDVENLSG 219
Cdd:COG3845 86 HQ----HFM---LVPNLT-VAE-NI--VL----------GLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSV 144
|
170 180
....*....|....*....|....*...
gi 22328793 220 GELQRFAIAVVAIQNAEIYMFDEPSSYL 247
Cdd:COG3845 145 GEQQRVEILKALYRGARILILDEPTAVL 172
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
361-540 |
1.28e-09 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 60.94 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDdtEGP----DREIPEFN-------VSYKPQKIspkfqns 429
Cdd:COG4987 353 GLSLTLPPGE-----RVAIVGPSGSGKSTLLALLLRFLDPQ--SGSitlgGVDLRDLDeddlrrrIAVVPQRP------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 430 vrHLLHQKIRD---------SymhPQFMSDVMKPLQIEQLMDQEV-----------VNLSGGELQRVALTLCLGKPADIY 489
Cdd:COG4987 419 --HLFDTTLREnlrlarpdaT---DEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 490 LIDEPSAYLD--SEQRIVASkvikrfILHA--KKTAFVVEHDFIMATyLADRVIV 540
Cdd:COG4987 494 LLDEPTEGLDaaTEQALLAD------LLEAlaGRTVLLITHRLAGLE-RMDRILV 541
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
82-274 |
1.42e-09 |
|
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: 58.27 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 82 DTTHRYGANTFKLHrLPVPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT--------SPPDWQEILTHFRgselq 153
Cdd:cd03298 5 KIRFSYGEQPMHFD-LTFAQ-GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLingvdvtaAPPADRPVSMLFQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 154 nyftrilEDNLKAiikpqyvdHIprAVKGNVGEVLD-----QKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIA 228
Cdd:cd03298 78 -------ENNLFA--------HL--TVEQNVGLGLSpglklTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22328793 229 VVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSY-VIVVEH 274
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMtVLMVTH 187
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
350-542 |
1.43e-09 |
|
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: 57.71 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 350 YKYPTMTKTQ-GNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDDTEgpdREIPEFNVSykpqkispKFQN 428
Cdd:cd03247 8 FSYPEQEQQVlKNLSLELKQGEK-----IALLGRSGSGKSTLLQLLTGDLKPQQGE---ITLDGVPVS--------DLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 SVRHL---LHQKirdsymhPQFMSDVmkplqieqLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDseqRIV 505
Cdd:cd03247 72 ALSSLisvLNQR-------PYLFDTT--------LRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD---PIT 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 22328793 506 ASKVIKRFILHAK-KTAFVVEHDFIMATYlADRVIVYE 542
Cdd:cd03247 134 ERQLLSLIFEVLKdKTLIWITHHLTGIEH-MDKILFLE 170
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
355-499 |
1.44e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.89 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 355 MTKTQGNFRLRVSEgEFTDSQIIVMLGENGTGKTTFIRMLAGLLKPD------------DTEGpdreipefNVSYKPQK- 421
Cdd:PRK11144 6 FKQQLGDLCLTVNL-TLPAQGITAIFGRSGAGKTSLINAISGLTRPQkgrivlngrvlfDAEK--------GICLPPEKr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 422 -ISPKFQNSvRHLLHQKIR-------DSYMHPQFmSDVMKPLQIEQLMDQEVVNLSGGELQRVAL--TLcLGKPaDIYLI 491
Cdd:PRK11144 77 rIGYVFQDA-RLFPHYKVRgnlrygmAKSMVAQF-DKIVALLGIEPLLDRYPGSLSGGEKQRVAIgrAL-LTAP-ELLLM 152
|
....*...
gi 22328793 492 DEPSAYLD 499
Cdd:PRK11144 153 DEPLASLD 160
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
360-540 |
1.47e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.96 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 360 GNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDDTE----GPD-REIPefnvsykPQK--ISPKFQN---- 428
Cdd:PRK09452 31 SNLDLTINNGEF-----LTLLGPSGCGKTTVLRLIAGFETPDSGRimldGQDiTHVP-------AENrhVNTVFQSyalf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 ---SVRH-----LLHQKIRDSYMHPQFMsDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDS 500
Cdd:PRK09452 99 phmTVFEnvafgLRMQKTPAAEITPRVM-EALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 22328793 501 EQRIVASKVIKRfiLHAK-KTAFV-VEHDFIMATYLADRVIV 540
Cdd:PRK09452 178 KLRKQMQNELKA--LQRKlGITFVfVTHDQEEALTMSDRIVV 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
377-501 |
1.64e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 377 IVMLGENGTGKTTFIRMLAGLLKpdDTEGPDREIPEFNVSYKPQKisPKFQNS-------------VRHLLHQ--KIRDS 441
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDK--EFEGEARPAPGIKVGYLPQE--PQLDPEktvrenveegvaeVKAALDRfnEIYAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 442 YMHPQFMSDV----MKPLQ--------------IEQLM--------DQEVVNLSGGELQRVALT-LCLGKPaDIYLIDEP 494
Cdd:PRK11819 112 YAEPDADFDAlaaeQGELQeiidaadawdldsqLEIAMdalrcppwDAKVTKLSGGERRRVALCrLLLEKP-DMLLLDEP 190
|
....*..
gi 22328793 495 SAYLDSE 501
Cdd:PRK11819 191 TNHLDAE 197
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
361-542 |
1.69e-09 |
|
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: 58.31 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRvsEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPD----DTEGPDREIPEFNVSykpqkispkFQNS------- 429
Cdd:cd03220 42 SFEVP--RGE-----RIGLIGRNGAGKSTLLRLLAGIYPPDsgtvTVRGRVSSLLGLGGG---------FNPEltgreni 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 430 -VRHLLHqKIRDSYMHpQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASK 508
Cdd:cd03220 106 yLNGRLL-GLSRKEID-EKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190
....*....|....*....|....*....|....
gi 22328793 509 VIKRFILHAkKTAFVVEHDFIMATYLADRVIVYE 542
Cdd:cd03220 184 RLRELLKQG-KTVILVSHDPSSIKRLCDRALVLE 216
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
362-561 |
2.19e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.05 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 362 FRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDDTE----GPD-REIPEfnvSYKPqkISPKFQ--NSVRHL- 433
Cdd:PRK10771 18 FDLTVERGE-----RVAILGPSGAGKSTLLNLIAGFLTPASGSltlnGQDhTTTPP---SRRP--VSMLFQenNLFSHLt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 434 --------LHQKIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIV 505
Cdd:PRK10771 88 vaqniglgLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 506 ASKVIKRFILHAKKTAFVVEHDFIMATYLADRV-------IVYEGQPSIDCTANCPQSLLSGM 561
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSlvvadgrIAWDGPTDELLSGKASASALLGI 230
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
349-544 |
2.22e-09 |
|
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: 58.05 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 349 RYKYPTMTKtqgNFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDD----------TEGPDREIPEFNVSYK 418
Cdd:TIGR04406 10 SYKKRKVVN---DVSLSVKSGE-----IVGLLGPNGAGKTTSFYMIVGLVRPDAgkilidgqdiTHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 419 PQKISPKFQNSVRH-----LLHQKIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDE 493
Cdd:TIGR04406 82 PQEASIFRKLTVEEnimavLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 494 PSAYLDSeqriVASKVIKRFILHAKKTAFVV---EHDFIMATYLADRV-IVYEGQ 544
Cdd:TIGR04406 162 PFAGVDP----IAVGDIKKIIKHLKERGIGVlitDHNVRETLDICDRAyIISDGK 212
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
103-276 |
2.30e-09 |
|
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: 58.11 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFtsppdwqEILTHFRGSELQNYFTRIlednlkAII---KPQYVDHIPRA 179
Cdd:cd03267 47 GEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-------RVAGLVPWKRRKKFLRRI------GVVfgqKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 180 VKGNV-GEVLDQKDERDKK--AELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAA 256
Cdd:cd03267 114 DSFYLlAAIYDLPPARFKKrlDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
170 180
....*....|....*....|.
gi 22328793 257 QVVRSLLRP-NSYVIVVEHDL 276
Cdd:cd03267 194 NFLKEYNRErGTTVLLTSHYM 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
364-544 |
2.47e-09 |
|
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: 58.42 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKP----------DDTEGPDREIPEFnvsyKPQKISPKFQN----- 428
Cdd:cd03294 45 LDVREGE-----IFVIMGLSGSGKSTLLRCINRLIEPtsgkvlidgqDIAAMSRKELREL----RRKKISMVFQSfallp 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 ------------SVRHLLHQKIRDSYMHpqfmsdVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSA 496
Cdd:cd03294 116 hrtvlenvafglEVQGVPRAEREERAAE------ALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22328793 497 YLDSEQRIVASKVIKRfiLHAK--KTAFVVEHDFIMATYLADRV-IVYEGQ 544
Cdd:cd03294 190 ALDPLIRREMQDELLR--LQAElqKTIVFITHDLDEALRLGDRIaIMKDGR 238
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
66-277 |
2.89e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 59.79 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 66 PFEAIQIINLPRDLE-KDTTHRYGANTFKLHR--LPVPrPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT------- 135
Cdd:COG1132 327 PPGAVPLPPVRGEIEfENVSFSYPGDRPVLKDisLTIP-PGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvdir 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 136 --SPPDWQEILthfrGSELQNY--FTRILEDNLkAIIKPQYVDH-IPRAVK-GNVGEVLDQKDERdkkaelcadleLNQV 209
Cdd:COG1132 406 dlTLESLRRQI----GVVPQDTflFSGTIRENI-RYGRPDATDEeVEEAAKaAQAHEFIEALPDG-----------YDTV 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 210 IDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQrlkAAQVVRSL--LRPNSYVIVVEHDLS 277
Cdd:COG1132 470 VGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTET---EALIQEALerLMKGRTTIVIAHRLS 536
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
353-567 |
2.96e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.59 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 353 PTMTKTQGNFRLRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPddTEGPDR--EIPEFNVS----YKP--QKISP 424
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYT-----ALIGHTGSGKSTLLQHLNGLLQP--TEGKVTvgDIVVSSTSkqkeIKPvrKKVGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 425 KFQNSVRHLLHQKI-RDSYMHPQ---FMSDVMKPLQIEQL---------MDQEVVNLSGGELQRVALTLCLGKPADIYLI 491
Cdd:PRK13643 89 VFQFPESQLFEETVlKDVAFGPQnfgIPKEKAEKIAAEKLemvgladefWEKSPFELSGGQMRRVAIAGILAMEPEVLVL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22328793 492 DEPSAYLDSEQRIVASKVIKRfILHAKKTAFVVEHDFIMATYLADRVIVYEGQPSIDCtaNCPQSLLSGMNLFLSH 567
Cdd:PRK13643 169 DEPTAGLDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISC--GTPSDVFQEVDFLKAH 241
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
101-286 |
3.00e-09 |
|
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: 57.09 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPD--------WqeilthfrgseLQNyftrilednlkaiikpqy 172
Cdd:cd03250 29 PKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiayvsqepW-----------IQN------------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 173 vdhipRAVKGNV--GEVLDQkdERDKKA-ELCA---DLEL-----NQVI-DRDVeNLSGGELQRFAIAVVAIQNAEIYMF 240
Cdd:cd03250 80 -----GTIRENIlfGKPFDE--ERYEKViKACAlepDLEIlpdgdLTEIgEKGI-NLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22328793 241 DEPSSYLD--VKQRLkAAQVVRSLLRPNSYVIVVEHDLSVLDYlSDFI 286
Cdd:cd03250 152 DDPLSAVDahVGRHI-FENCILGLLLNNKTRILVTHQLQLLPH-ADQI 197
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
364-543 |
3.18e-09 |
|
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: 57.15 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPD---------DTEGPDREIPEFNvsykpQKISPKFQNSvrHLL 434
Cdd:cd03262 21 LTVKKGE-----VVVIIGPSGSGKSTLLRCINLLEEPDsgtiiidglKLTDDKKNINELR-----QKVGMVFQQF--NLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 435 -HQKIRDSYMHPQF----MSD------VMKPLQIEQLMDQEVV---NLSGGELQRVAL--TLCLgKPaDIYLIDEPSAYL 498
Cdd:cd03262 89 pHLTVLENITLAPIkvkgMSKaeaeerALELLEKVGLADKADAypaQLSGGQQQRVAIarALAM-NP-KVMLFDEPTSAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22328793 499 DSEQRIVASKVIKRfILHAKKTAFVVEHDFIMATYLADRVIVYEG 543
Cdd:cd03262 167 DPELVGEVLDVMKD-LAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
66-292 |
3.28e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 58.30 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 66 PFEAIQIINLprdlekdtthryganTFKLhrlpvpRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF----------T 135
Cdd:PRK13641 17 PMEKKGLDNI---------------SFEL------EEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhitpeT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 136 SPPDWQEILTH----FRGSELQNYFTRILEDnlkaiikpqyVDHIPRAVKGNVGEVLDQKDERDKKAELCADLelnqvID 211
Cdd:PRK13641 76 GNKNLKKLRKKvslvFQFPEAQLFENTVLKD----------VEFGPKNFGFSEDEAKEKALKWLKKVGLSEDL-----IS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 212 RDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDL-SVLDYLSDFICCLY 290
Cdd:PRK13641 141 KSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEH 220
|
..
gi 22328793 291 GK 292
Cdd:PRK13641 221 GK 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
101-287 |
3.29e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 58.58 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEILthFRGSELQnyftrilednlkaiikPQYVDHI---P 177
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTIRIILGILAPDSG---------EVL--WDGEPLD----------------PEDRRRIgylP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 178 --RAV--KGNVGEVL---------DQKDERDKKAELCADLELNQVIDRDVENLSGGELQR--FAIAVVAiqNAEIYMFDE 242
Cdd:COG4152 78 eeRGLypKMKVGEQLvylarlkglSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKvqLIAALLH--DPELLILDE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22328793 243 PSSYLD-VKQRLkAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFIC 287
Cdd:COG4152 156 PFSGLDpVNVEL-LKDVIRELAAKGTTVIFSSHQMELVEELCDRIV 200
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
101-279 |
3.33e-09 |
|
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: 56.46 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRftsppdwqeilthfrgselqnyftrILEDNlkAIIKPQYvdhiPRAV 180
Cdd:cd03246 26 EPGESLAIIGPSGSGKSTLARLILGLLRPTSGR-------------------------VRLDG--ADISQWD----PNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 181 KGNVGEVLdQKDErdkkaeLCADlELNQVIdrdvenLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVR 260
Cdd:cd03246 75 GDHVGYLP-QDDE------LFSG-SIAENI------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170
....*....|....*....
gi 22328793 261 SLLRPNSYVIVVEHDLSVL 279
Cdd:cd03246 141 ALKAAGATRIVIAHRPETL 159
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
361-539 |
3.41e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRvsEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPDDT----EGPD-----REIPEFNVSYKPQkiSPK-FQNSV 430
Cdd:PRK10247 27 SFSLR--AGEFK-----LITGPSGCGKSTLLKIVASLISPTSGtllfEGEDistlkPEIYRQQVSYCAQ--TPTlFGDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 431 RH--LLHQKIRDSYMHPQ-FMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVAS 507
Cdd:PRK10247 98 YDnlIFPWQIRNQQPDPAiFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVN 177
|
170 180 190
....*....|....*....|....*....|..
gi 22328793 508 KVIKRFILHAKKTAFVVEHDFIMATYlADRVI 539
Cdd:PRK10247 178 EIIHRYVREQNIAVLWVTHDKDEINH-ADKVI 208
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
7-73 |
4.12e-09 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 53.19 E-value: 4.12e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328793 7 RIAIVSSDRCKpkKCRQeCKKSCPvvkTGklCIEVtVGSKLAFISEELCIGCGICVKKCPFEAIQII 73
Cdd:COG1149 4 KIPVIDEEKCI--GCGL-CVEVCP---EG--AIKL-DDGGAPVVDPDLCTGCGACVGVCPTGAITLE 61
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
6-73 |
4.51e-09 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 53.52 E-value: 4.51e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328793 6 TRIAIVSSDRCKpkKCRQeCKKSCPVvktgkLCIEVTVGSKLAfISEELCIGCGICVKKCPFEAIQII 73
Cdd:COG1144 22 VERPVVDEDKCI--GCGL-CWIVCPD-----GAIRVDDGKYYG-IDYDYCKGCGICAEVCPVKAIEMV 80
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
102-276 |
4.54e-09 |
|
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: 56.60 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFtsppDWQEILTHfrgsELQNYFTRILednlkaiikpQYVDHIPrAVK 181
Cdd:TIGR01189 25 AGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV----RWNGTPLA----EQRDEPHENI----------LYLGHLP-GLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 182 G--NVGEVL-----DQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVK-QRL 253
Cdd:TIGR01189 86 PelSALENLhfwaaIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAgVAL 165
|
170 180
....*....|....*....|...
gi 22328793 254 KAAQVVRSLLRPNSYVIVVEHDL 276
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLTTHQDL 188
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
103-275 |
5.63e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.31 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT--------SPPDWQEILTHFRGSELQNYFTriLEDNLKAIIKPqyvD 174
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMldgvdlshVPPYQRPINMMFQSYALFPHMT--VEQNIAFGLKQ---D 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 175 HIPRAvkgnvgEVldqkdeRDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLK 254
Cdd:PRK11607 120 KLPKA------EI------ASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR 187
|
170 180
....*....|....*....|..
gi 22328793 255 AA-QVVRSLLRPNSYVIVVEHD 275
Cdd:PRK11607 188 MQlEVVDILERVGVTCVMVTHD 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
102-278 |
6.20e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 56.95 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGR---------FTSPPDWQEILTHFR--GSELQNY-----FTrILEDNLK 165
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQlniaghqfdFSQKPSEKAIRLLRQkvGMVFQQYnlwphLT-VMENLIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 166 AIIKpqyvdhipraVKGnvgevLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSS 245
Cdd:COG4161 106 APCK----------VLG-----LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190
....*....|....*....|....*....|...
gi 22328793 246 YLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSV 278
Cdd:COG4161 171 ALDPEITAQVVEIIRELSQTGITQVIVTHEVEF 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
70-276 |
6.20e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.43 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 70 IQIINLPRDLEKDTTHrYGANTFKLHrlpvPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLG-------RFTSPPDWQe 142
Cdd:PRK13650 5 IEVKNLTFKYKEDQEK-YTLNDVSFH----VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGqiiidgdLLTEENVWD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 143 iLTHFRGSELQN----YFTRILEDNLKAIIKPQYVDHipRAVKGNVGEVLDQKDERDKKaelcadlelnqviDRDVENLS 218
Cdd:PRK13650 79 -IRHKIGMVFQNpdnqFVGATVEDDVAFGLENKGIPH--EEMKERVNEALELVGMQDFK-------------EREPARLS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 219 GGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSY-VIVVEHDL 276
Cdd:PRK13650 143 GGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMtVISITHDL 201
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
102-276 |
7.42e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.33 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT----------------------SPPDWQeilthFRGSELQNYFTRI 159
Cdd:PRK13635 32 EGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmvlseetvwdvrrqvgmvfQNPDNQ-----FVGATVQDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 160 LEDNlkaiikpqyvdHIPRavkgnvgevlDQKDERDKKAelcadleLNQV-----IDRDVENLSGGELQRFAIAVVAIQN 234
Cdd:PRK13635 107 LENI-----------GVPR----------EEMVERVDQA-------LRQVgmedfLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22328793 235 AEIYMFDEPSSYLDVKQRLKAAQVVRSLLRP-NSYVIVVEHDL 276
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDL 201
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
356-540 |
8.68e-09 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 56.48 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 356 TKTQGNFR------LRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDDTEGPDREIPEFNVSYKPQKISPKFQNS 429
Cdd:cd03300 7 SKFYGGFValdgvsLDIKEGEF-----FTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 430 V--RHL---------LHQKIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYL 498
Cdd:cd03300 82 AlfPHLtvfeniafgLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22328793 499 DSEQRIVASKVIKRfiLHAK-KTAFV-VEHDFIMATYLADRVIV 540
Cdd:cd03300 162 DLKLRKDMQLELKR--LQKElGITFVfVTHDQEEALTMSDRIAV 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
101-286 |
9.09e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLG---------RFTSPPDWQE---ILTHfrgSELQNYFTRILEDNLkaii 168
Cdd:PRK11288 28 RAGQVHALMGENGAGKSTLLKILSGNYQPDAGsilidgqemRFASTTAALAagvAIIY---QELHLVPEMTVAENL---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 169 kpqYVDHIPravkgNVGEVLDQKDERDKKAELCADLELNqvIDRD--VENLSGGELQRFAIAVVAIQNAEIYMFDEPSSY 246
Cdd:PRK11288 101 ---YLGQLP-----HKGGIVNRRLLNYEAREQLEHLGVD--IDPDtpLKYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 22328793 247 LDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFI 286
Cdd:PRK11288 171 LSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAI 210
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
8-72 |
9.27e-09 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 56.27 E-value: 9.27e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 8 IAIVSSDRCKpkKCRQeCKKSCPVvktgkLCIEVTVGSKLAFISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG1145 176 KAVIDAEKCI--GCGL-CVKVCPT-----GAIRLKDGKPQIVVDPDKCIGCGACVKVCPVGAISL 232
|
|
| HycB_like |
cd10554 |
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ... |
7-72 |
9.72e-09 |
|
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.
