|
Name |
Accession |
Description |
Interval |
E-value |
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-608 |
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: 863.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 18 RIAIVEKDRCKPKNCGLACKRACPVNRQGKQCIVVEATSTISQISEILCIGCGICVKKCPYDAIKIINLPANLANETTHR 97
Cdd:COG1245 3 RIAVVDRDRCQPKKCNYECIKYCPVNRTGKEAIEIDEDDGKPVISEELCIGCGICVKKCPFDAISIVNLPEELEEDPVHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 98 YSQNSFKLHRLPTPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIINHFRGSELQNYFTRILEDTLKC 177
Cdd:COG1245 83 YGENGFRLYGLPVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKRFRGTELQDYFKKLANGEIKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 178 VIKPQYVDQIPRAAKGTVEKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSY 257
Cdd:COG1245 163 AHKPQYVDLIPKVFKGTVRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 258 LDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSDFICCLYGVPGVYGVVTLPSGVREGINMFLEGFIRTENMRFRE 337
Cdd:COG1245 243 LDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILYGEPGVYGVVSKPKSVRVGINQYLDGYLPEENVRIRD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 338 SKLSFKTSEQQEDIKRTGNIKYPSMSKTLGNFHLDVEAGDFSDSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPhV 417
Cdd:COG1245 323 EPIEFEVHAPRREKEEETLVEYPDLTKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-L 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 418 SISYKPQKISPKSETTVRFMLHDKIQNMYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDE 497
Cdd:COG1245 402 KISYKPQYISPDYDGTVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 498 PSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEGQPSVKCTACKPQSLLEGMNRFLKMLDITFR 577
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGVHGHASGPMDMREGMNRFLKELGITFR 561
|
570 580 590
....*....|....*....|....*....|.
gi 17555800 578 RDQETYRPRINKLDSVKDVDQKKSGQFFFLD 608
Cdd:COG1245 562 RDEETGRPRINKPGSYLDREQKERGEYYYYE 592
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-608 |
0e+00 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 857.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 18 RIAIVEKDRCKPKNCGLACKRACPVNRQGKQCIVVEATSTISQISEILCIGCGICVKKCPYDAIKIINLPANLANETTHR 97
Cdd:PRK13409 3 RIAVVDYDRCQPKKCNYECIKYCPVVRTGEETIEIDEDDGKPVISEELCIGCGICVKKCPFDAISIVNLPEELEEEPVHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 98 YSQNSFKLHRLPTPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIINHFRGSELQNYFTRILEDTLKC 177
Cdd:PRK13409 83 YGVNGFKLYGLPIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRFRGTELQNYFKKLYNGEIKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 178 VIKPQYVDQIPRAAKGTVEKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSY 257
Cdd:PRK13409 163 VHKPQYVDLIPKVFKGKVRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 258 LDVKQRLKAAAIIRERVSDtNYVVVVEHDLAVLDYLSDFICCLYGVPGVYGVVTLPSGVREGINMFLEGFIRTENMRFRE 337
Cdd:PRK13409 243 LDIRQRLNVARLIRELAEG-KYVLVVEHDLAVLDYLADNVHIAYGEPGAYGVVSKPKGVRVGINEYLKGYLPEENMRIRP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 338 SKLSFKTSEQQEDIKRTGNIKYPSMSKTLGNFHLDVEAGDFSDSEIIVMLGENGTGKTTMIKMMAGSLKPeDENTELPHV 417
Cdd:PRK13409 322 EPIEFEERPPRDESERETLVEYPDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKP-DEGEVDPEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 418 SISYKPQKISPKSETTVRFMLhDKIQNMYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDE 497
Cdd:PRK13409 401 KISYKPQYIKPDYDGTVEDLL-RSITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 498 PSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEGQPSVKCTACKPQSLLEGMNRFLKMLDITFR 577
Cdd:PRK13409 480 PSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGEPGKHGHASGPMDMREGMNRFLKELGITFR 559
|
570 580 590
....*....|....*....|....*....|.