Pssm-ID: 319876 [Multi-domain] Cd Length: 149 Bit Score: 54.57 E-value: 9.72e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 7 RIAIVSSDR-CKPKKCRQ-E---CKKSCPVvktGklCIEVTVGSKlaFISEELCIGCGICVKKCPFEAIQI 72
Cdd:cd10554 41 RLRVVKTGEvTAPVQCRQcEdapCANVCPV---G--AISQEDGVV--QVDEERCIGCKLCVLACPFGAIEM 104
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
353-540 |
9.74e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.98 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 353 PTMTKTQGNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKP-------DDTEGPDREIpefNVSYKPQKISPK 425
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEF-----VGLIGHTGSGKSTLIQHLNGLLKPtsgkiiiDGVDITDKKV---KLSDIRKKVGLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 426 FQNSVRHLLHQKI-RDSYMHPQFM--SD------VMKPLQI-----EQLMDQEVVNLSGGELQRVALTLCLGKPADIYLI 491
Cdd:PRK13637 89 FQYPEYQLFEETIeKDIAFGPINLglSEeeienrVKRAMNIvgldyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22328793 492 DEPSAYLDSEQRIVASKVIKRfiLHAKK--TAFVVEHDFIMATYLADRVIV 540
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKE--LHKEYnmTIILVSHSMEDVAKLADRIIV 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
351-541 |
1.09e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.02 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 351 KYPTMTKTQGNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDD---------------TEGPDREIPEFNV 415
Cdd:PRK13651 15 KLPTELKALDNVSVEINQGEF-----IAIIGQTGSGKTTFIEHLNALLLPDTgtiewifkdeknkkkTKEKEKVLEKLVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 416 SyKPQKISPKFQNSVR------------HLLHQKI-RDSYMHPqfMSDVMKPLQIEQL---------MDQEVV-----NL 468
Cdd:PRK13651 90 Q-KTRFKKIKKIKEIRrrvgvvfqfaeyQLFEQTIeKDIIFGP--VSMGVSKEEAKKRaakyielvgLDESYLqrspfEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328793 469 SGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRfiLHAK-KTAFVVEHDFIMATYLADRVIVY 541
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDN--LNKQgKTIILVTHDLDNVLEWTKRTIFF 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
81-277 |
1.13e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.22 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANT----FKLHrlpVPrPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF---TSPpdwqeiLTHFRGSelq 153
Cdd:PRK11247 16 NAVSKRYGERTvlnqLDLH---IP-AGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagTAP------LAEARED--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 154 nyfTRILEDNLKAIIKPQYVDHIPRAVKGNVgevldqkdeRDKKAELCADLELNqviDRDVE---NLSGGELQRFAIAVV 230
Cdd:PRK11247 83 ---TRLMFQDARLLPWKKVIDNVGLGLKGQW---------RDAALQALAAVGLA---DRANEwpaALSGGQKQRVALARA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22328793 231 AIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSY-VIVVEHDLS 277
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFtVLLVTHDVS 195
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
101-256 |
1.17e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.05 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEILTHFRGSELQN---------YFTRILEDNLKaIIKPQ 171
Cdd:PRK13657 359 KPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI--DGTDIRTVTRASLRRNiavvfqdagLFNRSIEDNIR-VGRPD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 172 YVD-HIPRAVKGnvGEVLDQKDERDKKaelcadleLNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDV- 249
Cdd:PRK13657 436 ATDeEMRAAAER--AQAHDFIERKPDG--------YDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVe 505
|
....*...
gi 22328793 250 -KQRLKAA 256
Cdd:PRK13657 506 tEAKVKAA 513
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
379-543 |
1.17e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 56.74 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 379 MLGENGTGKTTFIRMLAGLLKPD-------DTEGPDR-EIPEFNVSYKPQ--KISPKFqnSVRHLLHQKIRDSYMHPQFM 448
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDagsislcGEPVPSRaRHARQRVGVVPQfdNLDPDF--TVRENLLVFGRYFGLSAAAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 449 SDVMKPL----QIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIkRFILHAKKTAFVV 524
Cdd:PRK13537 116 RALVPPLlefaKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERL-RSLLARGKTILLT 194
|
170
....*....|....*....
gi 22328793 525 EHDFIMATYLADRVIVYEG 543
Cdd:PRK13537 195 THFMEEAERLCDRLCVIEE 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
361-542 |
1.17e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 56.17 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDDTEgpdREIP--EFNVSYKP---------QKISPKFQNS 429
Cdd:COG4161 20 DINLECPSGE-----TLVLLGPSGAGKSSLLRVLNLLETPDSGQ---LNIAghQFDFSQKPsekairllrQKVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 430 vrHLL-HQKIRD------------SYMHPQFMSD-VMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPS 495
Cdd:COG4161 92 --NLWpHLTVMEnlieapckvlglSKEQAREKAMkLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22328793 496 AYLDSEqrIVASKV-IKRFILHAKKTAFVVEHDFIMATYLADRVIVYE 542
Cdd:COG4161 170 AALDPE--ITAQVVeIIRELSQTGITQVIVTHEVEFARKVASQVVYME 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
101-289 |
1.29e-08 |
|
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: 55.70 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEI----LTHFRgselqnyftrilednlKAI-IKPQ---- 171
Cdd:cd03253 25 PAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI--DGQDIrevtLDSLR----------------RAIgVVPQdtvl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 172 YVDHIPRAVK-GNVGEVLDQKDERDKKAELcADLELN-------QVIDRDVEnLSGGELQRFAIAVVAIQNAEIYMFDEP 243
Cdd:cd03253 87 FNDTIGYNIRyGRPDATDEEVIEAAKAAQI-HDKIMRfpdgydtIVGERGLK-LSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22328793 244 SSYLDVKQRLKAAQVVRSLLRpNSYVIVVEHDLS-VLDylSDFICCL 289
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSK-GRTTIVIAHRLStIVN--ADKIIVL 208
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
344-544 |
1.35e-08 |
|
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: 55.35 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 344 IQSYARYKYPTMTKTQgNFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPddTEGPDREIPEFNVSYKPQKIS 423
Cdd:cd03233 9 ISFTTGKGRSKIPILK-DFSGVVKPGE-----MVLVLGRPGSGCSTLLKALANRTEG--NVSVEGDIHYNGIPYKEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 424 PKfqnsvrhllhqkiRDSYMHPQfmSDV-MKPLQIEQLMD--------QEVVNLSGGELQRVALTLCLGKPADIYLIDEP 494
Cdd:cd03233 81 YP-------------GEIIYVSE--EDVhFPTLTVRETLDfalrckgnEFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 495 SAYLDSeqrIVASKVIKRFILHAKKTAFVVehdfIMATYLA--------DRVIV-YEGQ 544
Cdd:cd03233 146 TRGLDS---STALEILKCIRTMADVLKTTT----FVSLYQAsdeiydlfDKVLVlYEGR 197
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
375-524 |
1.37e-08 |
|
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: 56.40 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 375 QIIVMLGENGTGKTTFIRMLAGLLKPddTEGPDREipEFNVSYKPQkispkfqnsVRHLLHQKIRD------SYMHPQFM 448
Cdd:cd03291 64 EMLAITGSTGSGKTSLLMLILGELEP--SEGKIKH--SGRISFSSQ---------FSWIMPGTIKEniifgvSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 449 SdVMKPLQIEQ-----------LMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLD--SEQRIVASKVIKrfiL 515
Cdd:cd03291 131 S-VVKACQLEEditkfpekdntVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfTEKEIFESCVCK---L 206
|
....*....
gi 22328793 516 HAKKTAFVV 524
Cdd:cd03291 207 MANKTRILV 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
101-292 |
1.39e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 56.66 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR--FtsppDWQEIlTHFRGSELQNYFTRIlednlkaiikpQYVDHIPR 178
Cdd:COG4608 42 RRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEilF----DGQDI-TGLSGRELRPLRRRM-----------QMVFQDPY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 179 A-------VKGNVGEVLD-----QKDERDKK-AELCADLELN-QVIDRDVENLSGGELQRFAIA---------VVAiqna 235
Cdd:COG4608 106 AslnprmtVGDIIAEPLRihglaSKAERRERvAELLELVGLRpEHADRYPHEFSGGQRQRIGIAralalnpklIVC---- 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 236 eiymfDEPSSYLDVKQRlkaAQVVRSL--LRPN---SYVIvVEHDLSVLDYLSDFICCLY-GK 292
Cdd:COG4608 182 -----DEPVSALDVSIQ---AQVLNLLedLQDElglTYLF-ISHDLSVVRHISDRVAVMYlGK 235
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
346-545 |
1.44e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 346 SYARYKYPTMtktqGNFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPD------DTEGPDREIPEFNVSYKP 419
Cdd:PRK13543 18 AFSRNEEPVF----GPLDFHVDAGE-----ALLVQGDNGAGKTTLLRVLAGLLHVEsgqiqiDGKTATRGDRSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 420 QKISPKFQNSVRHLLHQKIRDSYMHPQFMSDvmKPLQIEQLMDQE---VVNLSGGELQRVALTLCLGKPADIYLIDEPSA 496
Cdd:PRK13543 89 HLPGLKADLSTLENLHFLCGLHGRRAKQMPG--SALAIVGLAGYEdtlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22328793 497 YLDSEQRIVASKVIKRFiLHAKKTAFVVEHDFIMATYLADRVIVYEGQP 545
Cdd:PRK13543 167 NLDLEGITLVNRMISAH-LRGGGAALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
102-284 |
1.53e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEI-------LTHFRGSELQnyFTRILEDNLK--AIIKPQY 172
Cdd:PRK10636 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSG---------EIglakgikLGYFAQHQLE--FLRADESPLQhlARLAPQE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 173 VDHIPRAVKGNVGEvldqkdERDKKAELCadlelnqvidrdvENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQR 252
Cdd:PRK10636 406 LEQKLRDYLGGFGF------QGDKVTEET-------------RRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
170 180 190
....*....|....*....|....*....|..
gi 22328793 253 lkaAQVVRSLLRPNSYVIVVEHDLSVLDYLSD 284
Cdd:PRK10636 467 ---QALTEALIDFEGALVVVSHDRHLLRSTTD 495
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
14-74 |
1.53e-08 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 57.34 E-value: 1.53e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 14 DRCKPKKCRQeCKKSCPVVKtgklcieVTVGSKLAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:COG4624 89 DKEKCKNCYP-CVRACPVKA-------IKVDDGKAEIDEEKCISCGQCVAVCPFGAITEKS 141
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
43-74 |
1.62e-08 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 51.27 E-value: 1.62e-08
10 20 30
....*....|....*....|....*....|..
gi 22328793 43 VGSKLAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:COG1149 1 VKRKIPVIDEEKCIGCGLCVEVCPEGAIKLDD 32
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
375-500 |
1.67e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.88 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 375 QIIVMLGENGTGKTTFIRMLAGLLKPddTEGpdreipefNVSYKPQKI-SPKFQNSVRHLLHQkirdSYMHP-------- 445
Cdd:PRK13539 29 EALVLTGPNGSGKTTLLRLIAGLLPP--AAG--------TIKLDGGDIdDPDVAEACHYLGHR----NAMKPaltvaenl 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22328793 446 QFMSDVM--KPLQIEQLMD----QEVVNLSGGEL-----QRVALTLCLGKPADIYLIDEPSAYLDS 500
Cdd:PRK13539 95 EFWAAFLggEELDIAAALEavglAPLAHLPFGYLsagqkRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
348-501 |
1.85e-08 |
|
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: 57.37 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 348 ARYKYPTMTKTQGNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDDTE--GPDREIPEFNVSYKPQKISPK 425
Cdd:TIGR02868 340 LSAGYPGAPPVLDGVSLDLPPGER-----VAILGPSGSGKSTLLATLAGLLDPLQGEvtLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 426 FQNSvrHLLHQKIRDSYM------HPQFMSDVMKPLQIEQL-------MDQEVVN----LSGGELQRVALTLCLGKPADI 488
Cdd:TIGR02868 415 AQDA--HLFDTTVRENLRlarpdaTDEELWAALERVGLADWlralpdgLDTVLGEggarLSGGERQRLALARALLADAPI 492
|
170
....*....|...
gi 22328793 489 YLIDEPSAYLDSE 501
Cdd:TIGR02868 493 LLLDEPTEHLDAE 505
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
101-278 |
2.11e-08 |
|
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: 55.28 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEIlTHFRGSELQNYFTRIlednlkAIIKPQYVDHIPRAV 180
Cdd:cd03258 29 PKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV--DGTDL-TLLSGKELRKARRRI------GMIFQHFNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 181 KGNVG---EVLDQ-KDERDKKA-ELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKqrlKA 255
Cdd:cd03258 100 FENVAlplEIAGVpKAEIEERVlELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE---TT 176
|
170 180
....*....|....*....|....*..
gi 22328793 256 AQVVRSLLRPNS----YVIVVEHDLSV 278
Cdd:cd03258 177 QSILALLRDINRelglTIVLITHEMEV 203
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
379-547 |
2.12e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 56.38 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 379 MLGENGTGKTTFIRMLAGLLKPD-------DTEGPDRE---------IPEFNvsykpqKISPKFqnSVRHLLHQKIRDSY 442
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDagkitvlGVPVPARArlararigvVPQFD------NLDLEF--TVRENLLVFGRYFG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 443 MHPQFMSDVMKPL----QIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIkRFILHAK 518
Cdd:PRK13536 144 MSTREIEAVIPSLlefaRLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL-RSLLARG 222
|
170 180
....*....|....*....|....*....
gi 22328793 519 KTAFVVEHDFIMATYLADRVIVYEGQPSI 547
Cdd:PRK13536 223 KTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
370-539 |
2.12e-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: 53.90 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 370 EFTDSQIIVMLGENGTGKTTFIRMLAgllkpddtegpdreipeFNVSYKPQKISPKFQNSVRHllhqkirdsymhpqfms 449
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAIG-----------------LALGGAQSATRRRSGVKAGC----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 450 dvMKPLQIEQLMdQEVVNLSGGELQRVALTLCLG----KPADIYLIDEPSAYLDSEQRIVASKVIKRFILHaKKTAFVVE 525
Cdd:cd03227 63 --IVAAVSAELI-FTRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVIT 138
|
170
....*....|....
gi 22328793 526 HDFIMATyLADRVI 539
Cdd:cd03227 139 HLPELAE-LADKLI 151
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
350-547 |
2.18e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.51 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 350 YKYPTMTKTQGNFRLRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPddTEGP----DREIPEFNVSYKPQKISPK 425
Cdd:PRK13647 12 FRYKDGTKALKGLSLSIPEGSKT-----ALLGPNGAGKSTLLLHLNGIYLP--QRGRvkvmGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 426 FQNSVRHLLHQKI-RDSYMHPQFM-----------SDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDE 493
Cdd:PRK13647 85 FQDPDDQVFSSTVwDDVAFGPVNMgldkdeverrvEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 494 PSAYLDSEQRIVASKVIKRfiLHAK-KTAFVVEHDFIMATYLADRVIVY-------EGQPSI 547
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDR--LHNQgKTVIVATHDVDLAAEWADQVIVLkegrvlaEGDKSL 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
81-277 |
2.23e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 56.27 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANTF--KLHrLPVPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGR-FTSPPDwqeiLTHfrgSELQNyft 157
Cdd:PRK11432 10 KNITKRFGSNTVidNLN-LTIKQ-GTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQiFIDGED----VTH---RSIQQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 158 RILednlkAIIKPQYVDHIPRAVKGNVGEVLDQ----KDERDKK-AELCADLELNQVIDRDVENLSGGELQRFAIAVVAI 232
Cdd:PRK11432 78 RDI-----CMVFQSYALFPHMSLGENVGYGLKMlgvpKEERKQRvKEALELVDLAGFEDRYVDQISGGQQQRVALARALI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22328793 233 QNAEIYMFDEPSSYLDVKQRLKAAQVVRSL-LRPNSYVIVVEHDLS 277
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQS 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
101-289 |
2.27e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGkLKPNlgrftspPDWQ-EILthFRGSELQNYFTRILEDNLKAIIKpQYVDHIPR- 178
Cdd:PRK13549 29 RAGEIVSLCGENGAGKSTLMKVLSG-VYPH-------GTYEgEII--FEGEELQASNIRDTERAGIAIIH-QELALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 179 AVKGNV--------GEVLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVK 250
Cdd:PRK13549 98 SVLENIflgneitpGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTES 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 22328793 251 QRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCL 289
Cdd:PRK13549 178 ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVI 216
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
103-243 |
2.53e-08 |
|
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: 54.97 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEILT---HFRGSELQNY-------FTRI-LEDNLKAIIKPQ 171
Cdd:TIGR04406 27 GEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILI--DGQDITHlpmHERARLGIGYlpqeasiFRKLtVEENIMAVLEIR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 172 yvdhipravkgnvgEVLDqKDERDKKAE-LCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEP 243
Cdd:TIGR04406 105 --------------KDLD-RAEREERLEaLLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
349-546 |
2.67e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.47 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 349 RYKYPTMTKTQGNFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDDTEgpdREIPEFNVSYKP-------QK 421
Cdd:PRK13639 8 KYSYPDGTEALKGINFKAEKGE-----MVALLGPNGAGKSTLFLHFNGILKPTSGE---VLIKGEPIKYDKksllevrKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 422 ISPKFQNSVRHLLHQKIR-DSYMHPQFM-----------SDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIY 489
Cdd:PRK13639 80 VGIVFQNPDDQLFAPTVEeDVAFGPLNLglskeevekrvKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22328793 490 LIDEPSAYLDSeqrIVASKVIKRFILHAKK--TAFVVEHDFIMATYLADRV-------IVYEGQPS 546
Cdd:PRK13639 160 VLDEPTSGLDP---MGASQIMKLLYDLNKEgiTIIISTHDVDLVPVYADKVyvmsdgkIIKEGTPK 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
101-280 |
2.94e-08 |
|
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: 54.52 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF------TSPPDWQEILTHFrGSELQN--YFTRILEDNLkAIIKPqY 172
Cdd:cd03245 28 RAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdIRQLDPADLRRNI-GYVPQDvtLFYGTLRDNI-TLGAP-L 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 173 VD--HIPRAVK-GNVGEVLDqkdeRDKKAelcadLELnQVIDRDvENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLD- 248
Cdd:cd03245 105 ADdeRILRAAElAGVTDFVN----KHPNG-----LDL-QIGERG-RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDm 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 22328793 249 -----VKQRLKAaqvvrsLLRPNSyVIVVEHDLSVLD 280
Cdd:cd03245 174 nseerLKERLRQ------LLGDKT-LIIITHRPSLLD 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
375-526 |
3.12e-08 |
|
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: 56.84 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 375 QIIVMLGENGTGKTTFIRMLAGLLKPddTEGPDREipEFNVSYKPQkispkfqnsVRHLLHQKIRD------SYMHPQFM 448
Cdd:TIGR01271 453 QLLAVAGSTGSGKSSLLMMIMGELEP--SEGKIKH--SGRISFSPQ---------TSWIMPGTIKDniifglSYDEYRYT 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 449 SdVMKPLQIEQ------------LMDQEVVnLSGGELQRVALTLCLGKPADIYLIDEPSAYLD--SEQRIVASKVIKrfi 514
Cdd:TIGR01271 520 S-VIKACQLEEdialfpekdktvLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFTHLDvvTEKEIFESCLCK--- 594
|
170
....*....|....*.
gi 22328793 515 LHAKKTAFVV----EH 526
Cdd:TIGR01271 595 LMSNKTRILVtsklEH 610
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
103-278 |
3.13e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.64 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKIL-------AGKLK--PNLGRFTSPPDWQEILTHFR--GSELQNY-----FTrILEDNLKA 166
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLnllemprSGTLNiaGNHFDFSKTPSDKAIRELRRnvGMVFQQYnlwphLT-VQQNLIEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 167 iikpqyvdhiPRAVKGnvgevLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSY 246
Cdd:PRK11124 107 ----------PCRVLG-----LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190
....*....|....*....|....*....|....*
gi 22328793 247 LDVKqrlKAAQVV---RSLLRPNSYVIVVEHDLSV 278
Cdd:PRK11124 172 LDPE---ITAQIVsiiRELAETGITQVIVTHEVEV 203
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
17-81 |
3.22e-08 |
|
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 52.78 E-value: 3.22e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328793 17 KPKKCRQ----ECKKSCPV-----VKTGklcievtvgskLAFISEELCIGCGICVKKCPFEAIQIINLPRDLEK 81
Cdd:cd04410 46 LPVSCMHcedpPCVKACPTgaiykDEDG-----------IVLIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVK 108
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
101-289 |
3.42e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.22 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKL----KPNLGRFTSPpdwqeilTHFRGSELQNYFTRILEdNLKAIIkPQ----- 171
Cdd:PRK13547 25 EPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGARVTGD-------VTLNGEPLAAIDAPRLA-RLRAVL-PQaaqpa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 172 ---YVDHI------PRAVKGNV-----GEVLDQKDERDKKAELCAdlelnqvidRDVENLSGGELQRFAIAVV------- 230
Cdd:PRK13547 96 fafSAREIvllgryPHARRAGAlthrdGEIAWQALALAGATALVG---------RDVTTLSGGELARVQFARVlaqlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 231 --AIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRP-NSYVIVVEHDLSVLDYLSDFICCL 289
Cdd:PRK13547 167 hdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAML 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
356-540 |
3.49e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 54.29 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 356 TKTQGNFR-------LRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPddTEG------------PDREIPEFNvs 416
Cdd:COG2884 8 SKRYPGGRealsdvsLEIEKGEF-----VFLTGPSGAGKSTLLKLLYGEERP--TSGqvlvngqdlsrlKRREIPYLR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 417 ykpQKISPKFQN-------SV--------------RHLLHQKIRDsymhpqfmsdVMKPLQIEQLMDQEVVNLSGGELQR 475
Cdd:COG2884 79 ---RRIGVVFQDfrllpdrTVyenvalplrvtgksRKEIRRRVRE----------VLDLVGLSDKAKALPHELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 476 V----ALtlcLGKPaDIYLIDEPSAYLDSE--QRIVasKVIKRFilHAKKTAfvvehdFIMATYlaDRVIV 540
Cdd:COG2884 146 VaiarAL---VNRP-ELLLADEPTGNLDPEtsWEIM--ELLEEI--NRRGTT------VLIATH--DLELV 200
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
6-72 |
3.52e-08 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 50.43 E-value: 3.52e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328793 6 TRIAIVSSDRCKpkKCRqECKKSCPVvktgkLCIEVTVGSklAFISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG2221 7 TWPPKIDEEKCI--GCG-LCVAVCPT-----GAISLDDGK--LVIDEEKCIGCGACIRVCPTGAIKG 63
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
369-513 |
3.69e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.85 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 369 GEFTDSQIIVMLGENGTGKTTFIRMLAGLLkpddtEGP------DREIPEFNV-------SYKPQKISPKFQNSVRHL-- 433
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGLL-----PGQgeillnGRPLSDWSAaelarhrAYLSQQQSPPFAMPVFQYla 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 434 LHQ-KIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCL----------GKpadIYLIDEPSAYLDSEQ 502
Cdd:COG4138 92 LHQpAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptinpeGQ---LLLLDEPMNSLDVAQ 168
|
170
....*....|.
gi 22328793 503 RIVASKVIKRF 513
Cdd:COG4138 169 QAALDRLLREL 179
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
81-290 |
3.90e-08 |
|
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: 54.11 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANTFkLHR--LPVPrPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRftspPDWQEILthFRGSELQNYFTR 158
Cdd:cd03260 4 RDLNVYYGDKHA-LKDisLDIP-KGEITALIGPSGCGKSTLLRLLNRLNDLIPGA----PDEGEVL--LDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 159 ILEDNLKAIIKPQYVDHIPRAVKGNV-------GEVLDQK-DERDKKAELCADLeLNQVIDR-DVENLSGGELQRFAIAV 229
Cdd:cd03260 76 VLELRRRVGMVFQKPNPFPGSIYDNVayglrlhGIKLKEElDERVEEALRKAAL-WDEVKDRlHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 230 VAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSyVIVVEHDLSVLDYLSDFICCLY 290
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYT-IVIVTHNMQQAARVADRTAFLL 214
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
14-72 |
4.01e-08 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 50.13 E-value: 4.01e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 14 DRCKpkKCRQeCKKSCPVvktgkLCIEVTVGSKLAF--ISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG1143 2 DKCI--GCGL-CVRVCPV-----DAITIEDGEPGKVyvIDPDKCIGCGLCVEVCPTGAISM 54
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
102-283 |
4.05e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.44 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPDWQEILTHFRGSELQNY-------FTRILED--NLKAIIKPQY 172
Cdd:PRK11629 34 EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQklgfiyqFHHLLPDftALENVAMPLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 173 VDHIPRAvkgnvgevldqkDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDvkqr 252
Cdd:PRK11629 114 IGKKKPA------------EINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD---- 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 22328793 253 LKAAQVVRSLL-----RPNSYVIVVEHDLSVLDYLS 283
Cdd:PRK11629 178 ARNADSIFQLLgelnrLQGTAFLVVTHDLQLAKRMS 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
364-542 |
4.57e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDDTEgpdREIP--EFNVSYKP---------QKISPKFQN---- 428
Cdd:PRK11124 23 LDCPQGE-----TLVLLGPSGAGKSSLLRVLNLLEMPRSGT---LNIAgnHFDFSKTPsdkairelrRNVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 ---SVRH-LLHQKIRDSYM-HPQFMSDVMK---PLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDS 500
Cdd:PRK11124 95 phlTVQQnLIEAPCRVLGLsKDQALARAEKlleRLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22328793 501 EqrIVASKV-IKRFILHAKKTAFVVEHDFIMATYLADRVIVYE 542
Cdd:PRK11124 175 E--ITAQIVsIIRELAETGITQVIVTHEVEVARKTASRVVYME 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
101-303 |
5.09e-08 |
|
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: 54.01 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLG-------RFTSP-PDwqeilthfRGSELQNYftrilednlkAIIKPQY 172
Cdd:TIGR01184 9 QQGEFISLIGHSGCGKSTLLNLISGLAQPTSGgvilegkQITEPgPD--------RMVVFQNY----------SLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 173 V-DHIPRAVKgnvgEVLDQ--KDERDKKAELCADL-ELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLD 248
Cdd:TIGR01184 71 VrENIALAVD----RVLPDlsKSERRAIVEEHIALvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 249 --VKQRLKaAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCLYGKPGAY--GVVTLPF 303
Cdd:TIGR01184 147 alTRGNLQ-EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANigQILEVPF 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
375-539 |
5.46e-08 |
|
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: 53.44 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 375 QIIVMLGENGTGKTTFIRMLAGLLKPD------DTEGPDREI-------PEFNVSYKPQKI--SPKFQNSVRHLLHQKIR 439
Cdd:cd03269 27 EIFGLLGPNGAGKTTTIRMILGIILPDsgevlfDGKPLDIAArnrigylPEERGLYPKMKVidQLVYLAQLKGLKKEEAR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 440 DSymhpqfMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSeqriVASKVIKRFILHAK- 518
Cdd:cd03269 107 RR------IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP----VNVELLKDVIRELAr 176
|
170 180
....*....|....*....|...
gi 22328793 519 --KTAFVVEHDFIMATYLADRVI 539
Cdd:cd03269 177 agKTVILSTHQMELVEELCDRVL 199
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
84-304 |
5.53e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.50 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 84 THRYGANTFKLHRLPVPRpGQVLGLVGTNGIGKSTALKILAGKLKpnlgrftsppdwqeiLTHFRGSELQNYFTRILEDN 163
Cdd:PRK15056 15 TWRNGHTALRDASFTVPG-GSIAALVGVNGSGKSTLFKALMGFVR---------------LASGKISILGQPTRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 164 LKAIIkPQY--VD-HIPRAVK-----GNVGEV--LDQKDERDKK--AELCADLELNQVIDRDVENLSGGELQRFAIAVVA 231
Cdd:PRK15056 79 LVAYV-PQSeeVDwSFPVLVEdvvmmGRYGHMgwLRRAKKRDRQivTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 232 IQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCLYGKPGAYGVVTLPFS 304
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFT 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
101-277 |
5.85e-08 |
|
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: 53.69 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT--------SPPDWQEILTHFrGSELQNY--FTR--ILEDNLKAII 168
Cdd:cd03262 24 KKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkltdDKKNINELRQKV-GMVFQQFnlFPHltVLENITLAPI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 169 KpqyvdhipraVKGNvgevldQKDERDKKA-ELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYL 247
Cdd:cd03262 103 K----------VKGM------SKAEAEERAlELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSAL 166
|
170 180 190
....*....|....*....|....*....|...
gi 22328793 248 D---VKQRLkaaQVVRSLLRPNSYVIVVEHDLS 277
Cdd:cd03262 167 DpelVGEVL---DVMKDLAEEGMTMVVVTHEMG 196
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
361-543 |
6.04e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGeftdsQIIVMLGENGTGKTTFIRMLAGLLKPDDTEGPDrEIPEFNVsykPQKISpkfqnsvrhllhqkIRD 440
Cdd:COG2401 48 DLNLEIEPG-----EIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-DVPDNQF---GREAS--------------LID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 441 SYMHPQFMSDVMKPLQIEQLMD-----QEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQ-RIVASKViKRFI 514
Cdd:COG2401 105 AIGRKGDFKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTaKRVARNL-QKLA 183
|
170 180
....*....|....*....|....*....
gi 22328793 515 LHAKKTAFVVEHDFIMATYLADRVIVYEG 543
Cdd:COG2401 184 RRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
361-539 |
6.17e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDdtEGPDREIPEFNVSYKPQKISPKFQNSVRHLlhqkird 440
Cdd:PRK15064 337 NLNLLLEAGE-----RLAIIGENGVGKTTLLRTLVGELEPD--SGTVKWSENANIGYYAQDHAYDFENDLTLF------- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 441 symhpQFMSDVMKPLQIEQLM--------------DQEVVNLSGGELQRVAL-TLCLGKPaDIYLIDEPSAYLDSEQRIV 505
Cdd:PRK15064 403 -----DWMSQWRQEGDDEQAVrgtlgrllfsqddiKKSVKVLSGGEKGRMLFgKLMMQKP-NVLVMDEPTNHMDMESIES 476
|
170 180 190
....*....|....*....|....*....|....
gi 22328793 506 ASKVIKRFilhaKKTAFVVEHDFIMATYLADRVI 539
Cdd:PRK15064 477 LNMALEKY----EGTLIFVSHDREFVSSLATRII 506
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
375-499 |
6.40e-08 |
|
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: 53.27 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 375 QIIVMLGENGTGKTTFIRMLAGLLKPDDTEgpdreipefnVSYKPQ---KISPKFQNSVRHLLHQKIRDSYMHP----QF 447
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGR----------VLLNGGpldFQRDSIARGLLYLGHAPGIKTTLSVlenlRF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 448 MSDVMKPLQIEQLMDQ---------EVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLD 499
Cdd:cd03231 97 WHADHSDEQVEEALARvglngfedrPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| RLI |
pfam04068 |
Possible Fer4-like domain in RNase L inhibitor, RLI; Possible metal-binding domain in ... |
6-37 |
6.50e-08 |
|
Possible Fer4-like domain in RNase L inhibitor, RLI; Possible metal-binding domain in endoribonuclease RNase L inhibitor. Found at the N-terminal end of RNase L inhibitor proteins, adjacent to the 4Fe-4S binding domain, fer4, pfam00037. Also often found adjacent to the DUF367 domain pfam04034 in uncharacterized proteins. The RNase L system plays a major role in the anti-viral and anti-proliferative activities of interferons, and could possibly play a more general role in the regulation of RNA stability in mammalian cells. Inhibitory activity requires concentration-dependent association of RLI with RNase L.
Pssm-ID: 427689 [Multi-domain] Cd Length: 35 Bit Score: 48.66 E-value: 6.50e-08
10 20 30
....*....|....*....|....*....|....*
gi 22328793 6 TRIAIVSSDRCKPKKCRQ-ECKKSCPV--VKTGKL 37
Cdd:pfam04068 1 MRLAIVDFDQCDPKKCTGrKCIRFCPVreVRTGKK 35
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
371-540 |
6.53e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.86 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 371 FTDSQIIVMLGENGTGKTTFIRMLAGLLKP--------DDTEGPDREIPEFNVSYKPQKI----------SPKFQNSVRH 432
Cdd:PRK13631 49 FEKNKIYFIIGNSGSGKSTLVTHFNGLIKSkygtiqvgDIYIGDKKNNHELITNPYSKKIknfkelrrrvSMVFQFPEYQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 433 LLHQKIRDSYMH-------PQFMSDVMKPLQIEQL------MDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLD 499
Cdd:PRK13631 129 LFKDTIEKDIMFgpvalgvKKSEAKKLAKFYLNKMglddsyLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22328793 500 SEqrivASKVIKRFILHAK---KTAFVVEHDFIMATYLADRVIV 540
Cdd:PRK13631 209 PK----GEHEMMQLILDAKannKTVFVITHTMEHVLEVADEVIV 248
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
364-539 |
7.10e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.99 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDD--TEGPDREIpEFNVSYKPQkispkfQNSVRHLLHQ----- 436
Cdd:PRK11264 24 LEVKPGE-----VVAIIGPSGSGKTTLLRCINLLEQPEAgtIRVGDITI-DTARSLSQQ------KGLIRQLRQHvgfvf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 437 KIRDSYMHPQFMSDVMK-PLQIEQLMDQEVV---------------------NLSGGELQRVALTLCLGKPADIYLIDEP 494
Cdd:PRK11264 92 QNFNLFPHRTVLENIIEgPVIVKGEPKEEATararellakvglagketsyprRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22328793 495 SAYLDSEqriVASKVIK--RFILHAKKTAFVVEHDFIMATYLADRVI 539
Cdd:PRK11264 172 TSALDPE---LVGEVLNtiRQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
376-501 |
7.39e-08 |
|
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: 53.13 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 376 IIVMLGENGTGKTTFIRMLAGLLKPDDTE--------GPDREIPEFNVSYKPQKISPKFQNSVRHLLHQKIRDSYMHPQF 447
Cdd:TIGR01189 28 ALQVTGPNGIGKTTLLRILAGLLRPDSGEvrwngtplAEQRDEPHENILYLGHLPGLKPELSALENLHFWAAIHGGAQRT 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 22328793 448 MSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSE 501
Cdd:TIGR01189 108 IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
361-543 |
7.63e-08 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 54.04 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPddTEGpdreipefNVSYKPQ---KISPK------------ 425
Cdd:TIGR02769 29 NVSLSIEEGE-----TVGLLGRSGCGKSTLARLLLGLEKP--AQG--------TVSFRGQdlyQLDRKqrrafrrdvqlv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 426 FQNSV-----RHLLHQKIRDSYMHPQFMSDVMKPLQIEQL----------MDQEVVNLSGGELQRVALTLCLGKPADIYL 490
Cdd:TIGR02769 94 FQDSPsavnpRMTVRQIIGEPLRHLTSLDESEQKARIAELldmvglrsedADKLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22328793 491 IDEPSAYLDSEQRIVASKVIKRfILHAKKTAFV-VEHDFIMATYLADRVIVYEG 543
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRK-LQQAFGTAYLfITHDLRLVQSFCQRVAVMDK 226
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
18-70 |
7.71e-08 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 51.24 E-value: 7.71e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 22328793 18 PKKCR--QECKKSCPV--VKTGKLCIEVTVGSKLAFISEELCIGCGICVKKCPFEAI 70
Cdd:cd10549 39 EDKCVfcGACVEVCPTgaIELTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCPVDAI 95
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
377-542 |
7.99e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.04 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 377 IVMLGENGTGKTTFIRMLAGLLKPDDTEGPDR--EIPEFNVSYKPQKISPKFQNSVRHLLHQKI-RDSYMHPQFM----- 448
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRgePITKENIREVRKFVGLVFQNPDDQIFSPTVeQDIAFGPINLgldee 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 449 ------SDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFILHAKKTAF 522
Cdd:PRK13652 113 tvahrvSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVI 192
|
170 180
....*....|....*....|
gi 22328793 523 VVEHDFIMATYLADRVIVYE 542
Cdd:PRK13652 193 FSTHQLDLVPEMADYIYVMD 212
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
101-290 |
8.35e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.97 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF-------TSPPDWQEIL-------THFRGSELQNYFTRILEDnlkA 166
Cdd:PRK13643 30 KKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvSSTSKQKEIKpvrkkvgVVFQFPESQLFEETVLKD---V 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 167 IIKPQyvdhipravkgNVGevlDQKDERDKKAelCADLEL----NQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDE 242
Cdd:PRK13643 107 AFGPQ-----------NFG---IPKEKAEKIA--AEKLEMvglaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22328793 243 PSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHdlsVLDYLSDFICCLY 290
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTH---LMDDVADYADYVY 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
376-539 |
8.90e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 53.82 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 376 IIVMLGENGTGKTTFIRMLAGLLKPddTEGP----DREIPEFNVSYKPQKISPKFQnsvRHLLHQKIRDSYMHPQFMS-- 449
Cdd:PRK10619 33 VISIIGSSGSGKSTFLRCINFLEKP--SEGSivvnGQTINLVRDKDGQLKVADKNQ---LRLLRTRLTMVFQHFNLWShm 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 450 ----DVMK-PLQIEQLMDQEV----------------------VNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQ 502
Cdd:PRK10619 108 tvleNVMEaPIQVLGLSKQEAreravkylakvgideraqgkypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPEL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 22328793 503 RIVASKVIKRfILHAKKTAFVVEHDFIMATYLADRVI 539
Cdd:PRK10619 188 VGEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
370-542 |
8.93e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.06 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 370 EFTDSQIIVMLGENGTGKTTFIRMLAGLLKPD----DTEGPDREIPEFNVSYKP--QKISPKFQNSVRHLLHQKI-RDSY 442
Cdd:PRK13641 29 ELEEGSFVALVGHTGSGKSTLMQHFNALLKPSsgtiTIAGYHITPETGNKNLKKlrKKVSLVFQFPEAQLFENTVlKDVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 443 MHPQ---FMSDVMKPLQI---------EQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVI 510
Cdd:PRK13641 109 FGPKnfgFSEDEAKEKALkwlkkvglsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLF 188
|
170 180 190
....*....|....*....|....*....|..
gi 22328793 511 KRFiLHAKKTAFVVEHDFIMATYLADRVIVYE 542
Cdd:PRK13641 189 KDY-QKAGHTVILVTHNMDDVAEYADDVLVLE 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
103-275 |
1.05e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.27 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGklkpnLGRFTS-------------PPDWQEILTHFRGSELQNYFTriLEDNLKAIIK 169
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAG-----LEDITSgdlfigekrmndvPPAERGVGMVFQSYALYPHLS--VAENMSFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 170 PQYVDhipravkgnvgevldqKDERDKKAELCAD-LELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLD 248
Cdd:PRK11000 102 LAGAK----------------KEEINQRVNQVAEvLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190
....*....|....*....|....*....|.
gi 22328793 249 ----VKQRLKAAQVVRSLlrpNSYVIVVEHD 275
Cdd:PRK11000 166 aalrVQMRIEISRLHKRL---GRTMIYVTHD 193
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
375-532 |
1.08e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 375 QIIVMLGENGTGKTTFIRMLAGLLKPDdtegpdreipefnvsykpqkispkfqnsvrhllhqKIRDSYMHPQFMSDVMKP 454
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPP-----------------------------------GGGVIYIDGEDILEEVLD 47
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328793 455 LQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFILHAKKTAFVVehDFIMAT 532
Cdd:smart00382 48 QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNL--TVILTT 123
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
9-70 |
1.11e-07 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 50.86 E-value: 1.11e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 9 AIVSSDRCKpkKCRqECKKSCPVVktgklCIEVTVGsKLAFISEELCIGCGICVKKCPFEAI 70
Cdd:cd10549 73 AEIDEEKCI--GCG-LCVKVCPVD-----AITLEDE-LEIVIDKEKCIGCGICAEVCPVNAI 125
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
375-540 |
1.12e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 53.24 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 375 QIIVMLGENGTGKTTFIRMLAGLLKPDDTE----GpdREIpefnVSYKPQKISpkfqnsvRHLLhqkirdsyMHPQFMS- 449
Cdd:PRK13548 29 EVVAILGPNGAGKSTLLRALSGELSPDSGEvrlnG--RPL----ADWSPAELA-------RRRA--------VLPQHSSl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 450 -------DVMK----PLQIEQLMDQEVVN------------------LSGGELQRVAL--TLC-LGKPAD---IYLIDEP 494
Cdd:PRK13548 88 sfpftveEVVAmgraPHGLSRAEDDALVAaalaqvdlahlagrdypqLSGGEQQRVQLarVLAqLWEPDGpprWLLLDEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22328793 495 SAYLDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIV 540
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVL 213
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
7-73 |
1.18e-07 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 51.20 E-value: 1.18e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 7 RIAIV-SSDRCKPKKCRQ----ECKKSCPVvktGklCIEVTVGSKLafISEELCIGCGICVKKCPFEAIQII 73
Cdd:COG1142 37 RIRVVrKAGVSAPVQCRHcedaPCAEVCPV---G--AITRDDGAVV--VDEEKCIGCGLCVLACPFGAITMV 101
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
357-511 |
1.20e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.97 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 357 KTQGNFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPD------DTEG----PDREIPEFNVSYKPQKISPKF 426
Cdd:PRK10895 17 RVVEDVSLTVNSGE-----IVGLLGPNGAGKTTTFYMVVGIVPRDagniiiDDEDisllPLHARARRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 427 QNSVRHLLHQ--KIRDSYMHPQF---MSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSE 501
Cdd:PRK10895 92 RLSVYDNLMAvlQIRDDLSAEQRedrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170
....*....|
gi 22328793 502 QRIVASKVIK 511
Cdd:PRK10895 172 SVIDIKRIIE 181
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
101-243 |
1.29e-07 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 52.93 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEIlTH---FRGSEL--------QNYFTRI-LEDNLKAII 168
Cdd:cd03218 24 KQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL--DGQDI-TKlpmHKRARLgigylpqeASIFRKLtVEENILAVL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22328793 169 KPQYVDhipravkgnvgevldqKDERDKKAE-LCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEP 243
Cdd:cd03218 101 EIRGLS----------------KKEREEKLEeLLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
91-277 |
1.39e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.73 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 91 TFKLHrlpvprPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEIlthfrgSELQNYFTRilednLKAIIKP 170
Cdd:TIGR00958 501 TFTLH------PGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL--DGVPL------VQYDHHYLH-----RQVALVG 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 171 QYVDHIPRAVKGNVGEVLDQKDERDKKA---ELCAD---LELNQVIDRDV----ENLSGGELQRFAIAVVAIQNAEIYMF 240
Cdd:TIGR00958 562 QEPVLFSGSVRENIAYGLTDTPDEEIMAaakAANAHdfiMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190
....*....|....*....|....*....|....*..
gi 22328793 241 DEPSSYLDVkQRLKAAQVVRSllRPNSYVIVVEHDLS 277
Cdd:TIGR00958 642 DEATSALDA-ECEQLLQESRS--RASRTVLLIAHRLS 675
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
101-252 |
1.39e-07 |
|
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: 52.62 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR-FTSPPDWQEILTHFRGSEL--QNY--FTRI-LEDNLKaiikpqyvd 174
Cdd:cd03300 24 KEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEiLLDGKDITNLPPHKRPVNTvfQNYalFPHLtVFENIA--------- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328793 175 hIPRAVKGnvgevLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQR 252
Cdd:cd03300 95 -FGLRLKK-----LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLR 166
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
371-543 |
1.48e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 371 FTDSQIIVMLGENGTGKTTFIRMLAGLLKPddTEGP----DREIPEFN-------VSYKPQKISPKFQNSVRHLL----- 434
Cdd:PRK10575 34 FPAGKVTGLIGHNGSGKSTLLKMLGRHQPP--SEGEilldAQPLESWSskafarkVAYLPQQLPAAEGMTVRELVaigry 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 435 -------------HQKIRDSymhpqfMSDV-MKPLQiEQLMDqevvNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDS 500
Cdd:PRK10575 112 pwhgalgrfgaadREKVEEA------ISLVgLKPLA-HRLVD----SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22328793 501 EQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIVYEG 543
Cdd:PRK10575 181 AHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRG 223
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
4-73 |
1.61e-07 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 50.27 E-value: 1.61e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328793 4 RLTRIAIVS---SDRCKPKKCRQ----ECKKSCPvvkTGKLCIEVTVGSKLafISEELCIGCGICVKKCPFEAIQII 73
Cdd:cd10550 29 SLSRIRVVRfepEGLDVPVVCRQcedaPCVEACP---VGAISRDEETGAVV--VDEDKCIGCGMCVEACPFGAIRVD 100
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
8-72 |
2.00e-07 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 48.17 E-value: 2.00e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22328793 8 IAIVSSDRCKpkKCRqECKKSCPVVktgklCIEVTVGSKLAF-ISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG1146 2 MPVIDTDKCI--GCG-ACVEVCPVD-----VLELDEEGKKALvINPEECIGCGACELVCPVGAITV 59
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
101-289 |
2.01e-07 |
|
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: 52.05 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT--------SPPDwqEILThfRG----SELQNYFTRI-LEDNLKai 167
Cdd:cd03224 24 PEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfdgrditgLPPH--ERAR--AGigyvPEGRRIFPELtVEENLL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 168 ikpqyvdhipravkgnVGEVLDQKDERDKKAELCADL--ELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSS 245
Cdd:cd03224 98 ----------------LGAYARRRAKRKARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22328793 246 YL---------DVKQRLKAAQVVrsllrpnsyVIVVEHDLSVLDYLSDFICCL 289
Cdd:cd03224 162 GLapkiveeifEAIRELRDEGVT---------ILLVEQNARFALEIADRAYVL 205
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
73-278 |
2.13e-07 |
|
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: 53.98 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 73 INLPRDLE-KDTTHRYGANTFKLHRLPVPRP-GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT-SPPDWQEILTHfrg 149
Cdd:TIGR01193 468 NNLNGDIViNDVSYSYGYGSNILSDISLTIKmNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILlNGFSLKDIDRH--- 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 150 sELQNYFTRILEDNLkaIIKPQYVDHIPRAVKGNVGEvlDQKDERDKKAELCADLE-----LNQVIDRDVENLSGGELQR 224
Cdd:TIGR01193 545 -TLRQFINYLPQEPY--IFSGSILENLLLGAKENVSQ--DEIWAACEIAEIKDDIEnmplgYQTELSEEGSSISGGQKQR 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 225 FAIAVVAIQNAEIYMFDEPSSYLDVkqrLKAAQVVRSLLRPNSYVIV-VEHDLSV 278
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDT---ITEKKIVNNLLNLQDKTIIfVAHRLSV 671
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
18-73 |
2.13e-07 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 50.09 E-value: 2.13e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 18 PKKCRQ--ECKKSCPV----VKTGKLCIEVTVgsklafISEELCIGCGICVKKCPFEAIQII 73
Cdd:cd10549 5 PEKCIGcgICVKACPTdaieLGPNGAIARGPE------IDEDKCVFCGACVEVCPTGAIELT 60
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
103-276 |
2.19e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.20 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPDWQEILT-HFRGSELQNY-------FTRI-LEDNLKAIIKpqyv 173
Cdd:PRK10895 29 GEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYlpqeasiFRRLsVYDNLMAVLQ---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 174 dhipravkgnVGEVLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRL 253
Cdd:PRK10895 105 ----------IRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180
....*....|....*....|...
gi 22328793 254 KAAQVVRSLLRPNSYVIVVEHDL 276
Cdd:PRK10895 175 DIKRIIEHLRDSGLGVLITDHNV 197
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
101-281 |
2.36e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 52.38 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdWQ-EILTHFRGSElQNYFTR----ILEDNLKAIiKPQyvdh 175
Cdd:PRK10419 36 KSGETVALLGRSGCGKSTLARLLVGLESPSQGNVS----WRgEPLAKLNRAQ-RKAFRRdiqmVFQDSISAV-NPR---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 176 ipRAVKGNVGE------VLDQKDERDKKAELCADLELN-QVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLD 248
Cdd:PRK10419 106 --KTVREIIREplrhllSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 22328793 249 vkqRLKAAQVVRSL--LRPNS---YVIVVeHDLSVLDY 281
Cdd:PRK10419 184 ---LVLQAGVIRLLkkLQQQFgtaCLFIT-HDLRLVER 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
69-264 |
2.43e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 53.18 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 69 AIQIINLprdlekdtTHRYGANTFkLHR--LPVPrPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRftsppdwqeILth 146
Cdd:COG3842 5 ALELENV--------SKRYGDVTA-LDDvsLSIE-PGEFVALLGPSGCGKTTLLRMIAGFETPDSGR---------IL-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 147 FRGSEL--------------QNY--F---TrilednlkaiikpqyvdhipraVKGNVGEVLDQ----KDERDKKA-ELCA 202
Cdd:COG3842 64 LDGRDVtglppekrnvgmvfQDYalFphlT----------------------VAENVAFGLRMrgvpKAEIRARVaELLE 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 203 DLELNQVIDRDVENLSGGELQRFAIA-VVAIQnAEIYMFDEPSSYLDVKQRLKAAQVVRSLLR 264
Cdd:COG3842 122 LVGLEGLADRYPHQLSGGQQQRVALArALAPE-PRVLLLDEPLSALDAKLREEMREELRRLQR 183
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
461-539 |
2.49e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.17 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 461 MDQEVVNLSGGELQRVALTLCLGKPAD--IYLIDEPSAYLDSEQRIVASKVIKRfILHAKKTAFVVEHDFIMATYlADRV 538
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKG-LIDLGNTVILIEHNLDVLSS-ADWI 158
|
.