gi 17555800 578 RDQETYRPRINKLDSVKDVDQKKSGQFFFLD 608
Cdd:PRK13409 560 RDEETGRPRVNKPGSYLDREQKERGEYYYAD 590
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
89-343 |
1.31e-172 |
|
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: 490.34 E-value: 1.31e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 89 NLANETTHRYSQNSFKLHRLPTPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIINHFRGSELQNYFT 168
Cdd:cd03236 1 ELEDEPVHRYGPNSFKLHRLPVPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 169 RILEDTLKCVIKPQYVDQIPRAAKGTVEKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADV 248
Cdd:cd03236 81 KLLEGDVKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 249 YMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSDFICCLYGVPGVYGVVTLPSGVREGINMFLEGFI 328
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPGAYGVVTLPKSVREGINEFLDGYL 240
|
250
....*....|....*
gi 17555800 329 RTENMRFRESKLSFK 343
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) ... |
357-602 |
4.14e-164 |
|
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: 468.04 E-value: 4.14e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 357 IKYPSMSKTLGNFHLDVEAGDFSDSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQKISPKSETTVRF 436
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 437 MLHDKIQNMYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKR 516
Cdd:cd03237 81 LLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 517 FIMHAKKTAFVVEHDFIMATYLADRVVVFEGQPSVKCTACKPQSLLEGMNRFLKMLDITFRRDQETYRPRINKLDSVKDV 596
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVANPPQSLRSGMNRFLKNLDITFRRDPETGRPRINKLGSVKDR 240
|
....*.
gi 17555800 597 DQKKSG 602
Cdd:cd03237 241 EQKESG 246
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
357-577 |
1.94e-95 |
|
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: 289.86 E-value: 1.94e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 357 IKYPSMSKTLGNFHLDVEAGDFSDSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQKISpksettvrf 436
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYID--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 437 mlhdkiqnmyehpqfktdvmnplmmeqlldrnvkeLSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKR 516
Cdd:cd03222 72 -----------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17555800 517 FIMHAKKTAFVVEHDFIMATYLADRVVVFEGQPSVKCTACKPQSLLEGMNRFLKMLDITFR 577
Cdd:cd03222 117 LSEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYLITFR 177
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
98-350 |
2.55e-48 |
|
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: 169.13 E-value: 2.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 98 YSQNSFKLHRLP-TPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNfqkeqewttiinhfrgselqnyftrILEDTLK 176
Cdd:cd03237 8 KTLGEFTLEVEGgSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD-------------------------IEIELDT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 177 CVIKPQYV--DQipraaKGTVEKNL---TRKHDNDNL--NSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVY 249
Cdd:cd03237 63 VSYKPQYIkaDY-----EGTVRDLLssiTKDFYTHPYfkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 250 MFDEPSSYLDVKQRLKAAAIIReRVSDTN--YVVVVEHDLAVLDYLSDFICCLYGVPGVYGVVTLPSGVREGINMFLEG- 326
Cdd:cd03237 138 LLDEPSAYLDVEQRLMASKVIR-RFAENNekTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVANPPQSLRSGMNRFLKNl 216
|
250 260
....*....|....*....|....*....
gi 17555800 327 ---FIR-TENMRFRESKL-SFKTSEQQED 350
Cdd:cd03237 217 ditFRRdPETGRPRINKLgSVKDREQKES 245
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
95-332 |
2.40e-45 |
|
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: 158.50 E-value: 2.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 95 THRYSqNSFKLHRLPTPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNfqkeQEWttiinhfrgselqnyftrileDT 174
Cdd:cd03222 7 VKRYG-VFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN----DEW---------------------DG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 175 LKCVIKPQYVDqipraakgtveknltrkhdndnlnsvidqmelrglldreidqLSGGELQRFAIAMCCVQKADVYMFDEP 254
Cdd:cd03222 61 ITPVYKPQYID------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEP 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 255 SSYLDVKQRLKAAAIIReRVSDTNY--VVVVEHDLAVLDYLSDFICCLYGVPGVYGVVTLPSGVREGINMFLEGFIRTEN 332
Cdd:cd03222 99 SAYLDIEQRLNAARAIR-RLSEEGKktALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYLITFR 177
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
380-570 |
6.47e-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: 138.27 E-value: 6.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 380 DSEIIVMLGENGTGKTTMIKMMAGSLKPE----------DE------NTELPH---------VSISYKPQKIS--PKSET 432
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNlgkfddppdwDEildefrGSELQNyftkllegdVKVIVKPQYVDliPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 433 -TVRFMLHDKIQNmyehpQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAA 511
Cdd:cd03236 105 gKVGELLKKKDER-----GKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 512 KVIKRFIMHaKKTAFVVEHDFIMATYLADRVVVFEGQPSVKCTACKPQSLLEGMNRFLK 570
Cdd:cd03236 180 RLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLYGEPGAYGVVTLPKSVREGINEFLD 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
102-544 |
2.02e-31 |
|