gi 22328793 539 I 539
Cdd:cd03238 159 I 159
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
361-549 |
2.51e-07 |
|
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: 52.10 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDD----TEGPDREIPEFNvSYKPQkISPKFQNSVrhLLHQ 436
Cdd:cd03252 20 NISLRIKPGE-----VVGIVGRSGSGKSTLTKLIQRFYVPENgrvlVDGHDLALADPA-WLRRQ-VGVVLQENV--LFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 437 KIRDSY--------MHP-----------QFMSDVmkPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAY 497
Cdd:cd03252 91 SIRDNIaladpgmsMERvieaaklagahDFISEL--PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22328793 498 LDSEQRIVASKVIKRFIlhAKKTAFVVEHDfIMATYLADRVIVYEGQPSIDC 549
Cdd:cd03252 169 LDYESEHAIMRNMHDIC--AGRTVIIIAHR-LSTVKNADRIIVMEKGRIVEQ 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
81-304 |
2.80e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.50 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANTFKLHRLPVPRP-GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPpdwQEILTHFRGSELQNYFTRI 159
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPrNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR---GEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 160 LEDNLKAIIKPQYVDHIpraVKGNVGEVLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYM 239
Cdd:PRK13652 84 FQNPDDQIFSPTVEQDI---AFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 240 FDEPSSYLDVKQRLKAAQVVRSLlrPNSY---VIVVEHDLSVLDYLSDFICCL-YGKPGAYGVVTLPFS 304
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDL--PETYgmtVIFSTHQLDLVPEMADYIYVMdKGRIVAYGTVEEIFL 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
364-540 |
2.83e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.78 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPddTEGpdreipefNVS---YKPQKISPKFqnsVRHL---LHQK 437
Cdd:COG4586 43 FTIEPGE-----IVGFIGPNGAGKSTTIKMLTGILVP--TSG--------EVRvlgYVPFKRRKEF---ARRIgvvFGQR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 438 --------IRDSY-----MH--PQ--------FMSDVmkpLQIEQLMDQEVVNLSGGelQR----VALTLcLGKPADIYL 490
Cdd:COG4586 105 sqlwwdlpAIDSFrllkaIYriPDaeykkrldELVEL---LDLGELLDTPVRQLSLG--QRmrceLAAAL-LHRPKILFL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22328793 491 iDEPSAYLDseqrIVASKVIKRFILHAKK----TAFVVEHDfiMA--TYLADRVIV 540
Cdd:COG4586 179 -DEPTIGLD----VVSKEAIREFLKEYNRergtTILLTSHD--MDdiEALCDRVIV 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
375-540 |
3.67e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 52.53 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 375 QIIVMLGENGTGKTTFIRMLAGLLKPDD----TEGPD-REIPEF----NVSYKPQKISPKF---QNSVRHLLHQKIRDSY 442
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGFEQPTAgqimLDGVDlSHVPPYqrpiNMMFQSYALFPHMtveQNIAFGLKQDKLPKAE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 443 MHPQfMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFILHAKKTAF 522
Cdd:PRK11607 126 IASR-VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCV 204
|
170
....*....|....*...
gi 22328793 523 VVEHDFIMATYLADRVIV 540
Cdd:PRK11607 205 MVTHDQEEAMTMAGRIAI 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
101-540 |
3.89e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLkpnlgrftsPPDWQEILTHFRgseLQNYFTRILEDNLKAIIKPQYVDHIPR-A 179
Cdd:PRK15439 35 HAGEVHALLGGNGAGKSTLMKIIAGIV---------PPDSGTLEIGGN---PCARLTPAKAHQLGIYLVPQEPLLFPNlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 180 VKGNV--GEVLDQKDERdKKAELCAdlELNQVIDRDVE--NLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKA 255
Cdd:PRK15439 103 VKENIlfGLPKRQASMQ-KMKQLLA--ALGCQLDLDSSagSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 256 AQVVRSLLRPNSYVIVVEHDLSVLDYLSDFIcclygkpgaygvvtlpfSV-REGInIFLAGfvPTENLRfRDESLTfkvA 334
Cdd:PRK15439 180 FSRIRELLAQGVGIVFISHKLPEIRQLADRI-----------------SVmRDGT-IALSG--KTADLS-TDDIIQ---A 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 335 ETPQESAEEI----QSYARYKYPTMTKTQGNFRLRVSE--GE-FTD-------SQIIVMLGENGTGKTTFIRMLAGLLKP 400
Cdd:PRK15439 236 ITPAAREKSLsasqKLWLELPGNRRQQAAGAPVLTVEDltGEgFRNislevraGEILGLAGVVGAGRTELAETLYGLRPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 401 -------DDTEGPDREI-----------PE--------------FNVS-----YKPQKISPKFQNSVRHLLHQKIRDSYM 443
Cdd:PRK15439 316 rggrimlNGKEINALSTaqrlarglvylPEdrqssglyldaplaWNVCalthnRRGFWIKPARENAVLERYRRALNIKFN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 444 HPqfmsdvmkplqieqlmDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRfiLHAKKTAFV 523
Cdd:PRK15439 396 HA----------------EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRS--IAAQNVAVL 457
|
490
....*....|....*...
gi 22328793 524 -VEHDFIMATYLADRVIV 540
Cdd:PRK15439 458 fISSDLEEIEQMADRVLV 475
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
101-291 |
4.08e-07 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 51.98 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNL---GRFT---------SPPDWQEIlthfRGSELQ----------N-YFT 157
Cdd:COG0444 29 RRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILfdgedllklSEKELRKI----RGREIQmifqdpmtslNpVMT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 158 --RILEDNLKAiikpqyvdHipravkgnvgEVLDQKDERDKKAELcadleLNQV-IDRDVE-------NLSGGELQRFAI 227
Cdd:COG0444 105 vgDQIAEPLRI--------H----------GGLSKAEARERAIEL-----LERVgLPDPERrldryphELSGGMRQRVMI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 228 A---------VVAiqnaeiymfDEPSSYLDV-KQrlkaAQVVRsLLR-----PNSYVIVVEHDLSVLDYLSDFICCLYG 291
Cdd:COG0444 162 AralalepklLIA---------DEPTTALDVtIQ----AQILN-LLKdlqreLGLAILFITHDLGVVAEIADRVAVMYA 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-546 |
4.27e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.58 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 365 RVSEG---EFTDSQIIVMLGENGTGKTTFIRMLAGLLKPDDTEGPDREIPEFNVSYKPQKIS------------PK---F 426
Cdd:PRK14258 21 KILEGvsmEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNlnrlrrqvsmvhPKpnlF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 427 QNSVRHLLHQKIRDSYMHPQFMSD--VMKPLQIEQLMDQ-------EVVNLSGGELQRVALTLCLGKPADIYLIDEPSAY 497
Cdd:PRK14258 101 PMSVYDNVAYGVKIVGWRPKLEIDdiVESALKDADLWDEikhkihkSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22328793 498 LDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIVYEGQPS 546
Cdd:PRK14258 181 LDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNEN 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
102-291 |
4.60e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.14 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT---SPPDWQEILTHFR------GSELQNYFTriLEDNLkaIIKPQY 172
Cdd:PRK13536 66 SGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgVPVPARARLARARigvvpqFDNLDLEFT--VRENL--LVFGRY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 173 VDHIPRAVKGNVGEVLDqkderdkkaelCADLElnQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQR 252
Cdd:PRK13536 142 FGMSTREIEAVIPSLLE-----------FARLE--SKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR 208
|
170 180 190
....*....|....*....|....*....|....*....
gi 22328793 253 LKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCLYG 291
Cdd:PRK13536 209 HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEA 247
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
364-505 |
4.79e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.55 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDDTEGPDREIPEFNVSyKPQKISPKFQNSVRHllhqkirDSYM 443
Cdd:PRK09984 25 LNIHHGE-----MVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQ-REGRLARDIRKSRAN-------TGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 444 HPQF--------MSDVM-----------------KPLQIEQLMD------------QEVVNLSGGELQRVALTLCLGKPA 486
Cdd:PRK09984 92 FQQFnlvnrlsvLENVLigalgstpfwrtcfswfTREQKQRALQaltrvgmvhfahQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180
....*....|....*....|
gi 22328793 487 DIYLIDEPSAYLDSEQ-RIV 505
Cdd:PRK09984 172 KVILADEPIASLDPESaRIV 191
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
364-545 |
5.34e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 51.40 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPDD---------TEGPDRE----------IPEFNV------SYK 418
Cdd:COG4525 28 LTIESGEFV-----VALGASGCGKTTLLNLIAGFLAPSSgeitldgvpVTGPGADrgvvfqkdalLPWLNVldnvafGLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 419 PQKISPK-FQNSVRHLLHQkirdsymhpqfmsdvmkpLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAY 497
Cdd:COG4525 103 LRGVPKAeRRARAEELLAL------------------VGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22328793 498 LDSEQRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIVYEGQP 545
Cdd:COG4525 165 LDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGP 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
81-277 |
5.75e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 50.86 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANTFkLHRLPVP-RPGQVLGLVGTNGIGKSTALK-------ILAGKLKPNLGRFTSPPDWQEILTHFRGSEL 152
Cdd:PRK09493 5 KNVSKHFGPTQV-LHNIDLNiDQGEVVVIIGPSGSGKSTLLRcinkleeITSGDLIVDGLKVNDPKVDERLIRQEAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 153 QNYFtriLEDNLKAIikpQYVDHIPRAVKGnvgevLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIA-VVA 231
Cdd:PRK09493 84 QQFY---LFPHLTAL---ENVMFGPLRVRG-----ASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIArALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22328793 232 IQnAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLS 277
Cdd:PRK09493 153 VK-PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
364-544 |
6.21e-07 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 50.62 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDdtEGP----DREIPEFNV--------SYKPQKISPKFQNSVR 431
Cdd:cd03218 21 LSVKQGE-----IVGLLGPNGAGKTTTFYMIVGLVKPD--SGKilldGQDITKLPMhkrarlgiGYLPQEASIFRKLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 432 ---------HLLHQKIRDsymhpQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSeq 502
Cdd:cd03218 94 enilavleiRGLSKKERE-----EKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP-- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22328793 503 riVASKVIKRFILHAKKTAFVV---EHDFIMATYLADRV-IVYEGQ 544
Cdd:cd03218 167 --IAVQDIQKIIKILKDRGIGVlitDHNVRETLSITDRAyIIYEGK 210
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
2-73 |
6.26e-07 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 49.18 E-value: 6.26e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328793 2 ADRLTRI--AIVSSDRC----KPKKCRQeCKKSCPvvkTGKLCIEVTVGSKLAFISEELCIGCGICVKKCPFEAIQII 73
Cdd:cd16373 77 EEQKVKMgvAVIDKDRClawqGGTDCGV-CVEACP---TEAIAIVLEDDVLRPVVDEDKCVGCGLCEYVCPVEPPKAI 150
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
99-264 |
6.87e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.36 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 99 VPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTS------PPDWQEI-------------LTHFRGSELQNYFTRI 159
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSvllngmPIDAKEMraisayvqqddlfIPTLTVREHLMFQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 160 -LEDNLKAIIKPQYVDhipravkgnvgEVLDQKDERDkkaelCADLELNqvIDRDVENLSGGELQRFAIAVVAIQNAEIY 238
Cdd:TIGR00955 127 rMPRRVTKKEKRERVD-----------EVLQALGLRK-----CANTRIG--VPGRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180
....*....|....*....|....*.
gi 22328793 239 MFDEPSSYLDvkqRLKAAQVVRSLLR 264
Cdd:TIGR00955 189 FCDEPTSGLD---SFMAYSVVQVLKG 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
364-543 |
7.71e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.86 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKPDD----TEGPDREIPEfNVSYKPQKISPKFQNSVRHLLHQKIR 439
Cdd:PRK13633 31 LEVKKGEF-----LVILGRNGSGKSTIAKHMNALLIPSEgkvyVDGLDTSDEE-NLWDIRNKAGMVFQNPDNQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 440 -DSYMHPQFMSdvMKPLQIEQLMDQ--EVVN-----------LSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIV 505
Cdd:PRK13633 105 eDVAFGPENLG--IPPEEIRERVDEslKKVGmyeyrrhaphlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 22328793 506 ASKVIKRFILHAKKTAFVVEHdFIMATYLADRVIVYEG 543
Cdd:PRK13633 183 VVNTIKELNKKYGITIILITH-YMEEAVEADRIIVMDS 219
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
45-74 |
7.88e-07 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 47.03 E-value: 7.88e-07
10 20 30
....*....|....*....|....*....|
gi 22328793 45 SKLAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:COG2768 3 LGKPYVDEEKCIGCGACVKVCPVGAISIED 32
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
101-289 |
8.25e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.50 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSPPdwqeilthfrgselqnyftriledNLKAIIKPQYVdHIPRAV 180
Cdd:PRK09544 28 KPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------------------KLRIGYVPQKL-YLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 181 KGNVGEVLDQKDERdKKAELCADLELNQ---VIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQ 257
Cdd:PRK09544 83 PLTVNRFLRLRPGT-KKEDILPALKRVQaghLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190
....*....|....*....|....*....|...
gi 22328793 258 VVRSLLRP-NSYVIVVEHDLSVLDYLSDFICCL 289
Cdd:PRK09544 162 LIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
101-306 |
8.49e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.76 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSELQNY-------------FTRI-LEDNLKA 166
Cdd:PRK11300 29 REQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIL-----------LRGQHIEGLpghqiarmgvvrtFQHVrLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 167 IIKPQYVDHipRAVKGNVGEVL--------DQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIY 238
Cdd:PRK11300 98 IENLLVAQH--QQLKTGLFSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 239 MFDEPSSYLDVKQRLKAAQVVRSLLRP-NSYVIVVEHDLSVLDYLSDFICCL-YGKPGAYGvvtLPFSVR 306
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVnQGTPLANG---TPEEIR 242
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
102-277 |
8.54e-07 |
|
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: 50.30 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEILTHFRgSELQNYFTRILEDNLKaiikpqyvdhIPRAVK 181
Cdd:cd03254 28 PGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI--DGIDIRDISR-KSLRSMIGVVLQDTFL----------FSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 182 GNVgeVLDQKDERDKK-AELCADLELNQVIDR-----------DVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDV 249
Cdd:cd03254 95 ENI--RLGRPNATDEEvIEAAKEAGAHDFIMKlpngydtvlgeNGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190
....*....|....*....|....*....|
gi 22328793 250 K--QRLKAAqvVRSLLRpNSYVIVVEHDLS 277
Cdd:cd03254 173 EteKLIQEA--LEKLMK-GRTSIIIAHRLS 199
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
103-293 |
8.83e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.82 E-value: 8.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT----SPPDWQEILTHFR---GSELQNYFTRILEDNLKAIIK--PQyv 173
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvDITDKKVKLSDIRkkvGLVFQYPEYQLFEETIEKDIAfgPI-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 174 dhipravkgNVGEVLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRL 253
Cdd:PRK13637 111 ---------NLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22328793 254 KAAQVVRSLLRP-NSYVIVVEHDLSVLDYLSDFI-------CCLYGKP 293
Cdd:PRK13637 182 EILNKIKELHKEyNMTIILVSHSMEDVAKLADRIivmnkgkCELQGTP 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
104-291 |
9.09e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.81 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 104 QVLGLVGTNGIGKSTALKIL------AGKLKPNlGRftsppdwqeilTHFRGSELqnYFTRILEDNLK---AIIKPQyVD 174
Cdd:PRK14258 34 KVTAIIGPSGCGKSTFLKCLnrmnelESEVRVE-GR-----------VEFFNQNI--YERRVNLNRLRrqvSMVHPK-PN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 175 HIPRAVKGNVG------------EVLDQKDERDKKAELCAdlELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDE 242
Cdd:PRK14258 99 LFPMSVYDNVAygvkivgwrpklEIDDIVESALKDADLWD--EIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22328793 243 PSSYLDVKQRLKAAQVVRSL-LRPNSYVIVVEHDLSVLDYLSDFICCLYG 291
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
101-289 |
9.71e-07 |
|
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: 49.47 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPnlgrftsppdwqeilTHFRGSELQNYFTRILeDNLKAIIKpqYVD----HI 176
Cdd:cd03213 33 KPGELTAIMGPSGAGKSTLLNALAGRRTG---------------LGVSGEVLINGRPLDK-RSFRKIIG--YVPqddiLH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 177 PRAvkgNVGEVLDQKderdkkAELcadlelnqvidrdvENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAA 256
Cdd:cd03213 95 PTL---TVRETLMFA------AKL--------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190
....*....|....*....|....*....|....
gi 22328793 257 QVVRSLLRPNSYVIVVEHDLSVLDY-LSDFICCL 289
Cdd:cd03213 152 SLLRRLADTGRTIICSIHQPSSEIFeLFDKLLLL 185
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
364-543 |
1.14e-06 |
|
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: 49.89 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDDTE----GPD-REIPEFNVSYKPQKISPKFQNSvrHLLHQK- 437
Cdd:cd03258 26 LSVPKGE-----IFGIIGRSGAGKSTLIRCINGLERPTSGSvlvdGTDlTLLSGKELRKARRRIGMIFQHF--NLLSSRt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 438 IRDSYMHP---QFMSDVMKPLQIEQLMdqEVV-----------NLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSE-- 501
Cdd:cd03258 99 VFENVALPleiAGVPKAEIEERVLELL--ELVgledkadaypaQLSGGQKQRVGIARALANNPKVLLCDEATSALDPEtt 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22328793 502 QRIVA--SKVIKRFILhakkTAFVVEHDFIMATYLADRVIVYEG 543
Cdd:cd03258 177 QSILAllRDINRELGL----TIVLITHEMEVVKRICDRVAVMEK 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
101-277 |
1.15e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 50.13 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------TSPP--DWQEILTHFR---GSELQNYFTRILEDNLKAI 167
Cdd:PRK11264 27 KPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidTARSlsQQKGLIRQLRqhvGFVFQNFNLFPHRTVLENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 168 IKPqyvdhiPRAVKGnvgevlDQKDERDKKA-ELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSY 246
Cdd:PRK11264 107 IEG------PVIVKG------EPKEEATARArELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190
....*....|....*....|....*....|.
gi 22328793 247 LDVKQRLKAAQVVRSLLRPNSYVIVVEHDLS 277
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
375-540 |
1.17e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.17 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 375 QIIVMLGENGTGKTTFIRMLAGLLKPDDTEG--PDREIPEFNVSYKPQKISPKFQNSVRHL-LHQKIRDSYMHPQFMSDV 451
Cdd:PRK15112 40 QTLAIIGENGSGKSTLAKMLAGMIEPTSGELliDDHPLHFGDYSYRSQRIRMIFQDPSTSLnPRQRISQILDFPLRLNTD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 452 MKPLQIEQLMDQEVVN--------------LSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRivaSKVIKRFI-LH 516
Cdd:PRK15112 120 LEPEQREKQIIETLRQvgllpdhasyyphmLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR---SQLINLMLeLQ 196
|
170 180
....*....|....*....|....*..
gi 22328793 517 AKKT---AFVVEHdFIMATYLADRVIV 540
Cdd:PRK15112 197 EKQGisyIYVTQH-LGMMKHISDQVLV 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
377-544 |
1.25e-06 |
|
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: 48.75 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 377 IVMLGENGTGKTTFIRMLAGLLKPddTEGpdreipefnvsykpqkispkfqnSVRhLLHQKIRDSYM--HPQFMSDVMkp 454
Cdd:cd03246 31 LAIIGPSGSGKSTLARLILGLLRP--TSG-----------------------RVR-LDGADISQWDPneLGDHVGYLP-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 455 lQIEQLMDQEVVN--LSGGELQRVALTLCL-GKPAdIYLIDEPSAYLDSEQRIVASKVIKRFILhAKKTAFVVEHDfiMA 531
Cdd:cd03246 83 -QDDELFSGSIAEniLSGGQRQRLGLARALyGNPR-ILVLDEPNSHLDVEGERALNQAIAALKA-AGATRIVIAHR--PE 157
|
170
....*....|....
gi 22328793 532 TY-LADRVIVYEGQ 544
Cdd:cd03246 158 TLaSADRILVLEDG 171
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
50-71 |
1.27e-06 |
|
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 459642 [Multi-domain] Cd Length: 24 Bit Score: 44.93 E-value: 1.27e-06
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
364-542 |
1.35e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 50.80 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKP----------DDTEGPDREIPEFnvsyKPQKISPKFQnSVRHL 433
Cdd:PRK10070 49 LAIEEGE-----IFVIMGLSGSGKSTMVRLLNRLIEPtrgqvlidgvDIAKISDAELREV----RRKKIAMVFQ-SFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 434 LHQKIRDSYMHPQFMS------------DVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSE 501
Cdd:PRK10070 119 PHMTVLDNTAFGMELAginaeerrekalDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22328793 502 QRIVASKVIKRFILHAKKTAFVVEHDFIMATYLADRVIVYE 542
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
356-542 |
1.36e-06 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 50.53 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 356 TKTQGNFR------LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDdtEG---------------PDREI---- 410
Cdd:COG1118 9 SKRFGSFTllddvsLEIASGE-----LVALLGPSGSGKTTLLRIIAGLETPD--SGrivlngrdlftnlppRERRVgfvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 411 ------PEFNVsykpqkispkFQN-----SVRHLLHQKIRDSYMHpqfmsdVMKPLQIEQLMDQEVVNLSGGELQRVALt 479
Cdd:COG1118 82 qhyalfPHMTV----------AENiafglRVRPPSKAEIRARVEE------LLELVQLEGLADRYPSQLSGGQRQRVAL- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 480 lclgkpA-------DIYLIDEP-SAyLDS----EQRIVASKVIKRFilhaKKTAFVVEHDFIMATYLADRVIVYE 542
Cdd:COG1118 145 ------AralavepEVLLLDEPfGA-LDAkvrkELRRWLRRLHDEL----GGTTVFVTHDQEEALELADRVVVMN 208
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
372-540 |
1.51e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.09 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 372 TDSQIIVMLGENGTGKTTFIRMLAGLLkpDDTEG-----PDREIPEfNVSYKPQKISPKFQNSVRHLLHQKIRDSYM--- 443
Cdd:PRK13642 31 TKGEWVSIIGQNGSGKSTTARLIDGLF--EEFEGkvkidGELLTAE-NVWNLRRKIGMVFQNPDNQFVGATVEDDVAfgm 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 444 ------HPQFMSDVMKPLQIEQLMD---QEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFI 514
Cdd:PRK13642 108 enqgipREEMIKRVDEALLAVNMLDfktREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIK 187
|
170 180
....*....|....*....|....*.