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: 128.10 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQkPNLGNFQKE-----QEWTTIINHFRGSE----LQNYFTRILe 172
Cdd:COG1123 26 SLTIAP------GETVALVGESGSGKSTLALALMGLL-PHGGRISGEvlldgRDLLELSEALRGRRigmvFQDPMTQLN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 173 dtlkcvikPQYV-DQIpraAKGTVEKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMF 251
Cdd:COG1123 98 --------PVTVgDQI---AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 252 DEPSSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDLAVLDYLSDFICCLYGVPGV-----YGVVTLPSGVREGINMFLE 325
Cdd:COG1123 167 DEPTTALDVTTQAEILDLLRELQRERGTtVLLITHDLGVVAEIADRVVVMDDGRIVedgppEEILAAPQALAAVPRLGAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 326 GFIRTENMRFRESKLSFKtseqqeDIKRTGNIKYPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSL 405
Cdd:COG1123 247 RGRAAPAAAAAEPLLEVR------NLSKRYPVRGKGGVRAVDDVSLTLRRG-----ETLGLVGESGSGKSTLARLLLGLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 406 KPEDEntelphvSISYKPQKISPKSETTVRfMLHDKIQNMYEHP--QFktdvmNPLMM---------------------- 461
Cdd:COG1123 316 RPTSG-------SILFDGKDLTKLSRRSLR-ELRRRVQMVFQDPysSL-----NPRMTvgdiiaeplrlhgllsraerre 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 462 ------------EQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEP-SAyLDseqRLHAAKVIkRFIMHAKK----T 524
Cdd:COG1123 383 rvaellervglpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPtSA-LD---VSVQAQIL-NLLRDLQRelglT 457
|
490 500
....*....|....*....|
gi 17555800 525 AFVVEHDFIMATYLADRVVV 544
Cdd:COG1123 458 YLFISHDLAVVRYIADRVAV 477
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
102-287 |
9.81e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 107.14 E-value: 9.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIinHFRGSELQNYFTRILedTLKCVIKP 181
Cdd:cd03214 19 SLSIEA------GEIVGILGPNGAGKSTLLKTLAGLLKPSSG---------EI--LLDGKDLASLSPKEL--ARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QyvdqipraakgtveknltrkhdndnlnsVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVK 261
Cdd:cd03214 80 Q----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180
....*....|....*....|....*..
gi 17555800 262 QRLKAAAIIRERVSDTNY-VVVVEHDL 287
Cdd:cd03214 132 HQIELLELLRRLARERGKtVVMVLHDL 158
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
114-287 |
3.52e-26 |
|
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: 107.82 E-value: 3.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIinHFRGSELQNYftriledtlkcviKPQ-------YVDQ 186
Cdd:COG1120 27 GEVTALLGPNGSGKSTLLRALAGLLKPSSG---------EV--LLDGRDLASL-------------SRRelarriaYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 187 IPRAAKG-TVE-----------KNLTR--KHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFD 252
Cdd:COG1120 83 EPPAPFGlTVRelvalgryphlGLFGRpsAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLD 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 17555800 253 EPSSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDL 287
Cdd:COG1120 163 EPTSHLDLAHQLEVLELLRRLARERGRtVVMVLHDL 198
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
102-546 |
5.97e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.00 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWT--------------TIIN-----HFRGSE 162
Cdd:COG0488 18 SLSINP------GDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRigylpqeppldddlTVLDtvldgDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 163 LQNYFTRILEDTlkcvikPQYVDQIPRAAKgtVEKNLTRkHDNDNLNSVIDQMeLRGL------LDREIDQLSGGELQRF 236
Cdd:COG0488 92 LEAELEELEAKL------AEPDEDLERLAE--LQEEFEA-LGGWEAEARAEEI-LSGLgfpeedLDRPVSELSGGWRRRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 237 AIAMCCVQKADVYMFDEPSSYLDVK------QRLKaaaiirervsdtNY---VVVVEHDLAVLDYLSDFICCLYgvpgvY 307
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLEsiewleEFLK------------NYpgtVLVVSHDRYFLDRVATRILELD-----R 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 308 GVVTLPSG--------------------------VREginmfLEGFIRtenmRFRE--SKLSFKTS--------EQQEDI 351
Cdd:COG0488 225 GKLTLYPGnysayleqraerleqeaaayakqqkkIAK-----EEEFIR----RFRAkaRKAKQAQSrikaleklEREEPP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 352 KRTGN--IKYPSM-------------SKTLG------NFHLDVEAGDfsdseIIVMLGENGTGKTTMIKMMAGSLKPEDE 410
Cdd:COG0488 296 RRDKTveIRFPPPerlgkkvleleglSKSYGdktlldDLSLRIDRGD-----RIGLIGPNGAGKSTLLKLLAGELEPDSG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 411 NTEL-PHVSISYKPQKISP-KSETTVRFMLHDKIQNMYEhpqfkTDVMNplMMEQLL------DRNVKELSGGELQRVAL 482
Cdd:COG0488 371 TVKLgETVKIGYFDQHQEElDPDKTVLDELRDGAPGGTE-----QEVRG--YLGRFLfsgddaFKPVGVLSGGEKARLAL 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 483 ALCLGKTASLYLIDEPSAYLDSEQRlhaaKVIKRFIMHAKKTAFVVEHD--FIMAtyLADRVVVFE 546
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIETL----EALEEALDDFPGTVLLVSHDryFLDR--VATRILEFE 503
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
366-547 |
2.00e-24 |
|
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: 100.59 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSIS-YKPQKISPKsettVRFMlhdkiqn 444
Cdd:cd03214 15 LDDLSLSIEAG-----EIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAsLSPKELARK----IAYV------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 445 myehPQfktdVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKT 524
Cdd:cd03214 79 ----PQ----ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKT 150
|
170 180
....*....|....*....|...
gi 17555800 525 AFVVEHDFIMATYLADRVVVFEG 547
Cdd:cd03214 151 VVMVLHDLNLAARYADRVILLKD 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
355-546 |
2.65e-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: 96.55 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 355 GNIKYPSmSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPedentelPHVSISYKPQKISPKSETTV 434
Cdd:cd00267 5 LSFRYGG-RTALDNVSLTLKAG-----EIVALVGPNGSGKSTLLRAIAGLLKP-------TSGEILIDGKDIAKLPLEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 435 RfmlhDKIQnmYehpqfktdvmnplmmeqlldrnVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVI 514
Cdd:cd00267 72 R----RRIG--Y----------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELL 123
|
170 180 190
....*....|....*....|....*....|..
gi 17555800 515 KRFIMHaKKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:cd00267 124 RELAEE-GRTVIIVTHDPELAELAADRVIVLK 154
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
357-545 |
2.84e-23 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 98.95 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 357 IKYPSMSKTLGNFHLDVEAGDFSDSEIIVMLGENGTGKTTMIKMMAGSLKPE--------DENTELP--HVSISYKPQKI 426
Cdd:cd03299 1 LKVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDsgkillngKDITNLPpeKRDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 427 SPKSETTVR----FMLHDKIQNMYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYL 502
Cdd:cd03299 81 ALFPHMTVYkniaYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17555800 503 DSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVF 545
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIM 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
114-298 |
4.84e-23 |
|
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: 97.60 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFqkeqewttiinHFRGSELQNYFTRIledtlkcvikpQYVDQ---IPRA 190
Cdd:cd03235 25 GEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI-----------RVFGKPLEKERKRI-----------GYVPQrrsIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 191 AKGTVE--------------KNLTRKhDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSS 256
Cdd:cd03235 83 FPISVRdvvlmglyghkglfRRLSKA-DKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17555800 257 YLDVKQRLKAAAIIRERVSDTNYVVVVEHDL-AVLDYLSDFIC 298
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLgLVLEYFDRVLL 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
366-544 |
1.15e-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: 97.42 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPED-----ENTELPHVS-------ISYKPQKISPKSETT 433
Cdd:COG1120 17 LDDVSLSLPPG-----EVTALLGPNGSGKSTLLRALAGLLKPSSgevllDGRDLASLSrrelarrIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 434 VRFML------HdkiQNMYEHPQfKTD------VMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAY 501
Cdd:COG1120 92 VRELValgrypH---LGLFGRPS-AEDreaveeALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17555800 502 LDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVV 544
Cdd:COG1120 168 LDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVL 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
358-546 |
1.37e-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: 96.00 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 358 KYPS-MSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQK-ISPK------ 429
Cdd:cd03225 8 SYPDgARPALDDISLTIKKG-----EFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKeLRRKvglvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 430 ------SETTVR----F---MLHDKIQNMYEHpqfKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLID 496
Cdd:cd03225 83 npddqfFGPTVEeevaFgleNLGLPEEEIEER---VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17555800 497 EPSAYLDSEQRLHAAKVIKRFImHAKKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
364-544 |
2.28e-22 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 95.40 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 364 KTLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAG-----------------SLKPEDENTEL--------PHVS 418
Cdd:cd03301 14 TALDDLNLDIADGEF-----VVLLGPSGCGKTTTLRMIAGleeptsgriyiggrdvtDLPPKDRDIAMvfqnyalyPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 419 ----ISYkPQKI--SPKSETTVRFmlhdkiqnmyehpqfkTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASL 492
Cdd:cd03301 89 vydnIAF-GLKLrkVPKDEIDERV----------------REVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17555800 493 YLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVV 544
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAV 203
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
112-298 |
2.94e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 96.31 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 112 RCGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIinHFRGSELQNYFTRIledtlkcvikpQYVDQIPRAA 191
Cdd:COG1121 30 PPGEFVAIVGPNGAGKSTLLKAILGLLPPTSG---------TV--RLFGKPPRRARRRI-----------GYVPQRAEVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 192 KG---TVE----------KNLTR---KHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPS 255
Cdd:COG1121 88 WDfpiTVRdvvlmgrygrRGLFRrpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPF 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17555800 256 SYLDVKQRLKAAAIIRERVSDTNYVVVVEHDL-AVLDYLSDFIC 298