gi 22328793 515 LHAKKTAFVVEHDFIMATYlADRVIV 540
Cdd:PRK13642 188 EKYQLTVLSITHDLDEAAS-SDRILV 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
322-540 |
1.53e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 49.69 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 322 LRFRDESLTFKVAETPQESAEEIQSYARYKYPtmtktqGNFR------LRVSEGEftdsqIIVMLGENGTGKTTFIRMLA 395
Cdd:COG1134 5 IEVENVSKSYRLYHEPSRSLKELLLRRRRTRR------EEFWalkdvsFEVERGE-----SVGIIGRNGAGKSTLLKLIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 396 GLLKPddTEG-------------------PD---REipefNV-------SYKPQKISPKFqnsvrhllhQKIRDsymhpq 446
Cdd:COG1134 74 GILEP--TSGrvevngrvsallelgagfhPEltgRE----NIylngrllGLSRKEIDEKF---------DEIVE------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 447 FmSDvmkplqIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSE-QRivasKVIKRF--ILHAKKTAFV 523
Cdd:COG1134 133 F-AE------LGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQK----KCLARIreLRESGRTVIF 201
|
250
....*....|....*..
gi 22328793 524 VEHDFIMATYLADRVIV 540
Cdd:COG1134 202 VSHSMGAVRRLCDRAIW 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
369-500 |
1.63e-06 |
|
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: 49.58 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 369 GEFTDSQIIVMLGENGTGKTTFIRMLAGLLKPDDT---------EGPDREIPEFNVSYKPQkispkFQNSVRHL------ 433
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTtsgqilfngQPRKPDQFQKCVAYVRQ-----DDILLPGLtvretl 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328793 434 -------LHQKIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDS 500
Cdd:cd03234 103 tytailrLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
101-286 |
1.87e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.64 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKlkpnlgrftspPDWQ----EILthFRGSELqNYFTRILEDNLKAIIKPQYVDHI 176
Cdd:CHL00131 31 NKGEIHAIMGPNGSGKSTLSKVIAGH-----------PAYKilegDIL--FKGESI-LDLEPEERAHLGIFLAFQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 177 P--------RAVKgNVGEVLDQKDERD---------KKAELcadLELNQV-IDRDV-ENLSGGELQRFAIAVVAIQNAEI 237
Cdd:CHL00131 97 PgvsnadflRLAY-NSKRKFQGLPELDplefleiinEKLKL---VGMDPSfLSRNVnEGFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22328793 238 YMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLS-DFI 286
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYV 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
101-279 |
1.97e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.10 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFtsppdWqeilthFRG---SELQNYFTRILEDNLKAIIKpqyvDH-- 175
Cdd:PRK10908 26 RPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI-----W------FSGhdiTRLKNREVPFLRRQIGMIFQ----DHhl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 176 -IPRAVKGNVGE--VLDQKDERDKKAELCADLELNQVIDRDVE---NLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDV 249
Cdd:PRK10908 91 lMDRTVYDNVAIplIIAGASGDDIRRRVSAALDKVGLLDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190
....*....|....*....|....*....|
gi 22328793 250 KQRLKAAQVVRSLLRPNSYVIVVEHDLSVL 279
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
363-513 |
1.98e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.55 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 363 RLRVSEGEFTDSQIIVMLGENGTGKTTFIRMLAGLLKP------DDTEGPDREIPEFNV--SYKPQKISPKFQNSVRHLL 434
Cdd:PRK03695 11 RLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGsgsiqfAGQPLEAWSAAELARhrAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 435 --HQ-KIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALT-LCL-----GKP-ADIYLIDEPSAYLDSEQRI 504
Cdd:PRK03695 91 tlHQpDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAaVVLqvwpdINPaGQLLLLDEPMNSLDVAQQA 170
|
....*....
gi 22328793 505 VASKVIKRF 513
Cdd:PRK03695 171 ALDRLLSEL 179
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
380-540 |
2.10e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 49.63 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 380 LGENGTGKTTFIRMLAGLLKPddTEGP----DREI-PEF-NVSYKP--QKISPKFQNSVRHLLHQKI-RDSYMHPQ-F-M 448
Cdd:PRK13634 39 IGHTGSGKSTLLQHLNGLLQP--TSGTvtigERVItAGKkNKKLKPlrKKVGIVFQFPEHQLFEETVeKDICFGPMnFgV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 449 SD------VMKPLQI----EQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRivaSKVIKRFI-LHA 517
Cdd:PRK13634 117 SEedakqkAREMIELvglpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR---KEMMEMFYkLHK 193
|
170 180
....*....|....*....|....*
gi 22328793 518 KK--TAFVVEHDFIMATYLADRVIV 540
Cdd:PRK13634 194 EKglTTVLVTHSMEDAARYADQIVV 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
81-276 |
2.18e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 48.98 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANTFKLHrLPVPrPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdWQ-EILTHFRGSElqnyftR- 158
Cdd:COG3840 5 DDLTYRYGDFPLRFD-LTIA-AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIL----WNgQDLTALPPAE------Rp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 159 --IL--EDNLKAiikpqyvdHIprAVKGNVGEVLDQK-----DERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAV 229
Cdd:COG3840 73 vsMLfqENNLFP--------HL--TVAQNIGLGLRPGlkltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22328793 230 VAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRP-NSYVIVVEHDL 276
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDP 190
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
81-277 |
2.23e-06 |
|
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: 49.15 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGA---NTFKLHRLPVPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEIlthfRGSELQNY-- 155
Cdd:cd03251 4 KNVTFRYPGdgpPVLRDISLDIPA-GETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI--DGHDV----RDYTLASLrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 156 -----------FTRILEDNLkAIIKPQYV-DHIPRAVK-GNVGEVLDQKDErdkkaelcadlELNQVI-DRDVeNLSGGE 221
Cdd:cd03251 77 qiglvsqdvflFNDTVAENI-AYGRPGATrEEVEEAARaANAHEFIMELPE-----------GYDTVIgERGV-KLSGGQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 222 LQRFAIAVVAIQNAEIYMFDEPSSYLD-VKQRLkaaqVVRSL--LRPNSYVIVVEHDLS 277
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDtESERL----VQAALerLMKNRTTFVIAHRLS 198
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
106-275 |
2.26e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 106 LGLVGTNGIGKSTALKILAGKLKPNLGR-FTSPPDWQEILT--HFRGSELQN----YFTR----ILEDNLKAiikpqyvd 174
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTvFRSAKVRMAVFSqhHVDGLDLSSnpllYMMRcfpgVPEQKLRA-------- 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 175 HIpravkGNVGevldqkderdkkaeLCADLELnqvidRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDvkqrLK 254
Cdd:PLN03073 610 HL-----GSFG--------------VTGNLAL-----QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LD 661
|
170 180
....*....|....*....|..
gi 22328793 255 AAQ-VVRSLLRPNSYVIVVEHD 275
Cdd:PLN03073 662 AVEaLIQGLVLFQGGVLMVSHD 683
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
81-284 |
2.42e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.46 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANTFKLHRLPVPRP-GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFtsppdwqeilthFRGSELQNYFTRI 159
Cdd:PRK13636 9 EELNYNYSDGTHALKGININIKkGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI------------LFDGKPIDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 160 LEDNLKAI-IKPQYVDH------IPRAVK-GNVGEVLDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVA 231
Cdd:PRK13636 77 LMKLRESVgMVFQDPDNqlfsasVYQDVSfGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22328793 232 IQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVV-EHDLSVLDYLSD 284
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIaTHDIDIVPLYCD 210
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
50-74 |
2.59e-06 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 47.01 E-value: 2.59e-06
10 20
....*....|....*....|....*
gi 22328793 50 ISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:cd10549 3 YDPEKCIGCGICVKACPTDAIELGP 27
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
2-76 |
2.77e-06 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 49.16 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 2 ADRLTRIAIVSSDrcKPKKCRQECKKSCpvvkTG-KLCIE------VTVGSKLAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:PRK07118 190 KSARVFVACNSKD--KGKAVKKVCEVGC----IGcGKCVKacpagaITMENNLAVIDQEKCTSCGKCVEKCPTKAIRILN 263
|
..
gi 22328793 75 LP 76
Cdd:PRK07118 264 KP 265
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
461-539 |
3.14e-06 |
|
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: 48.41 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 461 MDQEVVNLSGGELQRVALTLCLGKPAD--IYLIDEPSAYL---DSEQRIVASKVIKrfilHAKKTAFVVEHD--FIMAty 533
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLhprDNDRLIETLKRLR----DLGNTVLVVEHDedTIRA-- 204
|
....*.
gi 22328793 534 lADRVI 539
Cdd:cd03270 205 -ADHVI 209
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
16-74 |
3.18e-06 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 48.95 E-value: 3.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 16 CKPKKCRQECKKSCPVVKTGKLCIEVTVGSKLAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:COG1145 145 AILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKD 203
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
102-278 |
3.49e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.11 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRF--------TSPPDWQEIL--THFrGSELQNYFtriLEDNLKAiikPQ 171
Cdd:PRK10535 33 AGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrvagqdvaTLDADALAQLrrEHF-GFIFQRYH---LLSHLTA---AQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 172 YVDhIPrAVKGNVGevldqKDERDKKA-ELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVK 250
Cdd:PRK10535 106 NVE-VP-AVYAGLE-----RKQRLLRAqELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180
....*....|....*....|....*...
gi 22328793 251 QRLKAAQVVRSLLRPNSYVIVVEHDLSV 278
Cdd:PRK10535 179 SGEEVMAILHQLRDRGHTVIIVTHDPQV 206
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
77-284 |
3.50e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.02 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 77 RDLEKdtTHRYGANTFKLHRL----PVP---RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEILTHFRG 149
Cdd:PRK15112 8 RNLSK--TFRYRTGWFRRQTVeavkPLSftlREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG---------ELLIDDHP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 150 SELQNYFTRilEDNLKAIIKPQYVDHIPRAvkgNVGEVLD---------QKDERDKKaelcADLELNQV-IDRDVEN--- 216
Cdd:PRK15112 77 LHFGDYSYR--SQRIRMIFQDPSTSLNPRQ---RISQILDfplrlntdlEPEQREKQ----IIETLRQVgLLPDHASyyp 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 217 --LSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRlkaAQVVRSLLRPN-----SYVIVVEHdLSVLDYLSD 284
Cdd:PRK15112 148 hmLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR---SQLINLMLELQekqgiSYIYVTQH-LGMMKHISD 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
81-291 |
3.65e-06 |
|
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: 48.45 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANTFKLHRLPVPRP-GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSELQNYFTRI 159
Cdd:cd03295 4 ENVTKRYGGGKKAVNNLNLEIAkGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIF-----------IDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 160 LEDNLKAIIkpQYVDHIP-RAVKGNVGEVLD----QKDERDKKA-ELCA--DLELNQVIDRDVENLSGGELQRFAIAVVA 231
Cdd:cd03295 73 LRRKIGYVI--QQIGLFPhMTVEENIALVPKllkwPKEKIRERAdELLAlvGLDPAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 232 IQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRP-NSYVIVVEHDLSVLDYLSDFICCLYG 291
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKN 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
99-276 |
3.83e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 49.03 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 99 VPRpGQVLGLVGTNGIGKSTALKILAGKLKPNlgrftsppDWQEILTHFRGSELQNYFTRILEDNLKAIIKPQYVDHIPR 178
Cdd:PRK13640 30 IPR-GSWTALIGHNGSGKSTISKLINGLLLPD--------DNPNSKITVDGITLTAKTVWDIREKVGIVFQNPDNQFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 179 AVKGNVGEVLDQKD-ERDKKAELCADLeLNQV-----IDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQR 252
Cdd:PRK13640 101 TVGDDVAFGLENRAvPRPEMIKIVRDV-LADVgmldyIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180
....*....|....*....|....*
gi 22328793 253 LKAAQVVRSLLRPNSYVIV-VEHDL 276
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVIsITHDI 204
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
43-81 |
4.36e-06 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 44.66 E-value: 4.36e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 22328793 43 VGSKLAFISEELCIGCGICVKKCPFEAIQIIN--LPRDLEK 81
Cdd:COG2221 5 IGTWPPKIDEEKCIGCGLCVAVCPTGAISLDDgkLVIDEEK 45
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
77-287 |
4.42e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.03 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 77 RDLEKdtthRYGANTFKLHRLPVPRPGQVLGLVGTNGIGKSTALKILAGKLKPNLG--RFTSPPdwqeILTHFRGSELqn 154
Cdd:PRK13537 11 RNVEK----RYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGsiSLCGEP----VPSRARHARQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 155 yftrilednlKAIIKPQYVDHIPR-AVKGNV---GEV--LDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIA 228
Cdd:PRK13537 81 ----------RVGVVPQFDNLDPDfTVRENLlvfGRYfgLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 229 VVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFIC 287
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLC 209
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
78-277 |
4.62e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 49.63 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 78 DLE-KDTTHRY-GANTFKLHRLPVPRP-GQVLGLVGTNGIGKSTALKILAgklkpnlgRFTSPpDWQEILthFRGSELQN 154
Cdd:PRK11176 341 DIEfRNVTFTYpGKEVPALRNINFKIPaGKTVALVGRSGSGKSTIANLLT--------RFYDI-DEGEIL--LDGHDLRD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 155 YFTRILEDNLkAIIKpQYVDHIPRAVKGNVGEVLDQKDERD---KKAELCADLE--------LNQVIDRDVENLSGGELQ 223
Cdd:PRK11176 410 YTLASLRNQV-ALVS-QNVHLFNDTIANNIAYARTEQYSREqieEAARMAYAMDfinkmdngLDTVIGENGVLLSGGQRQ 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22328793 224 RFAIAVVAIQNAEIYMFDEPSSYLDVKQRlKAAQVVRSLLRPNSYVIVVEHDLS 277
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESE-RAIQAALDELQKNRTSLVIAHRLS 540
|
|
| FDH-O_like |
cd10560 |
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ... |
12-72 |
4.91e-06 |
|
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N.
Pssm-ID: 319882 [Multi-domain] Cd Length: 225 Bit Score: 48.15 E-value: 4.91e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 12 SSDRCKpkKCRQE-CKKSCPvvkTGKLcIEVTVGSklAFISEELCIGCGICVKKCPFEAIQI 72
Cdd:cd10560 74 MSDVCK--HCTDAgCLEACP---TGAI-FRTEFGT--VYIQPDICNGCGYCVAACPFGVIDR 127
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
104-281 |
4.93e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 48.69 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 104 QVLGLVGTNGIGKSTALKILAGKLKPNLGrFTSPPDWQeILTHFRGSELQNYFTRILEDNLKAIIK--------PQYV-- 173
Cdd:PRK13631 53 KIYFIIGNSGSGKSTLVTHFNGLIKSKYG-TIQVGDIY-IGDKKNNHELITNPYSKKIKNFKELRRrvsmvfqfPEYQlf 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 174 -DHIPRAVK-GNVGevLDQKDERDKKAelcADLELNQV------IDRDVENLSGGELQRFAIA-VVAIQNaEIYMFDEPS 244
Cdd:PRK13631 131 kDTIEKDIMfGPVA--LGVKKSEAKKL---AKFYLNKMglddsyLERSPFGLSGGQKRRVAIAgILAIQP-EILIFDEPT 204
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22328793 245 SYLDVKQRLKAAQVVRSLLRPNSYVIVV----EHDLSVLDY 281
Cdd:PRK13631 205 AGLDPKGEHEMMQLILDAKANNKTVFVIthtmEHVLEVADE 245
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
101-287 |
5.03e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 49.44 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT----SPPDWQEilthfrgSELQNYFT----RI------LEDNLKa 166
Cdd:PRK11160 364 KAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlngqPIADYSE-------AALRQAISvvsqRVhlfsatLRDNLL- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 167 IIKPQYVDHIPRAVKGNVG-EVLDQKDERdkkaelcadleLNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSS 245
Cdd:PRK11160 436 LAAPNASDEALIEVLQQVGlEKLLEDDKG-----------LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22328793 246 YLDVKQRlkaaQVVRSLLRP---NSYVIVVEHDLSVLDYLsDFIC 287
Cdd:PRK11160 505 GLDAETE----RQILELLAEhaqNKTVLMITHRLTGLEQF-DRIC 544
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
211-285 |
5.52e-06 |
|
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: 48.02 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 211 DRDVENLSGGELQRFAIA------VVAIqnaeIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVL---DY 281
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLAtqigsgLTGV----LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIraaDH 207
|
....
gi 22328793 282 LSDF 285
Cdd:cd03270 208 VIDI 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
104-286 |
6.44e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 49.63 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 104 QVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqeilTHFRGSelqnyftRILEDNLKAIIK-----PQY---VDH 175
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSG------------TVLVGG-------KDIETNLDAVRQslgmcPQHnilFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 176 IPRAVKGNVGEVLDQKDERDKKAELCADLE---LNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQR 252
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWEEAQLEMEAMLEdtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190
....*....|....*....|....*....|....*..
gi 22328793 253 lkaaQVVRSLL---RPNSYVIVVEHDLSVLDYLSDFI 286
Cdd:TIGR01257 1098 ----RSIWDLLlkyRSGRTIIMSTHHMDEADLLGDRI 1130
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
103-290 |
6.76e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.04 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLG---------RFTSPPDWQeiLTHFRGSELQNYFTRI--------LEDNLK 165
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGsivvngqtiNLVRDKDGQ--LKVADKNQLRLLRTRLtmvfqhfnLWSHMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 166 AIikpQYVDHIPRAVKGnvgevLDQKDERDKkaelcADLELNQV-IDRDVE-----NLSGGELQRFAIAVVAIQNAEIYM 239
Cdd:PRK10619 109 VL---ENVMEAPIQVLG-----LSKQEARER-----AVKYLAKVgIDERAQgkypvHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22328793 240 FDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCLY 290
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLH 226
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
201-276 |
7.39e-06 |
|
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: 46.58 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 201 CADLELNQVIDRdvenLSGGELQRFAIAVV----AIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDL 276
Cdd:cd03227 66 AVSAELIFTRLQ----LSGGEKELSALALIlalaSLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP 141
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
101-284 |
7.60e-06 |
|
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: 48.91 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKST-ALKILagKLKPNLG--RFtsppDWQEILThFRGSELQNYFTRIlednlkaiikpQYV---- 173
Cdd:COG4172 310 RRGETLGLVGESGSGKSTlGLALL--RLIPSEGeiRF----DGQDLDG-LSRRALRPLRRRM-----------QVVfqdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 174 ----DhiPRAvkgNVGEV-----------LDQKDERDKKAELCADLELN-QVIDRDVENLSGGELQRFAIAVVAIQNAEI 237
Cdd:COG4172 372 fgslS--PRM---TVGQIiaeglrvhgpgLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22328793 238 YMFDEPSSYLDVKQRlkaAQVVrSLLR------PNSYvIVVEHDLSVLDYLSD 284
Cdd:COG4172 447 LVLDEPTSALDVSVQ---AQIL-DLLRdlqrehGLAY-LFISHDLAVVRALAH 494
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
81-289 |
7.67e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 47.77 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGaNTFKLHR--LPVPRpGQVLGLVGTNGIGKSTALKILAGKLkpnlgrftsPPDWQEILthFRGSELQNYFTR 158
Cdd:COG4604 5 KNVSKRYG-GKVVLDDvsLTIPK-GGITALIGPNGAGKSTLLSMISRLL---------PPDSGEVL--VDGLDVATTPSR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 159 ILEDNLkAIIKPQyvDHIprAVKGNVGEV------------LDQKDERdKKAELCADLELNQVIDRDVENLSGGELQRFA 226
Cdd:COG4604 72 ELAKRL-AILRQE--NHI--NSRLTVRELvafgrfpyskgrLTAEDRE-IIDEAIAYLDLEDLADRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328793 227 IAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRP-NSYVIVVEHDLSVLDYLSDFICCL 289
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAM 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
103-275 |
7.87e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 48.40 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT--------SPPDWQEILTHFrgselQNY--FTRI-LEDNLKAIIKPQ 171
Cdd:PRK09452 40 GEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMldgqdithVPAENRHVNTVF-----QSYalFPHMtVFENVAFGLRMQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 172 YVdhiPRA-VKGNVGEVLdqkderdkkaelcADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVK 250
Cdd:PRK09452 115 KT---PAAeITPRVMEAL-------------RMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190
....*....|....*....|....*....|.
gi 22328793 251 QR------LKAAQvvRSLlrpNSYVIVVEHD 275
Cdd:PRK09452 179 LRkqmqneLKALQ--RKL---GITFVFVTHD 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
355-498 |
9.26e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 355 MTKTQGNFR------LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDdtEGpdrEIpefNVSYKPQKI-SPKFq 427
Cdd:COG3845 11 ITKRFGGVVanddvsLTVRPGE-----IHALLGENGAGKSTLMKILYGLYQPD--SG---EI---LIDGKPVRIrSPRD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 428 nSVRH---LLHQkirdsymHpqFMsDV------------MKPL------------QIEQLMDQ---------EVVNLSGG 471
Cdd:COG3845 77 -AIALgigMVHQ-------H--FM-LVpnltvaenivlgLEPTkggrldrkaaraRIRELSERygldvdpdaKVEDLSVG 145
|
170 180 190
....*....|....*....|....*....|
gi 22328793 472 ELQRVAL--TLCLGkpADIyLI-DEPSAYL 498
Cdd:COG3845 146 EQQRVEIlkALYRG--ARI-LIlDEPTAVL 172
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
101-289 |
9.96e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 9.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGR---------FTSPPDWQEILTHFRGSELQNYFTRILEDNL---KAII 168
Cdd:PRK10982 22 RPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSilfqgkeidFKSSKEALENGISMVHQELNLVLQRSVMDNMwlgRYPT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 169 KPQYVDHipravkgnvgevldQKDERDKKAeLCADLELNqvID-RD-VENLSGGELQRFAIAVVAIQNAEIYMFDEPSSY 246
Cdd:PRK10982 102 KGMFVDQ--------------DKMYRDTKA-IFDELDID--IDpRAkVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22328793 247 LDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCL 289
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
103-276 |
1.05e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.47 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT------SPPDWQEILTHFR---GSELQNYFTRILEDNLKAIIkpqyv 173
Cdd:PRK13646 33 GKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvdditiTHKTKDKYIRPVRkriGMVFQFPESQLFEDTVEREI----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 174 DHIPRAVKGNVGEVldqkdeRDKKAELCADLELNQ-VIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQR 252
Cdd:PRK13646 108 IFGPKNFKMNLDEV------KNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180
....*....|....*....|....*
gi 22328793 253 LKAAQVVRSL-LRPNSYVIVVEHDL 276
Cdd:PRK13646 182 RQVMRLLKSLqTDENKTIILVSHDM 206
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
3-74 |
1.14e-05 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 48.10 E-value: 1.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 3 DRLTRIAIVSSDRCKPKKCRQECKKSCPVVKTGKLCIEVTVGSKLAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:COG4624 41 HVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDD 112
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
364-567 |
1.15e-05 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 47.01 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqIIVMLGENGTGKTTFIR------------MLAGLLKPDDTEGPDREI--------------PEF---- 413
Cdd:PRK09493 22 LNIDQGE-----VVVIIGPSGSGKSTLLRcinkleeitsgdLIVDGLKVNDPKVDERLIrqeagmvfqqfylfPHLtale 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 414 NVSYKPQKispkfqnsVRHLLHQKIRDSYMhpqfmsDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDE 493
Cdd:PRK09493 97 NVMFGPLR--------VRGASKEEAEKQAR------ELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 494 PSAYLDSEQRIVASKVIKRFilhAKK--TAFVVEHDFIMATYLADRVIVYE-GQPSIDCTancPQSLLSG-----MNLFL 565
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDL---AEEgmTMVIVTHEIGFAEKVASRLIFIDkGRIAEDGD---PQVLIKNppsqrLQEFL 236
|
..
gi 22328793 566 SH 567
Cdd:PRK09493 237 QH 238
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
211-539 |
1.23e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.47 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 211 DRDVENLSGGELQRFAIA--VVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHD---LSVLDYLSDF 285
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLAtqIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDedtIRAADYVIDI 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 286 icclygKPGAyGVvtlpfsvrEGINIFLAGfvPTENLRFRDESLTfkVAETPQESAEEIQSYARYKYPTMTKTQG----- 360
Cdd:TIGR00630 563 ------GPGA-GE--------HGGEVVASG--TPEEILANPDSLT--GQYLSGRKKIEVPAERRPGNGKFLTLKGarenn 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 --NFRLRVSEGEFTdsqiiVMLGENGTGKTTFI-----RMLAGLLKPDDTE-GPDREI---------------------- 410
Cdd:TIGR00630 624 lkNITVSIPLGLFT-----CITGVSGSGKSTLIndtlyPALANRLNGAKTVpGRYTSIeglehldkvihidqspigrtpr 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 411 --------------------PE------------FNVS----------------------------------YKPQKISP 424
Cdd:TIGR00630 699 snpatytgvfdeirelfaetPEakvrgytpgrfsFNVKggrceacqgdgvikiemhflpdvyvpcevckgkrYNRETLEV 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 425 KFQN-SVRHLLHQKIRDSYmhpQFMSDVMKPLQ-IEQLMD---------QEVVNLSGGELQRVALTLCLGKPAD---IYL 490
Cdd:TIGR00630 779 KYKGkNIADVLDMTVEEAY---EFFEAVPSISRkLQTLCDvglgyirlgQPATTLSGGEAQRIKLAKELSKRSTgrtLYI 855
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 22328793 491 IDEPSAYLDSEQRIVASKVIKRFIlHAKKTAFVVEHDF-IMATylADRVI 539
Cdd:TIGR00630 856 LDEPTTGLHFDDIKKLLEVLQRLV-DKGNTVVVIEHNLdVIKT--ADYII 902
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
356-515 |
1.29e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 47.41 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 356 TKTQGNFR------LRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDdtEGpdreipefNVSYKPQKISPKFQNS 429
Cdd:COG4152 8 TKRFGDKTavddvsFTVPKGE-----IFGLLGPNGAGKTTTIRIILGILAPD--SG--------EVLWDGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 430 V------RHL---------------LH----QKIRDSymhpqfMSDVMKPLQIEQLMDQEVVNLSGGELQRVAL--TLcL 482
Cdd:COG4152 73 IgylpeeRGLypkmkvgeqlvylarLKglskAEAKRR------ADEWLERLGLGDRANKKVEELSKGNQQKVQLiaAL-L 145
|
170 180 190
....*....|....*....|....*....|...
gi 22328793 483 GKPaDIYLIDEPSAYLDSeqriVASKVIKRFIL 515
Cdd:COG4152 146 HDP-ELLILDEPFSGLDP----VNVELLKDVIR 173
|
|
| PorD_KorD |
TIGR02179 |
2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number ... |
10-73 |
1.33e-05 |
|
2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes a subfamily of delta subunits, representing mostly pyruvate, 2-ketoisovalerate, and 2-oxoglutarate specific enzymes. The delta subunit is the smallest and resembles ferredoxins.