Cdd:COG1121 168 AGVDAATEEALYELLRELRREGKTILVVTHDLgAVREYFDRVLL 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
366-547 |
5.89e-22 |
|
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: 94.52 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPE-------DENTELPHVSISYKPQK--ISPKSETTVR- 435
Cdd:cd03235 15 LEDVSFEVKPGEF-----LAIVGPNGAGKSTLLKAILGLLKPTsgsirvfGKPLEKERKRIGYVPQRrsIDRDFPISVRd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 436 -----FMLHDKIQNMYEHPQFKtDVMNPLM---MEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQR 507
Cdd:cd03235 90 vvlmgLYGHKGLFRRLSKADKA-KVDEALErvgLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17555800 508 LHAAKVIKRfiMHAK-KTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:cd03235 169 EDIYELLRE--LRREgMTILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
366-544 |
7.07e-22 |
|
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: 94.12 E-value: 7.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAG-----------------SLKPEDENTEL--------PHVS-- 418
Cdd:cd03259 16 LDDLSLTVEPG-----EFLALLGPSGCGKTTLLRLIAGlerpdsgeilidgrdvtGVPPERRNIGMvfqdyalfPHLTva 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 419 --ISYkPQKISPKSETTVRfmlhDKIQNMYEHpqfktdvmnpLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLID 496
Cdd:cd03259 91 enIAF-GLKLRGVPKAEIR----ARVRELLEL----------VGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17555800 497 EPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVV 544
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAV 203
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
114-300 |
1.20e-21 |
|
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: 93.30 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGN--FQKEQEWTTIINHFR---GSELQNYFTRILEDTLKcvikpqyvDQIp 188
Cdd:cd03225 27 GEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvlVDGKDLTKLSLKELRrkvGLVFQNPDDQFFGPTVE--------EEV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 189 raAKGTVEKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAA 268
Cdd:cd03225 98 --AFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE 175
|
170 180 190
....*....|....*....|....*....|..
gi 17555800 269 IIRERVSDTNYVVVVEHDLAVLDYLSDFICCL 300
Cdd:cd03225 176 LLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
364-544 |
1.22e-21 |
|
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: 94.15 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 364 KTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKP---------EDENTELPHV--SISYKPQKISPKSET 432
Cdd:COG4555 15 PALKDVSFTAKDG-----EITGLLGPNGAGKTTLLRMLAGLLKPdsgsilidgEDVRKEPREArrQIGVLPDERGLYDRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 433 TVR------FMLHDkiqNMYEHPQFKTDVMNPLM-MEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDse 505
Cdd:COG4555 90 TVReniryfAELYG---LFDEELKKRIEELIELLgLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD-- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17555800 506 qrLHAAKVIKRFIMHAK---KTAFVVEHDFIMATYLADRVVV 544
Cdd:COG4555 165 --VMARRLLREILRALKkegKTVLFSSHIMQEVEALCDRVVI 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
366-548 |
1.91e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 93.62 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPE-------DENTELPHVSISYKPQKIS-----PkseTT 433
Cdd:COG1121 22 LEDVSLTIPPGEF-----VAIVGPNGAGKSTLLKAILGLLPPTsgtvrlfGKPPRRARRRIGYVPQRAEvdwdfP---IT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 434 VR-FML-----------------HDKIQNMYEhpqfKTDvmnplmMEQLLDRNVKELSGGELQRVALALCLGKTASLYLI 495
Cdd:COG1121 94 VRdVVLmgrygrrglfrrpsradREAVDEALE----RVG------LEDLADRPIGELSGGQQQRVLLARALAQDPDLLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 496 DEPSAYLD--SEQRLhaAKVIKRFImHAKKTAFVVEHDFIMATYLADRVVVFEGQ 548
Cdd:COG1121 164 DEPFAGVDaaTEEAL--YELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
101-300 |
2.11e-21 |
|
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: 91.15 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 101 NSFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFqkeqewttiinHFRGSELQNYFTRILEDTLkcvik 180
Cdd:cd00267 18 VSLTLKA------GEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI-----------LIDGKDIAKLPLEELRRRI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 181 pQYVDQipraakgtveknltrkhdndnlnsvidqmelrglldreidqLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDV 260
Cdd:cd00267 76 -GYVPQ-----------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17555800 261 KQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSDFICCL 300
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
114-290 |
5.07e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.14 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewttiinhfrgselqnyftrilEDTLKCVIKPQYVDQ---IPRA 190
Cdd:NF040873 18 GSLTAVVGPNGSGKSTLLKVLAGVLRPTSG----------------------------TVRRAGGARVAYVPQrseVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 191 AKGTV----------EKNLTRKHDNDNLNSVIDQME---LRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSY 257
Cdd:NF040873 70 LPLTVrdlvamgrwaRRGLWRRLTRDDRAAVDDALErvgLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|...
gi 17555800 258 LDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVL 290
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
363-544 |
3.05e-20 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 90.12 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 363 SKTLGNFH------LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKP---------EDENTELPHV--SISYKPQK 425
Cdd:COG1131 7 TKRYGDKTaldgvsLTVEPG-----EIFGLLGPNGAGKTTTIRMLLGLLRPtsgevrvlgEDVARDPAEVrrRIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 426 ISPKSETTVRFMLhDKIQNMYEHPQFKTD-----VMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSA 500
Cdd:COG1131 82 PALYPDLTVRENL-RFFARLYGLPRKEARerideLLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17555800 501 YLDSEQRLHAAKVIKRfIMHAKKTAFVVEHdfIM--ATYLADRVVV 544
Cdd:COG1131 161 GLDPEARRELWELLRE-LAAEGKTVLLSTH--YLeeAERLCDRVAI 203
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
356-547 |
3.26e-20 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 89.10 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 356 NIKYPSMSKT-LGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGsLKPEDENTelphvsISYKPQKISPKSETTV 434
Cdd:COG4619 5 GLSFRVGGKPiLSPVSLTLEAGEC-----VAITGPSGSGKSTLLRALAD-LDPPTSGE------IYLDGKPLSAMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 435 R----------FMLHDKIQNMYEHP-QFKTDVMNP----LMMEQL------LDRNVKELSGGELQRVALALCLGKTASLY 493
Cdd:COG4619 73 RrqvayvpqepALWGGTVRDNLPFPfQLRERKFDReralELLERLglppdiLDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17555800 494 LIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
366-500 |
3.88e-20 |
|
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: 87.32 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPE------------DENTELPHVSISYKPQKISPKSETT 433
Cdd:pfam00005 1 LKNVSLTLNPG-----EILALVGPNGAGKSTLLKLIAGLLSPTegtilldgqdltDDERKSLRKEIGYVFQDPQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 434 VR--FMLHDKIQNMYEHPQFK--TDVMN----PLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSA 500
Cdd:pfam00005 76 VRenLRLGLLLKGLSKREKDAraEEALEklglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
358-547 |
5.03e-20 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 87.44 E-value: 5.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 358 KYPSMSK-TLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSIsykpQKISPKSettvrf 436
Cdd:cd03228 9 SYPGRPKpVLKDVSLTIKPG-----EKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDL----RDLDLES------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 437 mLHDKI----QNMYehpqfktdvmnplmmeqLLDRNVKE--LSGGELQRVALALCLGKTASLYLIDEPSAYLD--SEQRL 508
Cdd:cd03228 74 -LRKNIayvpQDPF-----------------LFSGTIREniLSGGQRQRIAIARALLRDPPILILDEATSALDpeTEALI 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 17555800 509 HAAkvIKRfiMHAKKTAFVVEHDFIMATyLADRVVVFEG 547
Cdd:cd03228 136 LEA--LRA--LAKGKTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
102-300 |
5.27e-20 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 88.72 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIInhFRGSELQNYftriledtlkcviKP 181
Cdd:COG4619 20 SLTLEA------GECVAITGPSGSGKSTLLRALADLDPPTSG---------EIY--LDGKPLSAM-------------PP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 Q-------YVDQIPRAAKGTVEKNLTR----KHDNDNLNSVIDQMELRGL----LDREIDQLSGGELQRFAIAMCCVQKA 246
Cdd:COG4619 70 PewrrqvaYVPQEPALWGGTVRDNLPFpfqlRERKFDRERALELLERLGLppdiLDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 247 DVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDLAVLDYLSDFICCL 300
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRaVLWVSHDPEQIERVADRVLTL 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
358-547 |
6.16e-20 |
|
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: 88.93 E-value: 6.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 358 KYPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDentelphVSISYKPQKISPKSETTVRF- 436
Cdd:COG1122 9 SYPGGTPALDDVSLSIEKG-----EFVAIIGPNGSGKSTLLRLLNGLLKPTS-------GEVLVDGKDITKKNLRELRRk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 437 --MLHdkiQNmYEHpQF--KT---DVMNPLM---------------------MEQLLDRNVKELSGGELQRVALAlclgk 488
Cdd:COG1122 77 vgLVF---QN-PDD-QLfaPTveeDVAFGPEnlglpreeirerveealelvgLEHLADRPPHELSGGQKQRVAIA----- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 489 tASL-----YLI-DEPSAYLDSEQRLHAAKVIKRFImHAKKTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:COG1122 147 -GVLamepeVLVlDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