Pssm-ID: 131234 [Multi-domain] Cd Length: 78 Bit Score: 43.48 E-value: 1.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328793 10 IVSSDRCKpkKCRqECKKSCPvvktgKLCIEVTVGsKLAFISEELCIGCGICVKKCPFEAIQII 73
Cdd:TIGR02179 21 VVDKEKCI--KCK-NCWLYCP-----EGAIQEDEG-GFVGIDYDYCKGCGICANVCPVKAIEMV 75
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
184-280 |
1.41e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.42 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 184 VGEVLD--QKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRS 261
Cdd:NF000106 110 IGR*LDlsRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRS 189
|
90 100
....*....|....*....|....*....
gi 22328793 262 LLRPNSYVIV----------VEHDLSVLD 280
Cdd:NF000106 190 MVRDGATVLLttqymeeaeqLAHELTVID 218
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
101-290 |
1.47e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.71 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGK--LKPNLGRFTsppdwqeilthFRGSELQNyftriLEDNLKA----IIKPQYVD 174
Cdd:PRK09580 25 RPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVE-----------FKGKDLLE-----LSPEDRAgegiFMAFQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 175 HIP------------RAVKGNVG-EVLDQKDERDKKAELCADLELNQ-VIDRDV-ENLSGGELQRFAIAVVAIQNAEIYM 239
Cdd:PRK09580 89 EIPgvsnqfflqtalNAVRSYRGqEPLDRFDFQDLMEEKIALLKMPEdLLTRSVnVGFSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22328793 240 FDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLS-DFICCLY 290
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLY 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
349-544 |
1.69e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 46.29 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 349 RYKYPTMTKtqgNFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDdtEGP----DREIPEFNVSYKPqkISP 424
Cdd:COG3840 8 TYRYGDFPL---RFDLTIAAGE-----RVAILGPSGAGKSTLLNLIAGFLPPD--SGRilwnGQDLTALPPAERP--VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 425 KFQ--NSVRHL---------LHQKIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCL--GKPadIYLI 491
Cdd:COG3840 76 LFQenNLFPHLtvaqniglgLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLvrKRP--ILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 492 DEPSAYLDSEQR-----IVASkvikrfiLHAKK--TAFVVEHDFIMATYLADRVI-VYEGQ 544
Cdd:COG3840 154 DEPFSALDPALRqemldLVDE-------LCRERglTVLMVTHDPEDAARIADRVLlVADGR 207
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
361-545 |
1.71e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 46.68 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPDDTE--GPDREIPEFNVS--YKPQK-ISPKFQ-------- 427
Cdd:PRK11831 25 NISLTVPRGKIT-----AIMGPSGIGKTTLLRLIGGQIAPDHGEilFDGENIPAMSRSrlYTVRKrMSMLFQsgalftdm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 428 ---NSVRHLL--HQKIRDSYMHpqfmSDVMKPLQI------EQLMDQEvvnLSGGELQRVALTLCLGKPADIYLIDEPSA 496
Cdd:PRK11831 100 nvfDNVAYPLreHTQLPAPLLH----STVMMKLEAvglrgaAKLMPSE---LSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22328793 497 YLDSEQRIVASKVIKRFILHAKKTAFVVEHD----FIMATY---LADRVIVYEGQP 545
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDvpevLSIADHayiVADKKIVAHGSA 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
101-278 |
2.00e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKST-ALKILagKLKPNLGrftsppdwqEILthFRGSELQNyFTR------------ILED----- 162
Cdd:PRK15134 310 RPGETLGLVGESGSGKSTtGLALL--RLINSQG---------EIW--FDGQPLHN-LNRrqllpvrhriqvVFQDpnssl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 163 ----NLKAIIKPQYVDHIPRAVKGnvgevldQKDERDKKA--ELCADLELNQvidRDVENLSGGELQRFAIAVVAIQNAE 236
Cdd:PRK15134 376 nprlNVLQIIEEGLRVHQPTLSAA-------QREQQVIAVmeEVGLDPETRH---RYPAEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22328793 237 IYMFDEPSSYLD--VKQR----LKAAQVVRSLlrpnSYvIVVEHDLSV 278
Cdd:PRK15134 446 LIILDEPTSSLDktVQAQilalLKSLQQKHQL----AY-LFISHDLHV 488
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
379-540 |
2.08e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 46.67 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 379 MLGENGTGKTTFIRMLAGLLKPddTEGP----DREIPEFNVSYKPQKISPKFQN--------SVRH-----LLHQKIRDS 441
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIEKV--KSGEifynNQAITDDNFEKLRKHIGIVFQNpdnqfvgsIVKYdvafgLENHAVPYD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 442 YMH---PQFMSDVmkplQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFILHAK 518
Cdd:PRK13648 118 EMHrrvSEALKQV----DMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHN 193
|
170 180
....*....|....*....|..
gi 22328793 519 KTAFVVEHDFIMATYlADRVIV 540
Cdd:PRK13648 194 ITIISITHDLSEAME-ADHVIV 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
361-546 |
2.11e-05 |
|
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: 47.49 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRLRVSEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPDDTEG---------PD---REIPEF--------NVSYKPQ 420
Cdd:TIGR03269 18 NISFTIEEGE-----VLGILGRSGAGKSVLMHVLRGMDQYEPTSGriiyhvalcEKcgyVERPSKvgepcpvcGGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 421 KI-----SPKFQNSVRH---LLHQKIRDSYMHPQFMSDVMKPL---------------------QIEQLMDQEVVNLSGG 471
Cdd:TIGR03269 93 EVdfwnlSDKLRRRIRKriaIMLQRTFALYGDDTVLDNVLEALeeigyegkeavgravdliemvQLSHRITHIARDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 472 ELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFILHAKKTAFVVEH------DFI-MATYLADRVIVYEGQ 544
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevieDLSdKAIWLENGEIKEEGT 252
|
..
gi 22328793 545 PS 546
Cdd:TIGR03269 253 PD 254
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
102-287 |
2.52e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEIlthfrgselqnyftrILEDNLKAIIKPQ--YVDHiPRA 179
Cdd:PRK11819 32 PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG---------EA---------------RPAPGIKVGYLPQepQLDP-EKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 180 VKGNV----GEVLDQKDE--------------RDKKAELCADLE----------LNQVIDR------------DVENLSG 219
Cdd:PRK11819 87 VRENVeegvAEVKAALDRfneiyaayaepdadFDALAAEQGELQeiidaadawdLDSQLEIamdalrcppwdaKVTKLSG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 220 GELQRFAIAVVAIQNAEIYMFDEPSSYLDvkqrlkaAQVV----RSLLRPNSYVIVVEHDLSVLDYLSDFIC 287
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLD-------AESVawleQFLHDYPGTVVAVTHDRYFLDNVAGWIL 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
466-542 |
2.63e-05 |
|
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: 46.07 E-value: 2.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 466 VNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRfiLHAKKTAFVVEHDF--IMAtylADRVIVYE 542
Cdd:cd03251 137 VKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALER--LMKNRTTFVIAHRLstIEN---ADRIVVLE 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
81-276 |
2.64e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 46.27 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRY--GANTFKLHRLPVPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT------SPPDWQEILTH----FR 148
Cdd:PRK13647 8 EDLHFRYkdGTKALKGLSLSIPE-GSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvmgrevNAENEKWVRSKvglvFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 149 GSELQNYFTRILEDnlkAIIKPQYVDHIPRAVKGNVGEVLDQKDERDKKaelcadlelnqviDRDVENLSGGELQRFAIA 228
Cdd:PRK13647 87 DPDDQVFSSTVWDD---VAFGPVNMGLDKDEVERRVEEALKAVRMWDFR-------------DKPPYHLSYGQKKRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22328793 229 VVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDL 276
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDV 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
346-543 |
2.75e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 47.25 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 346 SYARYKYPTMTktqgNFRLRVSEGeftdsQIIVMLGENGTGKTTFIRMLAGLLkpDDTEGpdREIPEFNVSYKPQKisPK 425
Cdd:TIGR00957 645 TWARDLPPTLN----GITFSIPEG-----ALVAVVGQVGCGKSSLLSALLAEM--DKVEG--HVHMKGSVAYVPQQ--AW 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 426 FQN-SVR------HLLHQKIRDSYMHP-QFMSDV-MKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSA 496
Cdd:TIGR00957 710 IQNdSLRenilfgKALNEKYYQQVLEAcALLPDLeILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22328793 497 YLDSE-QRIVASKVIKRFILHAKKTAFVVEHDFimaTYL--ADRVIVYEG 543
Cdd:TIGR00957 790 AVDAHvGKHIFEHVIGPEGVLKNKTRILVTHGI---SYLpqVDVIIVMSG 836
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
364-539 |
2.78e-05 |
|
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: 45.89 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGllkpddtegpdreipefnvSYKPQ--KISPKFQNSV--------RHL 433
Cdd:COG4778 32 FSVAAGEC-----VALTGPSGAGKSTLLKCIYG-------------------NYLPDsgSILVRHDGGWvdlaqaspREI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 434 LHqkIRDSYMH--PQFMS--------D-VMKPLqIEQLMDQEV-----------VNL------------SGGELQRVALT 479
Cdd:COG4778 88 LA--LRRRTIGyvSQFLRviprvsalDvVAEPL-LERGVDREEarararellarLNLperlwdlppatfSGGEQQRVNIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328793 480 LCLGKPADIYLIDEPSAYLDSEQRIVaskVIkRFILHAKK--TAFV-VEHDF-IMATyLADRVI 539
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANRAV---VV-ELIEEAKArgTAIIgIFHDEeVREA-VADRVV 223
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
52-73 |
2.97e-05 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 42.04 E-value: 2.97e-05
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
27-72 |
3.08e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 46.78 E-value: 3.08e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 22328793 27 KSCPVVKTGKLCIEVTVgsklAFISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG1148 474 RAIQLLSKGELGVEPSV----AEVDPEKCTGCGRCVEVCPYGAISI 515
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
191-252 |
3.58e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.38 E-value: 3.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 191 KDERDKKAELCAD-LELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQR 252
Cdd:PRK11650 108 KAEIEERVAEAARiLELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
205-287 |
3.70e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.91 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 205 ELNQVIDRDVENLSGGE------LQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKA-AQVVRSLLR-PNSYVIVVEHDL 276
Cdd:cd03240 104 ESNWPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENIEESlAEIIEERKSqKNFQLIVITHDE 183
|
90
....*....|.
gi 22328793 277 SVLDYLSDFIC 287
Cdd:cd03240 184 ELVDAADHIYR 194
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
468-540 |
3.75e-05 |
|
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: 45.30 E-value: 3.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328793 468 LSGGELQRVALTLCLGKPADIYLIDEPSAYLDS--EQRIVASkvIKRfiLHAKKTAFVVEHDF--IMAtylADRVIV 540
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDThtEREIQAA--LRD--VSKGRTTIVIAHRLstIVN---ADKIIV 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
101-256 |
4.04e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 46.38 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAG------KLKPNlG---RFTSPPDWQEIL-------THFRGSelqnyftriLEDNL 164
Cdd:PRK11174 374 PAGQRIALVGPSGAGKTSLLNALLGflpyqgSLKIN-GielRELDPESWRKHLswvgqnpQLPHGT---------LRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 165 kAIIKPQYVDhipravkgnvgEVLDQKDERDKKAELCADLE--LNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDE 242
Cdd:PRK11174 444 -LLGNPDASD-----------EQLQQALENAWVSEFLPLLPqgLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180
....*....|....*....|
gi 22328793 243 PSSYLD------VKQRLKAA 256
Cdd:PRK11174 512 PTASLDahseqlVMQALNAA 531
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
350-546 |
4.06e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.89 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 350 YKYPTMTKTQG----NFRLRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPddTEGP----DREIP--EFNVSYKP 419
Cdd:PRK13649 10 YTYQAGTPFEGralfDVNLTIEDGSYT-----AFIGHTGSGKSTIMQLLNGLHVP--TQGSvrvdDTLITstSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 420 --QKISPKFQNSVRHLLHQKI-RDSYMHPQ-FMSDVMKPLQI-----------EQLMDQEVVNLSGGELQRVALTLCLGK 484
Cdd:PRK13649 83 irKKVGLVFQFPESQLFEETVlKDVAFGPQnFGVSQEEAEALareklalvgisESLFEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 485 PADIYLIDEPSAYLDSEQRIVASKVIKRfiLHAK-KTAFVVEHdfIM---ATYlADRVIVYE-------GQPS 546
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKK--LHQSgMTIVLVTH--LMddvANY-ADFVYVLEkgklvlsGKPK 230
|
|
| DMSOR_beta_like |
cd16371 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
49-72 |
4.26e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319893 [Multi-domain] Cd Length: 140 Bit Score: 43.71 E-value: 4.26e-05
10 20
....*....|....*....|....
gi 22328793 49 FISEELCIGCGICVKKCPFEAIQI 72
Cdd:cd16371 80 VVDQDKCIGCGYCVWACPYGAPQY 103
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
370-537 |
4.41e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.54 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 370 EFTDSQIIVMLGENGTGKTTFIRML--AGLLKPDDTEGPDREIPEFNVsYKP--------QKISPKFQ-----------N 428
Cdd:PRK14239 27 DFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNI-YSPrtdtvdlrKEIGMVFQqpnpfpmsiyeN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 429 SVRHLLHQKIRDSYMHPQFMSDVMKPLQI-EQLMDQ---EVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSeqrI 504
Cdd:PRK14239 106 VVYGLRLKGIKDKQVLDEAVEKSLKGASIwDEVKDRlhdSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDP---I 182
|
170 180 190
....*....|....*....|....*....|....
gi 22328793 505 VASKVIKR-FILHAKKTAFVVEHDFIMATYLADR 537
Cdd:PRK14239 183 SAGKIEETlLGLKDDYTMLLVTRSMQQASRISDR 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
363-523 |
4.77e-05 |
|
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: 44.07 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 363 RLRVSEGEFT--DSQIIVMLGENGTGKTTFIRMLAGL--------LKPDDTegpdreipefNVSYKPQKispkfqnsvrh 432
Cdd:cd03223 14 RVLLKDLSFEikPGDRLLITGPSGTGKSSLFRALAGLwpwgsgriGMPEGE----------DLLFLPQR----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 433 llhqkirdSYMhPQ--FMSDVMKPLQIEqlmdqevvnLSGGELQRVALT-LCLGKPaDIYLIDEPSAYLD--SEQRIVAs 507
Cdd:cd03223 73 --------PYL-PLgtLREQLIYPWDDV---------LSGGEQQRLAFArLLLHKP-KFVFLDEATSALDeeSEDRLYQ- 132
|
170
....*....|....*.
gi 22328793 508 kvikrfILHAKKTAFV 523
Cdd:cd03223 133 ------LLKELGITVI 142
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
49-74 |
4.78e-05 |
|
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).
Pssm-ID: 468407 [Multi-domain] Cd Length: 243 Bit Score: 45.24 E-value: 4.78e-05
10 20
....*....|....*....|....*.
gi 22328793 49 FISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:NF038196 181 FHVTDKCIGCGICAKVCPVNNIEMED 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
108-275 |
5.10e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 108 LVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthfRGSELQ-NYFtrileDNLKAIIKPQyvdhipRAVKGNVGE 186
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIH------------CGTKLEvAYF-----DQHRAELDPE------KTVMDNLAE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 187 vldqkderDKKaelcaDLELNQViDRD------------------VENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLD 248
Cdd:PRK11147 407 --------GKQ-----EVMVNGR-PRHvlgylqdflfhpkramtpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
170 180 190
....*....|....*....|....*....|
gi 22328793 249 VkqrlKAAQVVRSLLrpNSY---VIVVEHD 275
Cdd:PRK11147 473 V----ETLELLEELL--DSYqgtVLLVSHD 496
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
101-262 |
5.75e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTS-------PPDwqEILTHFRG-----SELQNYFTRI-LEDNLKAI 167
Cdd:TIGR00956 85 KPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGvitydgiTPE--EIKKHYRGdvvynAETDVHFPHLtVGETLDFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 168 IKPQYVdhipravkGNVGEVLDQKDERDKKAELCA-----DLELNQVIDRD-VENLSGGELQRFAIAVVAIQNAEIYMFD 241
Cdd:TIGR00956 163 ARCKTP--------QNRPDGVSREEYAKHIADVYMatyglSHTRNTKVGNDfVRGVSGGERKRVSIAEASLGGAKIQCWD 234
|
170 180
....*....|....*....|.
gi 22328793 242 EPSSYLDVKqrlKAAQVVRSL 262
Cdd:TIGR00956 235 NATRGLDSA---TALEFIRAL 252
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
55-78 |
5.81e-05 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 41.00 E-value: 5.81e-05
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
47-70 |
6.49e-05 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 45.17 E-value: 6.49e-05
10 20
....*....|....*....|....
gi 22328793 47 LAFISEELCIGCGICVKKCPFEAI 70
Cdd:PRK06991 79 VAVIDEQLCIGCTLCMQACPVDAI 102
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
92-284 |
6.79e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.34 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 92 FKLHRlpvprpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEILTHFRGSE----------LQNYFT---- 157
Cdd:PRK11308 36 FTLER------GKTLAVVGESGCGKSTLARLLTMIETPTGGELYY--QGQDLLKADPEAQkllrqkiqivFQNPYGslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 158 -----RILEDNLkaIIKPQyvdhipravkgnvgevLDQKDERDKKAELCADLELN-QVIDRDVENLSGGELQRFAIAVVA 231
Cdd:PRK11308 108 rkkvgQILEEPL--LINTS----------------LSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22328793 232 IQNAEIYMFDEPSSYLDVKQRlkaAQVVRSLLRPN-----SYVIvVEHDLSVLDYLSD 284
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVSVQ---AQVLNLMMDLQqelglSYVF-ISHDLSVVEHIAD 223
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
102-248 |
7.01e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.45 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFtsppdwqEILTH-FRGSELQNYFTrilednlkaiikpqYVDHIPrAV 180
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-------QIDGKtATRGDRSRFMA--------------YLGHLP-GL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22328793 181 KGNVGEV--------LDQKDERDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLD 248
Cdd:PRK13543 94 KADLSTLenlhflcgLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
18-79 |
7.20e-05 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 44.60 E-value: 7.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 18 PKKCRQEC------KKSCPV---VKTGKLcievtvgskLAFISEELCIGCGICVKKCPFEAIQIINLPRDL 79
Cdd:COG2878 132 PKGCEYGCigcgdcIKACPFdaiVGAAKG---------MHTVDEDKCTGCGLCVEACPVDCIEMVPVSPTV 193
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
370-544 |
7.26e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 44.90 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 370 EFTDSQIIVMLGENGTGKTTFIRMLAGL--LKPDDTEGPD-----REIPEFNVSYKPQKISPKFQ--NSVRHL------- 433
Cdd:PRK14247 25 EIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEARVSGEvyldgQDIFKMDVIELRRRVQMVFQipNPIPNLsifenva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 434 --------------LHQKIRDSYMHPQFMSDVMKPLqieqlmDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYLD 499
Cdd:PRK14247 105 lglklnrlvkskkeLQERVRWALEKAQLWDEVKDRL------DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22328793 500 SEQrivaSKVIKRFILHAKK--TAFVVEHDFIMATYLADRV-IVYEGQ 544
Cdd:PRK14247 179 PEN----TAKIESLFLELKKdmTIVLVTHFPQQAARISDYVaFLYKGQ 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
468-544 |
8.11e-05 |
|
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: 43.57 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 468 LSGGELQRVALTLCLGKPADIYLIDEPSAYLDseqriVASK--VIKRFILHAKK-TAFVV---EHDFIMAtyLADRVIV- 540
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVD-----VGAKaeIYRLIRELADAgKAVLLissELDELLG--LCDRILVm 177
|
....
gi 22328793 541 YEGQ 544
Cdd:cd03215 178 YEGR 181
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
364-499 |
8.32e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.02 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEFTdsQIivmLGENGTGKTTFIRMLAGLLKPDDTEgpdreipefnVSYKPQKIspkfqnsvrhllhQKIRDSYM 443
Cdd:PRK13538 22 FTLNAGELV--QI---EGPNGAGKTSLLRILAGLARPDAGE----------VLWQGEPI-------------RRQRDEYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 444 -------HPQFMSDVMKPL-------QIEQLMDQEVV------------------NLSGGELQRVALT-LCLGKPAdIYL 490
Cdd:PRK13538 74 qdllylgHQPGIKTELTALenlrfyqRLHGPGDDEALwealaqvglagfedvpvrQLSAGQQRRVALArLWLTRAP-LWI 152
|
....*....
gi 22328793 491 IDEPSAYLD 499
Cdd:PRK13538 153 LDEPFTAID 161
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
102-280 |
8.35e-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: 43.13 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFtsppdwqeilthfrgselqnyftrilednlkAIIKPqyvdhipravk 181
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------------IYIDG----------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 182 gnvgevldqkderDKKAELCADLELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQR------LKA 255
Cdd:smart00382 39 -------------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEalllllEEL 105
|
170 180
....*....|....*....|....*
gi 22328793 256 AQVVRSLLRPNSYVIVVEHDLSVLD 280
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEKDLG 130
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
350-543 |
8.99e-05 |
|
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: 44.38 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 350 YKYPTMTKTQ--GNFRLRVSEGEFTdsqiiVMLGENGTGKTTFIRMLAGLLKPDDTEG--PDREIPEFN----------V 415
Cdd:cd03248 19 FAYPTRPDTLvlQDVSFTLHPGEVT-----ALVGPSGSGKSTVVALLENFYQPQGGQVllDGKPISQYEhkylhskvslV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 416 SYKPQKISPKFQNSVRHLLHQKIRDSYMHPQ-------FMSDVMKPLQIEqlMDQEVVNLSGGELQRVALTLCLGKPADI 488
Cdd:cd03248 94 GQEPVLFARSLQDNIAYGLQSCSFECVKEAAqkahahsFISELASGYDTE--VGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 489 YLIDEPSAYLDSEQRIVASKVIKRFilHAKKTAFVVEHDfIMATYLADRVIVYEG 543
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDW--PERRTVLVIAHR-LSTVERADQILVLDG 223
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
18-74 |
9.03e-05 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 44.60 E-value: 9.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 18 PKKCRQECKKSCPVVKTgKLCIEVTVGSKLAFIS-----EELCIGCGICVKKCPFEAIQIIN 74
Cdd:COG2878 98 PEVAVVRCNGGCEKAKP-KYEYDGIKDCRAAVIGgpkgcEYGCIGCGDCIKACPFDAIVGAA 158
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
364-519 |
9.54e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 44.25 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 364 LRVSEGEftdsqiIV-MLGENGTGKTTFIRMLAGLLKPDdtEGP----DREI---PEFN-----VSYKPQkispkfQNSV 430
Cdd:COG1137 24 LEVNQGE------IVgLLGPNGAGKTTTFYMIVGLVKPD--SGRifldGEDIthlPMHKrarlgIGYLPQ------EASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 431 -RHL---------LHQKIRDSYMHPQFMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCL-GKPADIyLIDEPSAYLD 499
Cdd:COG1137 90 fRKLtvednilavLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALaTNPKFI-LLDEPFAGVD 168
|
170 180
....*....|....*....|....
gi 22328793 500 ----SEqrivaskvIKRFILHAKK 519
Cdd:COG1137 169 piavAD--------IQKIIRHLKE 184
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
102-290 |
9.88e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.23 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEILThFRGSELQNyftriLEDNLKAIIKPQYVDHIPRAVK 181
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIF--NGQRIDT-LSPGKLQA-----LRRDIQFIFQDPYASLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 182 G-------NVGEVLDQKDERDKKAELCADLELN-QVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRl 253
Cdd:PRK10261 421 GdsimeplRVHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR- 499
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22328793 254 kaAQVVRSLLRPNSYV----IVVEHDLSVLDYLSDFICCLY 290
Cdd:PRK10261 500 --GQIINLLLDLQRDFgiayLFISHDMAVVERISHRVAVMY 538
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
63-286 |
1.00e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 45.31 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 63 KKCPFEAIQIINLPR----DLE-KDTTHRYGAN------TFKLhrlpvPrPGQVLGLVGTNGIGKSTALKILAGKLKPNL 131
Cdd:TIGR03719 303 KRNETAEIYIPPGPRlgdkVIEaENLTKAFGDKlliddlSFKL-----P-PGGIVGVIGPNGAGKSTLFRMITGQEQPDS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 132 GRFTsppdwqeilthfrgselqnyftrilednLKAIIKPQYVDHIPRAVKGN--VGEvldqkderdkkaELCADLELNQV 209
Cdd:TIGR03719 377 GTIE----------------------------IGETVKLAYVDQSRDALDPNktVWE------------EISGGLDIIKL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 210 IDRD--------------------VENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVkQRLKAAQvvRSLLRPNSYV 269
Cdd:TIGR03719 417 GKREipsrayvgrfnfkgsdqqkkVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV-ETLRALE--EALLNFAGCA 493
|
250
....*....|....*..
gi 22328793 270 IVVEHDLSVLDYLSDFI 286
Cdd:TIGR03719 494 VVISHDRWFLDRIATHI 510
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
378-543 |
1.03e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 378 VMLGENGTGKTTFIRMLAGllKPDDTEGpdREIPEFNVSYKPQKisPKFQNSVrhllhqkIRDSYM-----HPQFMSDVM 452
Cdd:PTZ00243 690 VVLGATGSGKSTLLQSLLS--QFEISEG--RVWAERSIAYVPQQ--AWIMNAT-------VRGNILffdeeDAARLADAV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 453 KPLQIE----QL---MDQEV----VNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSE--QRIVASKVIKRFilhAKK 519
Cdd:PTZ00243 757 RVSQLEadlaQLgggLETEIgekgVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvgERVVEECFLGAL---AGK 833
|
170 180 190
....*....|....*....|....*....|..
gi 22328793 520 TAFVVEH--------DFIMAtyLADRVIVYEG 543
Cdd:PTZ00243 834 TRVLATHqvhvvpraDYVVA--LGDGRVEFSG 863
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
103-276 |
1.08e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 44.31 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLG-------RFTSPPDWQeiLTHFRGSELQN----YFTRILEDNLKAIIKPQ 171
Cdd:PRK13642 33 GEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidgeLLTAENVWN--LRRKIGMVFQNpdnqFVGATVEDDVAFGMENQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 172 yvdHIPRAvkgnvgEVLDQKDErdkkaelcADLELNQV--IDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDV 249
Cdd:PRK13642 111 ---GIPRE------EMIKRVDE--------ALLAVNMLdfKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180
....*....|....*....|....*...
gi 22328793 250 KQRLKAAQVVRSLL-RPNSYVIVVEHDL 276
Cdd:PRK13642 174 TGRQEIMRVIHEIKeKYQLTVLSITHDL 201
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
25-70 |
1.10e-04 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 40.23 E-value: 1.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 22328793 25 CKKSCPVvktgKLCIEVTVGSKLAF-ISEELCIGCGICVKKCPFEAI 70
Cdd:pfam13187 8 CVAACPA----GAIVPDLVGQTIRGdIAGLACIGCGACVDACPRGAI 50
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
99-286 |
1.11e-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: 43.86 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 99 VPRpGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdWQEILTHFRGSELQNYFTRIlednlkaiiKPQYVDHIPR 178
Cdd:cd03290 24 IPT-GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH----WSNKNESEPSFEATRSRNRY---------SVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 179 AVKGNVGEVLDQKDERDKK-----AELCA---DLEL------NQVIDRDVeNLSGGELQRFAIAVVAIQNAEIYMFDEPS 244
Cdd:cd03290 90 LLNATVEENITFGSPFNKQrykavTDACSlqpDIDLlpfgdqTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22328793 245 SYLDV--KQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYlSDFI 286
Cdd:cd03290 169 SALDIhlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPH-ADWI 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
359-501 |
1.12e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.71 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 359 QG-NFRLRVSEGEFtdsqiivMLGENGTGKTTFIRMLAGLLKP----------DDTEGPDREIPefnvsYKPQKISPKFQ 427
Cdd:PRK10908 19 QGvTFHMRPGEMAF-------LTGHSGAGKSTLLKLICGIERPsagkiwfsghDITRLKNREVP-----FLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 428 NsvRHLLHQK-IRDSYMHPQFMSD---------VMKPLQIEQLMDQEV---VNLSGGELQRVALT-LCLGKPAdIYLIDE 493
Cdd:PRK10908 87 D--HHLLMDRtVYDNVAIPLIIAGasgddirrrVSAALDKVGLLDKAKnfpIQLSGGEQQRVGIArAVVNKPA-VLLADE 163
|
....*...
gi 22328793 494 PSAYLDSE 501
Cdd:PRK10908 164 PTGNLDDA 171
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
102-247 |
1.15e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.99 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKPNLGR---------FTSPPDWQEI---LTH---------------FRGSELQN 154
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSilylgkevtFNGPKSSQEAgigIIHqelnlipqltiaeniFLGREFVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 155 YFTRILEDNLKAiikpqyvdhipravkgnvgevldqkdERDKkaeLCADLELNQVIDRDVENLSGGELQRFAIA-VVAIQ 233
Cdd:PRK10762 109 RFGRIDWKKMYA--------------------------EADK---LLARLNLRFSSDKLVGELSIGEQQMVEIAkVLSFE 159
|
170
....*....|....
gi 22328793 234 NAEIYMfDEPSSYL 247
Cdd:PRK10762 160 SKVIIM-DEPTDAL 172
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
81-248 |
1.16e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGANT-FKLHRLPVpRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT-------------SPPDWQEILTH 146
Cdd:PRK15064 323 ENLTKGFDNGPlFKNLNLLL-EAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsenanigyyaqdHAYDFENDLTL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 147 FrgsELQNYFTRILEDNLkaiikpqyvdhiprAVKGNVGEVLDQKDERDKKaelcadlelnqvidrdVENLSGGELQRFA 226
Cdd:PRK15064 402 F---DWMSQWRQEGDDEQ--------------AVRGTLGRLLFSQDDIKKS----------------VKVLSGGEKGRML 448
|
170 180
....*....|....*....|..
gi 22328793 227 IAVVAIQNAEIYMFDEPSSYLD 248
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
209-281 |
1.19e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 1.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22328793 209 VIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLL-RPNSYVIVVEHDLSVLDY 281
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIRY 645
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
102-284 |
1.24e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKS-TALKILagKLKPnlgrftSPP---DWQEILthFRGSELQNYFTRILE----DNLKAIIKPQYV 173
Cdd:PRK15134 34 AGETLALVGESGSGKSvTALSIL--RLLP------SPPvvyPSGDIR--FHGESLLHASEQTLRgvrgNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 174 DHIP-RAVKGNVGEVLDQKDERDKKAelcADLELNQVIDR-----------DV-ENLSGGELQRFAIAVVAIQNAEIYMF 240
Cdd:PRK15134 104 SLNPlHTLEKQLYEVLSLHRGMRREA---ARGEILNCLDRvgirqaakrltDYpHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22328793 241 DEPSSYLDVKQRLKAAQVVRSLLRP-NSYVIVVEHDLSVLDYLSD 284
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLAD 225
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
217-284 |
1.28e-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: 1.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328793 217 LSGGELQRFAIAVVAIQNAE---IYMFDEPSSYL---DVKQRLkaaQVVRSLLRPNSYVIVVEHDLSVL---DYLSD 284
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfdDIKKLL---EVLQRLVDKGNTVVVIEHNLDVIktaDYIID 903
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
373-544 |
1.40e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 43.88 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 373 DSQIIVMLGENGTGKTTFIRMLAGLLKPDDTEGP--------DREIPEFNVSYKPQKISPKFQNSvRHLLHQKIRDSYMH 444
Cdd:PRK14246 35 NNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvdgkvlyfGKDIFQIDAIKLRKEVGMVFQQP-NPFPHLSIYDNIAY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 445 PQFMSDVMKPLQIEQLMDQ---------EVVN--------LSGGELQRVALTLCLGKPADIYLIDEPSAYLDseqrIVAS 507
Cdd:PRK14246 114 PLKSHGIKEKREIKKIVEEclrkvglwkEVYDrlnspasqLSGGQQQRLTIARALALKPKVLLMDEPTSMID----IVNS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 22328793 508 KVIKRFILHAKK--TAFVVEHDFIMATYLADRV-IVYEGQ 544
Cdd:PRK14246 190 QAIEKLITELKNeiAIVIVSHNPQQVARVADYVaFLYNGE 229
|
|
| FDH_beta_like |
cd16366 |
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ... |
25-72 |
1.51e-04 |
|
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.
Pssm-ID: 319888 [Multi-domain] Cd Length: 156 Bit Score: 42.39 E-value: 1.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 22328793 25 CKKSCP---VVKTGKLCIEVTvgsklafisEELCIGCGICVKKCPFEAIQI 72
Cdd:cd16366 78 CLAACPtgaIIRTETGTVVVD---------PETCIGCGYCVNACPFDIPRF 119
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
18-66 |
1.54e-04 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 39.93 E-value: 1.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 22328793 18 PKKCRQ--ECKKSCPVVKTGKLCIEVTVGSKLAFISEELCIGCGICVKKCP 66
Cdd:pfam13237 6 PDKCIGcgRCTAACPAGLTRVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
81-281 |
1.72e-04 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 43.17 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 81 KDTTHRYGAN--------TFKLhrlpvpRPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEIlTHFRGSEL 152
Cdd:cd03369 10 ENLSVRYAPDlppvlknvSFKV------KAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI--DGIDI-STIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 153 QNYFTRILEDnlkaiikpqyvdhiPRAVKGNVGEVLDQKDERDKKaELCADLElnqvIDRDVENLSGGELQRFAIAVVAI 232
Cdd:cd03369 81 RSSLTIIPQD--------------PTLFSGTIRSNLDPFDEYSDE-EIYGALR----VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22328793 233 QNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRpNSYVIVVEHDL-SVLDY 281
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLrTIIDY 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
94-340 |
1.95e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 44.55 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 94 LHRLPVPRP-GQVLGLVGTNGIGKSTALKILAGKLKPNLGRftsppdwqeilTHFRGSelqnyftrilednlkaiikpqy 172
Cdd:TIGR00957 654 LNGITFSIPeGALVAVVGQVGCGKSSLLSALLAEMDKVEGH-----------VHMKGS---------------------- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 173 VDHIPR-------AVKGNV--GEVLDQKDERD--KKAELCADLEL------NQVIDRDVeNLSGGELQRFAIAVVAIQNA 235
Cdd:TIGR00957 701 VAYVPQqawiqndSLRENIlfGKALNEKYYQQvlEACALLPDLEIlpsgdrTEIGEKGV-NLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 236 EIYMFDEPSSYLDVKQrlkAAQVVRSLLRP-----NSYVIVVEHDLSVLDYLsDFICCLYG----KPGAYGVVTlpfsVR 306
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHV---GKHIFEHVIGPegvlkNKTRILVTHGISYLPQV-DVIIVMSGgkisEMGSYQELL----QR 851
|
250 260 270
....*....|....*....|....*....|....*
gi 22328793 307 EG-INIFLAGFVPTENLRFRDESLTFKVAETPQES 340
Cdd:TIGR00957 852 DGaFAEFLRTYAPDEQQGHLEDSWTALVSGEGKEA 886
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
102-129 |
2.03e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.92 E-value: 2.03e-04
10 20
....*....|....*....|....*...
gi 22328793 102 PGQVLGLVGTNGIGKSTALKILAGKLKP 129
Cdd:COG4586 47 PGEIVGFIGPNGAGKSTTIKMLTGILVP 74
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
46-70 |
2.03e-04 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 42.62 E-value: 2.03e-04
10 20
....*....|....*....|....*
gi 22328793 46 KLAFISEELCIGCGICVKKCPFEAI 70
Cdd:PRK05113 107 KVAFIDEDNCIGCTKCIQACPVDAI 131
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
467-544 |
2.47e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 43.29 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 467 NLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSeqriVASKVIKRFILHAKK--TAFVVEHDFIMATYLADRV-IVYEG 543
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDP----VGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYVaFLYLG 224
|
.
gi 22328793 544 Q 544
Cdd:PRK14267 225 K 225
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
211-275 |
2.54e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 211 DRDVENLSGGELQ------RFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHD 275
Cdd:PRK03918 783 ERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHD 853
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
103-291 |
2.57e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 43.14 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEI------LTHFR---GSELQNYftrilEDNLKAIIKPQYV 173
Cdd:PRK13639 28 GEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI--KGEPIkydkksLLEVRktvGIVFQNP-----DDQLFAPTVEEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 174 DHIPRavkgNVGEVLDQKDERDKKAelcadleLNQVIDRDVEN-----LSGGELQRFAIAVVAIQNAEIYMFDEPSSYLD 248
Cdd:PRK13639 101 AFGPL----NLGLSKEEVEKRVKEA-------LKAVGMEGFENkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22328793 249 VKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDYLSDFICCLYG 291
Cdd:PRK13639 170 PMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSD 212
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
212-286 |
2.83e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 212 RDVENLSGGELQRFAIA---VVAIQNAEIYMFDEPSSYL---DVKQRLkaaQVVRSLLRPNSYVIVVEHDLSVLDyLSDF 285
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLhthDIKALI---YVLQSLTHQGHTVVIIEHNMHVVK-VADY 880
|
.
gi 22328793 286 I 286
Cdd:PRK00635 881 V 881
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
7-86 |
2.91e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 43.97 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 7 RIAIVSSDRCK-PKKCRQ----ECKKSCPvvkTGKLcieVTVGSKLAFISEElCIGCGICVKKCPFEAIQIINLP--RDL 79
Cdd:PRK12769 41 RITVIKHQQQRsAVTCHHcedaPCARSCP---NGAI---SHVDDSIQVNQQK-CIGCKSCVVACPFGTMQIVLTPvaAGK 113
|
....*..
gi 22328793 80 EKDTTHR 86
Cdd:PRK12769 114 VKATAHK 120
|
|
| FDH_b_like |
cd10562 |
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ... |
25-72 |
2.99e-04 |
|
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.
Pssm-ID: 319884 [Multi-domain] Cd Length: 161 Bit Score: 41.52 E-value: 2.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 22328793 25 CKKSCPvvkTGKLcievtvgSKLAF----ISEELCIGCGICVKKCPFEAIQI 72
Cdd:cd10562 78 CVKVCP---TGAL-------YKTENgavvVDEDKCIGCGYCVAACPFDVPRY 119
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
46-70 |
3.36e-04 |
|
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]
Pssm-ID: 273887 [Multi-domain] Cd Length: 165 Bit Score: 41.71 E-value: 3.36e-04
10 20
....*....|....*....|....*
gi 22328793 46 KLAFISEELCIGCGICVKKCPFEAI 70
Cdd:TIGR01944 106 MVALIDEDNCIGCTKCIQACPVDAI 130
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
103-291 |
3.41e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKS-TALKILA-----GKLKPNLGRFTSPpDWQEILTHFR----GSELqnyfTRILEDNLKAIiKPQY 172
Cdd:PRK11022 33 GEVVGIVGESGSGKSvSSLAIMGlidypGRVMAEKLEFNGQ-DLQRISEKERrnlvGAEV----AMIFQDPMTSL-NPCY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 173 VD--HIPRAVKGNVGEvlDQKDERDKKAELcadleLNQV--------IDRDVENLSGGELQRFAIAVVAIQNAEIYMFDE 242
Cdd:PRK11022 107 TVgfQIMEAIKVHQGG--NKKTRRQRAIDL-----LNQVgipdpasrLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22328793 243 PSSYLDVKQRlkaAQVVRSLL----RPNSYVIVVEHDLSVLDYLSDFICCLYG 291
Cdd:PRK11022 180 PTTALDVTIQ---AQIIELLLelqqKENMALVLITHDLALVAEAAHKIIVMYA 229
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
48-73 |
3.55e-04 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 434137 [Multi-domain] Cd Length: 59 Bit Score: 38.80 E-value: 3.55e-04
10 20
....*....|....*....|....*.
gi 22328793 48 AFISEELCIGCGICVKKCPFEAIQII 73
Cdd:pfam14697 1 ARIDEDTCIGCGKCYIACPDTSHQAI 26
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
4-74 |
4.22e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 43.44 E-value: 4.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 4 RLTRIAIVSSDRCKpkKCRqECKKSCPVVktgklCIEVTVGSKLAFISEELCIGCGICVKKCPfeAIQIIN 74
Cdd:PRK13795 571 KDAARLLRRAAECV--GCG-VCVGACPTG-----AIRIEEGKRKISVDEEKCIHCGKCTEVCP--VVKYKD 631
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
43-70 |
4.27e-04 |
|
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.
Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 42.37 E-value: 4.27e-04
10 20
....*....|....*....|....*...
gi 22328793 43 VGSKLAFISEELCIGCGICVKKCPFEAI 70
Cdd:cd03110 54 VGGKKAFIDQEKCIRCGNCERVCKFGAI 81
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
101-277 |
4.51e-04 |
|
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: 42.14 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAgklkpnlgRFTSPPDwQEILthFRGSELQNYFTRILEDNLKaiikpqYVDHIPRAV 180
Cdd:cd03249 27 PPGKTVALVGSSGCGKSTVVSLLE--------RFYDPTS-GEIL--LDGVDIRDLNLRWLRSQIG------LVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 181 KGNVGEVL-----DQKDERDKKAelCADLELNQVI------------DRDVEnLSGGELQRFAIAVVAIQNAEIYMFDEP 243
Cdd:cd03249 90 DGTIAENIrygkpDATDEEVEEA--AKKANIHDFImslpdgydtlvgERGSQ-LSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 22328793 244 SSYLD------VKQRLKAAQVVRSllrpnsyVIVVEHDLS 277
Cdd:cd03249 167 TSALDaeseklVQEALDRAMKGRT-------TIVIAHRLS 199
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
217-284 |
5.04e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.22 E-value: 5.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328793 217 LSGGELQRFAIAVvAIQNAE----IYMFDEPSSYL---DVKQRLkaaQVVRSLLRPNSYVIVVEHDLSVL---DYLSD 284
Cdd:cd03271 170 LSGGEAQRIKLAK-ELSKRStgktLYILDEPTTGLhfhDVKKLL---EVLQRLVDKGNTVVVIEHNLDVIkcaDWIID 243
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
101-284 |
5.58e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.99 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 101 RPGQVLGLVGTNGIGKSTALKILAGKLKPNL----GRFTSppDWQEILthfrGSELQNYFTRILEDNLKAIIKPQyvdhi 176
Cdd:PRK10418 27 QRGRVLALVGGSGSGKSLTCAAALGILPAGVrqtaGRVLL--DGKPVA----PCALRGRKIATIMQNPRSAFNPL----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 177 pRAVKGNVGEVLDQKDERDKKAELCADLE------LNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVK 250
Cdd:PRK10418 96 -HTMHTHARETCLALGKPADDATLTAALEavglenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180 190
....*....|....*....|....*....|....*
gi 22328793 251 QRLKAAQVVRSLLRPNSY-VIVVEHDLSVLDYLSD 284
Cdd:PRK10418 175 AQARILDLLESIVQKRALgMLLVTHDMGVVARLAD 209
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
102-284 |
5.67e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 42.07 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 102 PGQVLGLVGTNGIGKSTALKIL--AGKLKPNLGRFTSppdwqeilTHFRGSELQNYFTRILEDNLKAIIKPQYVDHIPRA 179
Cdd:PRK14239 30 PNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGS--------IVYNGHNIYSPRTDTVDLRKEIGMVFQQPNPFPMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 180 VKGNV-----------GEVLDQKDERDKKAELCADlelnQVIDRDVEN---LSGGELQRFAIAVVAIQNAEIYMFDEPSS 245
Cdd:PRK14239 102 IYENVvyglrlkgikdKQVLDEAVEKSLKGASIWD----EVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22328793 246 YLDvkqRLKAAQVVRSL--LRPNSYVIVVEHDLSVLDYLSD 284
Cdd:PRK14239 178 ALD---PISAGKIEETLlgLKDDYTMLLVTRSMQQASRISD 215
|
|
| PhsB_like |
cd10553 |
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ... |
24-71 |
6.02e-04 |
|
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319875 [Multi-domain] Cd Length: 146 Bit Score: 40.42 E-value: 6.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 22328793 24 ECKKSCPvvkTGKLCIEVTVGskLAFISEELCIGCGICVKKCPFEAIQ 71
Cdd:cd10553 65 WCVKACP---TGAMQKREKDG--IVYVDQELCIGCKACIEACPWGIPQ 107
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
50-75 |
6.07e-04 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 40.30 E-value: 6.07e-04
10 20
....*....|....*....|....*.
gi 22328793 50 ISEELCIGCGICVKKCPFEAIQIINL 75
Cdd:cd10564 114 LDADACTGCGACVSVCPVGAITLTPL 139
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
467-540 |
6.36e-04 |
|
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: 42.81 E-value: 6.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 467 NLSGGELQRVALTLCL-GKPAdIYLIDEPSAYLDSEqrivASKVIKRFILHAKK---TAFVVEHDF-IMAtyLADRVIV 540
Cdd:COG4618 467 RLSGGQRQRIGLARALyGDPR-LVVLDEPNSNLDDE----GEAALAAAIRALKArgaTVVVITHRPsLLA--AVDKLLV 538
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
462-539 |
6.36e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 462 DQEVVNLSGGELQRVALTLCLGkpADI----YLIDEPSAYL---DSEQRIvasKVIKRfILHAKKTAFVVEHDFIMATyL 534
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLG--AELigitYILDEPSIGLhpqDTHKLI---NVIKK-LRDQGNTVLLVEHDEQMIS-L 543
|
....*
gi 22328793 535 ADRVI 539
Cdd:PRK00635 544 ADRII 548
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
217-285 |
6.53e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.08 E-value: 6.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 217 LSGGELQRFAIA-VVAIQnAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVeHDLSVLDYLSDF 285
Cdd:PRK14243 152 LSGGQQQRLCIArAIAVQ-PEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT-HNMQQAARVSDM 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
217-248 |
6.54e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 42.50 E-value: 6.54e-04
10 20 30
....*....|....*....|....*....|..
gi 22328793 217 LSGGELQRFAIAVVAIQNAEIYMFDEPSSYLD 248
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| IOR_alpha |
TIGR03336 |
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin ... |
10-70 |
6.71e-04 |
|
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin oxidoreductase (IOR) is an alpha 2/beta 2 tetramer related to ketoacid oxidoreductases for pyruvate (1.2.7.1, POR), 2-ketoglutarate (1.2.7.3, KOR), and 2-oxoisovalerate (1.2.7.7, VOR). These multi-subunit enzymes typically are found in anaerobes and are inactiviated by oxygen. IOR in Pyrococcus acts in fermentation of all three aromatic amino acids, following removal of the amino group by transamination. In Methanococcus maripaludis, by contrast, IOR acts in the opposite direction, in pathways of amino acid biosynthesis from phenylacetate, indoleacetate, and p-hydroxyphenylacetate. In M. maripaludis and many other species, iorA and iorB are found next to an apparent phenylacetate-CoA ligase.
Pssm-ID: 274526 [Multi-domain] Cd Length: 595 Bit Score: 42.79 E-value: 6.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 10 IVSSDRCKpkKCRQeCKKS--CPVVKTGKLCIEVTvgsklafiseELCIGCGICVKKCPFEAI 70
Cdd:TIGR03336 546 KVDQDKCI--GCKK-CIKElgCPAIEPEDKEAVID----------PLCTGCGVCAQICPFDAI 595
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
103-281 |
7.14e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.00 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGrftsppdwqEILTHFRGSELQNYFTRILEDNLKAIIKPQYVDHIPRA--V 180
Cdd:PRK13651 33 GEFIAIIGQTGSGKTTFIEHLNALLLPDTG---------TIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIKKIkeI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 181 KGNVGEVLD-----------QKD----------------ERDKKAELCADLELNqVIDRDVENLSGGELQRFAIAVVAIQ 233
Cdd:PRK13651 104 RRRVGVVFQfaeyqlfeqtiEKDiifgpvsmgvskeeakKRAAKYIELVGLDES-YLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22328793 234 NAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDL-SVLDY 281
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEW 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
103-244 |
7.44e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 41.40 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTsppdwqeilthFRGSELQNYFT-RILEDNLkAIIkPQYVDHIPR-AV 180
Cdd:PRK11614 31 GEIVTLIGANGAGKTTLLGTLCGDPRATSGRIV-----------FDGKDITDWQTaKIMREAV-AIV-PEGRRVFSRmTV 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 181 KGNV--GEVLDQKDERDKKAELCADLeLNQVIDRDVE---NLSGGELQRFAIAVVAIQNAEIYMFDEPS 244
Cdd:PRK11614 98 EENLamGGFFAERDQFQERIKWVYEL-FPRLHERRIQragTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| Fer4_6 |
pfam12837 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
50-70 |
7.54e-04 |
|
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 432822 [Multi-domain] Cd Length: 24 Bit Score: 37.21 E-value: 7.54e-04
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
8-74 |
7.55e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 42.54 E-value: 7.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 8 IAIVSSDRCKpkKCRQeCKKSCP-----VVKTGKlcievtvgsklAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:COG1148 490 VAEVDPEKCT--GCGR-CVEVCPygaisIDEKGV-----------AEVNPALCKGCGTCAAACPSGAISLKG 547
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
205-282 |
7.75e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.80 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 205 ELNQVIDRDVeNLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQrlkAAQV----VRSLLRPNSYVIVVE--HDLSV 278
Cdd:PLN03130 730 DLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV---GRQVfdkcIKDELRGKTRVLVTNqlHFLSQ 805
|
....
gi 22328793 279 LDYL 282
Cdd:PLN03130 806 VDRI 809
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
199-264 |
8.26e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.66 E-value: 8.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22328793 199 ELCADLELNQVIDRDVeNLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQrlkAAQVVRSLLR 264
Cdd:PLN03232 724 DLLPGRDLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV---AHQVFDSCMK 785
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
467-541 |
8.80e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 8.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 467 NLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSEQRIVASKVIKRFILHAKKTAFVVEHDfIMATYLADRVIVY 541
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR-IASIKRSDKIVVF 1431
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
103-274 |
1.04e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 41.27 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 103 GQVLGLVGTNGIGKSTALKILAGKLKPNLGRFTSppDWQEILTH----------------FRGSELQNYFTRILEDnlkA 166
Cdd:PRK13649 33 GSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV--DDTLITSTsknkdikqirkkvglvFQFPESQLFEETVLKD---V 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 167 IIKPQyvdhipravkgNVGeVLDQKDE---RDKKAELCADLELnqvIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEP 243
Cdd:PRK13649 108 AFGPQ-----------NFG-VSQEEAEalaREKLALVGISESL---FEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190
....*....|....*....|....*....|.
gi 22328793 244 SSYLDVKQRLKAAQVVRSLLRPNSYVIVVEH 274
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
211-275 |
1.08e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 211 DRDVENLSGGELQRFAIAvvAIQNAEI----YMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHD 275
Cdd:PRK00635 471 ERALATLSGGEQERTALA--KHLGAELigitYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
217-284 |
1.16e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 41.23 E-value: 1.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328793 217 LSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSyVIVVEHDLSVLDYLSD 284
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLT-VIIVTHNLAQAARISD 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
361-401 |
1.32e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.54 E-value: 1.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 22328793 361 NFRLRvsEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPD 401
Cdd:COG1129 24 SLELR--PGE-----VHALLGENGAGKSTLMKILSGVYQPD 57
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
361-503 |
1.42e-03 |
|
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: 40.28 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFR--LRVSEGEFtDSQIIVMLGENGTGKTTFIR----MLAGLLKPDDTEGP-DREIpeFNVSYKPQKISPKFQNSVRHL 433
Cdd:cd03240 8 NIRsfHERSEIEF-FSPLTLIVGQNGAGKTTIIEalkyALTGELPPNSKGGAhDPKL--IREGEVRAQVKLAFENANGKK 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328793 434 LhqKIRDSYmhPQFMSDVMKPL-QIEQLMDQEVVNLSGGE------LQRVALTLCLGKPADIYLIDEPSAYLDSEQR 503
Cdd:cd03240 85 Y--TITRSL--AILENVIFCHQgESNWPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENI 157
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
335-501 |
1.46e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.63 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 335 ETPQESAEEIQSYARYKYPTMTKTQGNFRLRVSEGEFTDSQIIVMLGENGTGKTTFIRMLAGLLKPDDTEGPDREI--PE 412
Cdd:TIGR00956 750 DMEKESGEDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVngRP 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 413 FNVSYkpQKISPKFQNSVRHLLHQKIRDS-----YM-HPQFMSD---------VMKPLQIEQLMDQeVVNLSGGEL---Q 474
Cdd:TIGR00956 830 LDSSF--QRSIGYVQQQDLHLPTSTVRESlrfsaYLrQPKSVSKsekmeyveeVIKLLEMESYADA-VVGVPGEGLnveQ 906
|
170 180 190
....*....|....*....|....*....|
gi 22328793 475 RVALTLCL---GKPADIYLIDEPSAYLDSE 501
Cdd:TIGR00956 907 RKRLTIGVelvAKPKLLLFLDEPTSGLDSQ 936
|
|
| Fer4_16 |
pfam13484 |
4Fe-4S double cluster binding domain; |
20-67 |
1.64e-03 |
|
4Fe-4S double cluster binding domain;
Pssm-ID: 463893 [Multi-domain] Cd Length: 65 Bit Score: 37.08 E-value: 1.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 20 KCRQeCKKSCPV--------VKTGKLCIEVTVGSKLAFISEEL-------CIGCGICVKKCPF 67
Cdd:pfam13484 3 SCGK-CIDACPTgaivgpegVLDARRCISYLTIEKKGLIPDELrcllgnrCYGCDICQDVCPW 64
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
217-284 |
1.64e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 217 LSGGELQRFAIAvvaiqnAE---------IYMFDEPSSYL---DVKQRLKaaqVVRSLL-RPNSyVIVVEHDLSVL---D 280
Cdd:COG0178 827 LSGGEAQRVKLA------SElskrstgktLYILDEPTTGLhfhDIRKLLE---VLHRLVdKGNT-VVVIEHNLDVIktaD 896
|
....
gi 22328793 281 YLSD 284
Cdd:COG0178 897 WIID 900
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
212-274 |
1.76e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 1.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22328793 212 RDVENLSGGELQRFAIAVV-AIQN---AEIYMFDEPSSYLDVKQRLKAAQVVRSlLRPNSYVIVVEH 274
Cdd:pfam02463 1073 KNLDLLSGGEKTLVALALIfAIQKykpAPFYLLDEIDAALDDQNVSRVANLLKE-LSKNAQFIVISL 1138
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-541 |
1.97e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.46 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 365 RVSEGeFTDSQIIVMLGENGTGKTTFIRMLAGLlkPDDTEGPD---------------REIPEFN--VSYKPQKISPkFQ 427
Cdd:PRK14271 39 QVSMG-FPARAVTSLMGPTGSGKTTFLRTLNRM--NDKVSGYRysgdvllggrsifnyRDVLEFRrrVGMLFQRPNP-FP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 428 NSVRHLLHQKIRDSYMHPQ---------FMSDVMKPLQIEQLMDQEVVNLSGGELQRVALTLCLGKPADIYLIDEPSAYL 498
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVPRkefrgvaqaRLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 22328793 499 DSeqriVASKVIKRFI--LHAKKTAFVVEHDFIMATYLADRVIVY 541
Cdd:PRK14271 195 DP----TTTEKIEEFIrsLADRLTVIIVTHNLAQAARISDRAALF 235
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
463-539 |
2.10e-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: 40.29 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 463 QEVVNLSGGELQRVALTLCLGKPAD---IYLIDEPSAYL--DSEQRIVAskVIKRfILHAKKTAFVVEHDF-IMATylAD 536
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfHDVKKLLE--VLQR-LVDKGNTVVVIEHNLdVIKC--AD 239
|
...
gi 22328793 537 RVI 539
Cdd:cd03271 240 WII 242
|
|
| DMSOR_beta_like |
cd16367 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
18-73 |
2.20e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319889 [Multi-domain] Cd Length: 138 Bit Score: 38.83 E-value: 2.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 18 PKKCRQ----ECKKSCPVvktgklcievtvGSKLAFISEEL-----CIGCGICVKKCPFEAIQII 73
Cdd:cd16367 54 PTACRHcvdpVCMIGCPT------------GAIHRDDGGEVvisdaCCGCGNCASACPYGAIQMV 106
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
353-543 |
2.28e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 353 PTMTktqgNFRLRVSEGEFtdsqiIVMLGENGTGKTTFIRMLAGLLKP-DDTEGPDREipefNVSYKPQkISPKFQNSVR 431
Cdd:PLN03130 631 PTLS----NINLDVPVGSL-----VAIVGSTGEGKTSLISAMLGELPPrSDASVVIRG----TVAYVPQ-VSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 432 -HLLHQKIRDS--YMHPQFMSDVMKPLQIEQLMDQ-EV----VNLSGGELQRVALTLCLGKPADIYLIDEPSAYLDSE-Q 502
Cdd:PLN03130 697 dNILFGSPFDPerYERAIDVTALQHDLDLLPGGDLtEIgergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvG 776
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 22328793 503 RIVASKVIKRFIlhAKKTAFVVEHDFIMATYLaDRVI-VYEG 543
Cdd:PLN03130 777 RQVFDKCIKDEL--RGKTRVLVTNQLHFLSQV-DRIIlVHEG 815
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
21-72 |
2.45e-03 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 39.16 E-value: 2.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 21 CRQ----ECKKSCPV-----VKTGklcievTVgsklaFISEELCIGCGICVKKCPFEAIQI 72
Cdd:COG0437 60 CNHcddpPCVKVCPTgatykREDG------IV-----LVDYDKCIGCRYCVAACPYGAPRF 109
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
214-281 |
2.52e-03 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 40.00 E-value: 2.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328793 214 VENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEhdLSVLDY 281
Cdd:PRK09984 150 VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVT--LHQVDY 215
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
17-83 |
2.74e-03 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 39.92 E-value: 2.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328793 17 KPKKCRQECKKSCPVVKT-----G-KLCIEVTV---GSKLAFISeelCIGCGICVKKCPFEAIQIIN-LPR-DLEKDT 83
Cdd:PRK07118 97 EPKVAVVRCQGTCDKAKEryeyqGiKDCAAAALlfgGPKGCSYG---CLGLGSCVAACPFDAIHIENgLPVvDEDKCT 171
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
468-526 |
2.83e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 40.58 E-value: 2.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22328793 468 LSGGELQRVALTLCLGKPADIYLIDEPSAYLDS--EQRIVAskVIKRFILHakKTAFVVEH 526
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAetERQILE--LLAEHAQN--KTVLMITH 532
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
2-74 |
2.88e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 40.78 E-value: 2.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328793 2 ADRLTRIAIV-SSDRCKPKKCRQ----ECKKSCPVVKtgklcieVTVGSKLAFISEELCIGCGICVKKCPFEAIQIIN 74
Cdd:PRK12809 36 SDFRPRIHVVgKGQAANPVACHHcnnaPCVTACPVNA-------LTFQSDSVQLDEQKCIGCKRCAIACPFGVVEMVD 106
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
55-73 |
3.01e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 38.09 E-value: 3.01e-03
|
| FDH-N |
cd10558 |
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ... |
25-87 |
3.11e-03 |
|
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups.
Pssm-ID: 319880 [Multi-domain] Cd Length: 208 Bit Score: 39.29 E-value: 3.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22328793 25 CKKSCPvvkTGKLCIEVTVGSkLAFISEeLCIGCGICVKKCPFeaiqiiNLPRdLEKDTTHRY 87
Cdd:cd10558 78 CLKACP---SPGAIVQYANGI-VDFQSD-KCIGCGYCIKGCPF------DIPR-ISKDDNKMY 128
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
25-71 |
3.11e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319892 [Multi-domain] Cd Length: 131 Bit Score: 38.02 E-value: 3.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 22328793 25 CKKSCPvvkTGKLciEVTVGSKLAFIsEELCIGCGICVKKCPFEAIQ 71
Cdd:cd16370 61 CAEACP---TGAL--EPRKGGGVVLD-KEKCIGCGNCVKACIVGAIF 101
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
373-418 |
3.46e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.60 E-value: 3.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 22328793 373 DSQIIVMLGENGTGKTTFIRMLAGLLKPDDTEGPDREIPEFNVSYK 418
Cdd:COG3950 24 PPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNG 69
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
108-313 |
3.50e-03 |
|
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: 39.99 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 108 LVGTNGIGKSTALKILAGKLKPNLGR------FTSPPDWQEILTHFRGsELQNYFTRILEDNLKAIIKPQYVDHIpRAVK 181
Cdd:COG3593 28 LVGENNSGKSSILEALRLLLGPSSSRkfdeedFYLGDDPDLPEIEIEL-TFGSLLSRLLRLLLKEEDKEELEEAL-EELN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 182 GNVGEVLD----------QKDERDKKAELC------------ADLELNQVIDRDVENLSGGELQRFAIAVV-AIQNAE-- 236
Cdd:COG3593 106 EELKEALKalnellseylKELLDGLDLELElsldeledllksLSLRIEDGKELPLDRLGSGFQRLILLALLsALAELKra 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 237 ----IYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSYVIVVEHDLSVLDyLSDF--ICCLYGKPGAYGVVTLPFSVREGIN 310
Cdd:COG3593 186 panpILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLS-EVPLenIRRLRRDSGGTTSTKLIDLDDEDLR 264
|
...
gi 22328793 311 IFL 313
Cdd:COG3593 265 KLL 267
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
87-290 |
3.69e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 39.44 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 87 YGAN-TFKLHRLPVPRPGqVLGLVGTNGIGKSTALKILAGKLKPN-----------LGRFTSPPDWQEILTHFR-GSELQ 153
Cdd:PRK14267 14 YGSNhVIKGVDLKIPQNG-VFALMGPSGCGKSTLLRTFNRLLELNeearvegevrlFGRNIYSPDVDPIEVRREvGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 154 --NYFTRIlednlkaiikpQYVDHIPRAVKGNvgEVLDQKDERDKKAE--LCADLELNQVIDRDVE---NLSGGELQRFA 226
Cdd:PRK14267 93 ypNPFPHL-----------TIYDNVAIGVKLN--GLVKSKKELDERVEwaLKKAALWDEVKDRLNDypsNLSGGQRQRLV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328793 227 IAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLlrPNSYVIV-VEHDLSVLDYLSDFICCLY 290
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVlVTHSPAQAARVSDYVAFLY 222
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
7-73 |
3.91e-03 |
|
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]
Pssm-ID: 273887 [Multi-domain] Cd Length: 165 Bit Score: 38.63 E-value: 3.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22328793 7 RIAIVSSDRCKpkKCrQECKKSCPVvktgklciEVTVGSKLAF--ISEELCIGCGICVKKCPFEAIQII 73
Cdd:TIGR01944 106 MVALIDEDNCI--GC-TKCIQACPV--------DAIVGAAKAMhtVIADECTGCDLCVEPCPTDCIEMI 163
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
461-524 |
4.02e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 39.17 E-value: 4.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22328793 461 MDQEVVNLSGGELQRVALTL--CLGK--PADIYLIDEPSAYLDSEQRIVASKVIKRFilhAKKTAFVV 524
Cdd:cd03272 152 EQQEMQQLSGGQKSLVALALifAIQKcdPAPFYLFDEIDAALDAQYRTAVANMIKEL---SDGAQFIT 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
205-290 |
4.12e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.22 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 205 ELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLKAAQVVRSLLRPNSY-VIVVEHDLSVLDYLS 283
Cdd:PRK10261 157 EAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIA 236
|
....*..
gi 22328793 284 DFICCLY 290
Cdd:PRK10261 237 DRVLVMY 243
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
18-73 |
5.63e-03 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 39.15 E-value: 5.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328793 18 PKKCRQ------ECKKSCPVvktGKLCIEvtvgSKLAFISEELCIGCGICVKKCPFEAIQII 73
Cdd:PRK07118 134 PKGCSYgclglgSCVAACPF---DAIHIE----NGLPVVDEDKCTGCGACVKACPRNVIELI 188
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
105-290 |
5.93e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 38.87 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 105 VLGLVGTNGIGKSTALKILAGKLKPnlgrFTSPPDWQEILTHFRGSELQNYFTRILEDNLKAIIKPQYVDHIprAVKGNV 184
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVLNRLIEI----YDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHL--SIYDNI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 185 GEVLDQ---KDERDKKAELCADL-------ELNQVIDRDVENLSGGELQRFAIAVVAIQNAEIYMFDEPSSYLDVKQRLK 254
Cdd:PRK14246 112 AYPLKShgiKEKREIKKIVEECLrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQA 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 22328793 255 AAQVVRSlLRPNSYVIVVEHDLSVLDYLSDFICCLY 290
Cdd:PRK14246 192 IEKLITE-LKNEIAIVIVSHNPQQVARVADYVAFLY 226
|
|
| DMSOR_beta_like |
cd16374 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
18-72 |
7.51e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319896 [Multi-domain] Cd Length: 139 Bit Score: 37.25 E-value: 7.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 18 PKKCRQeCKKS-----CPvvkTGKLCIEVTvGSKLafISEELCIGCGICVKKCPFEAIQI 72
Cdd:cd16374 40 PVRCRH-CEDApcmevCP---TGAIYRDED-GAVL--VDPDKCIGCGMCAMACPFGVPRF 92
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
20-69 |
7.65e-03 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 34.81 E-value: 7.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 22328793 20 KCRQeCKKSCPVVKTGKLCIEVTVGSKLAFISEELCIGCGICVKKCPFEA 69
Cdd:pfam12838 3 GCGA-CVAACPVGAITLDEVGEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
361-405 |
7.91e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.34 E-value: 7.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 22328793 361 NFRLRvsEGEftdsqIIVMLGENGTGKTTFIRMLAGLLKPddTEG 405
Cdd:NF033858 286 SFRIR--RGE-----IFGFLGSNGCGKSTTMKMLTGLLPA--SEG 321
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
361-441 |
8.75e-03 |
|
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: 38.83 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328793 361 NFRlRVSEGEFT-DSQIIVMLGENGTGKTTFIRMLAGLLKPDDTEGPDREipEFNVSYKPQ----KISPKFQNSVRHLLH 435
Cdd:COG3593 10 NFR-SIKDLSIElSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEE--DFYLGDDPDlpeiEIELTFGSLLSRLLR 86
|
....*.
gi 22328793 436 QKIRDS 441
Cdd:COG3593 87 LLLKEE 92
|
|
| Fer4_2 |
pfam12797 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
49-67 |
8.95e-03 |
|
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 463711 [Multi-domain] Cd Length: 22 Bit Score: 33.91 E-value: 8.95e-03
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
96-135 |
9.63e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.95 E-value: 9.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 22328793 96 RLPvprPGQVLGLVGTNGIGKSTALKILAGKLKPNLGRFT 135
Cdd:PRK11819 346 SLP---PGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK 382
|
|
| |