102-295 |
6.37e-20 |
|
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: 89.48 E-value: 6.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFqkeqewttiinHFRGSELQNYFTRiledTLKCVIkp 181
Cdd:COG1124 25 SLEVAP------GESFGLVGESGSGKSTLLRALAGLERPWSGEV-----------TFDGRPVTRRRRK----AFRRRV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVDQIPRAA---KGTVE-------KNLTRKHDNDNLNSVIDQMEL-RGLLDREIDQLSGGELQRFAIAMCCVQKADVYM 250
Cdd:COG1124 82 QMVFQDPYASlhpRHTVDrilaeplRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17555800 251 FDEPSSYLDVK-QRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSD 295
Cdd:COG1124 162 LDEPTSALDVSvQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCD 207
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
102-302 |
2.28e-19 |
|
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: 87.18 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIInhFRGSELQNYFTRILEDTLKcviKP 181
Cdd:cd03257 25 SFSIKK------GETLGLVGESGSGKSTLARAILGLLKPTSG---------SII--FDGKDLLKLSRRLRKIRRK---EI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVDQIPRAA---KGTVEKNLT------RKHDNDNLNSVIDQMELRGL------LDREIDQLSGGELQRFAIAMCCVQKA 246
Cdd:cd03257 85 QMVFQDPMSSlnpRMTIGEQIAeplrihGKLSKKEARKEAVLLLLVGVglpeevLNRYPHELSGGQRQRVAIARALALNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 247 DVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDLAVLDYLSDFICCLYG 302
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEELGLtLLFITHDLGVVAKIADRVAVMYA 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
102-256 |
3.05e-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: 84.62 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIinHFRGSELQNYFTRILEDTLKCVikP 181
Cdd:pfam00005 5 SLTLNP------GEILALVGPNGAGKSTLLKLIAGLLSPTEG---------TI--LLDGQDLTDDERKSLRKEIGYV--F 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVDQIPRAakgTVEKNL---------TRKHDNDNLNSVIDQMELRGLLDREID----QLSGGELQRFAIAMCCVQKADV 248
Cdd:pfam00005 66 QDPQLFPRL---TVRENLrlglllkglSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKL 142
|
....*...
gi 17555800 249 YMFDEPSS 256
Cdd:pfam00005 143 LLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
114-291 |
7.15e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 85.22 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIinHFRGSELQNYFTRILEDTLkcvikpqYVDQIPrAAKG 193
Cdd:COG4133 28 GEALALTGPNGSGKTTLLRILAGLLPPSAG---------EV--LWNGEPIRDAREDYRRRLA-------YLGHAD-GLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 --TVEKNLT-------RKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRL 264
Cdd:COG4133 89 elTVRENLRfwaalygLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVA 168
|
170 180
....*....|....*....|....*..
gi 17555800 265 KAAAIIRERVSDTNYVVVVEHDLAVLD 291
Cdd:COG4133 169 LLAELIAAHLARGGAVLLTTHQPLELA 195
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
363-549 |
7.19e-19 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 85.42 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 363 SKTLGNFHLDVeagDFS-DSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHV----------------SISYKPQK 425
Cdd:cd03297 7 EKRLPDFTLKI---DFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 426 ISPKSETTVR----FMLHDKIQNmyEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAY 501
Cdd:cd03297 84 YALFPHLNVRenlaFGLKRKRNR--EDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17555800 502 LDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFE-GQP 549
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEdGRL 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
363-544 |
1.12e-18 |
|
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: 83.60 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 363 SKTLGNFH------LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKP---------EDENTELPHV--SISYKPQK 425
Cdd:cd03230 7 SKRYGKKTalddisLTVEKG-----EIYGLLGPNGAGKTTLIKIILGLLKPdsgeikvlgKDIKKEPEEVkrRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 426 ISPKSETTVRFMLhdkiqnmyehpqfktdvmnplmmeqlldrnvkELSGGELQRVALALCLGKTASLYLIDEPSAYLDSE 505
Cdd:cd03230 82 PSLYENLTVRENL--------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190
....*....|....*....|....*....|....*....
gi 17555800 506 QRLHAAKVIKRfIMHAKKTAFVVEHDFIMATYLADRVVV 544
Cdd:cd03230 130 SRREFWELLRE-LKKEGKTILLSSHILEEAERLCDRVAI 167
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
363-544 |
1.15e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.82 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 363 SKTLGNFH------LDVEAGDFsdseiIVMLGENGTGKTTMIKMMAG-----------------SLKPEDENTEL----- 414
Cdd:COG3839 10 SKSYGGVEalkdidLDIEDGEF-----LVLLGPSGCGKSTLLRMIAGledptsgeiliggrdvtDLPPKDRNIAMvfqsy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 415 ---PHVS----ISY--KPQKIsPKSEttvrfmLHDKIQNMYEhpqfktdvMnpLMMEQLLDRNVKELSGGELQRVALALC 485
Cdd:COG3839 85 alyPHMTvyenIAFplKLRKV-PKAE------IDRRVREAAE--------L--LGLEDLLDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17555800 486 LGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFimHAK-KTAFV-VEHDFIMATYLADRVVV 544
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRL--HRRlGTTTIyVTHDQVEAMTLADRIAV 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
102-301 |
1.42e-18 |
|
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: 89.19 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIInhFRGSELQNYFTRILEDTLKCVikp 181
Cdd:COG1123 285 SLTLRR------GETLGLVGESGSGKSTLARLLLGLLRPTSG---------SIL--FDGKDLTKLSRRSLRELRRRV--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVDQIPRAA---KGTVE----------KNLTRKHDNDNLNSVIDQMEL-RGLLDREIDQLSGGELQRFAIAMCCVQKAD 247
Cdd:COG1123 345 QMVFQDPYSSlnpRMTVGdiiaeplrlhGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPK 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 248 VYMFDEPSSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDLAVLDYLSDFICCLY 301
Cdd:COG1123 425 LLILDEPTSALDVSVQAQILNLLRDLQRELGLtYLFISHDLAVVRYIADRVAVMY 479
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
114-295 |
1.47e-18 |
|
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: 85.29 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIINHFRGSELQNYFTR----ILEDtlkcvikpqyvdQIPR 189
Cdd:COG4555 27 GEITGLLGPNGAGKTTLLRMLAGLLKPDSG---------SILIDGEDVRKEPREARrqigVLPD------------ERGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 190 AAKGTVEKNL---------TRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDV 260
Cdd:COG4555 86 YDRLTVRENIryfaelyglFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV 165
|
170 180 190
....*....|....*....|....*....|....*
gi 17555800 261 KQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSD 295
Cdd:COG4555 166 MARRLLREILRALKKEGKTVLFSSHIMQEVEALCD 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
114-563 |
2.49e-18 |
|
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: 88.32 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQkpnlgnfQKEQEWTTIINHFRGSELQNYFTRILEDTLKC-----VIKPQYVDQIP 188
Cdd:TIGR03269 26 GEVLGILGRSGAGKSVLMHVLRGMD-------QYEPTSGRIIYHVALCEKCGYVERPSKVGEPCpvcggTLEPEEVDFWN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 189 RAAKgtVEKNLTRK------------HDNDNLNSVIDQMELRGL-----LDREID----------------QLSGGELQR 235
Cdd:TIGR03269 99 LSDK--LRRRIRKRiaimlqrtfalyGDDTVLDNVLEALEEIGYegkeaVGRAVDliemvqlshrithiarDLSGGEKQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 236 FAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDLAVLDYLSDFICCLYGvpgvyGVVTLPS 314
Cdd:TIGR03269 177 VVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLTSHWPEVIEDLSDKAIWLEN-----GEIKEEG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 315 GVREGINMFLEGFIRTEnmRFRESklsfktsEQQEDIKRTGNIK--YPSMS----KTLGNFHLDVEAGdfsdsEIIVMLG 388
Cdd:TIGR03269 252 TPDEVVAVFMEGVSEVE--KECEV-------EVGEPIIKVRNVSkrYISVDrgvvKAVDNVSLEVKEG-----EIFGIVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 389 ENGTGKTTMIKMMAGSLKPE---------DENTEL------------PHVSISYKPQKISPKSET------TVRFMLHDK 441
Cdd:TIGR03269 318 TSGAGKTTLSKIIAGVLEPTsgevnvrvgDEWVDMtkpgpdgrgrakRYIGILHQEYDLYPHRTVldnlteAIGLELPDE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 442 IQNMYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVikrfIMHA 521
Cdd:TIGR03269 398 LARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHS----ILKA 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 17555800 522 KK----TAFVVEHDFIMATYLADRVVVFEGQPSVKCTacKPQSLLE 563
Cdd:TIGR03269 474 REemeqTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG--DPEEIVE 517
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
366-546 |
6.66e-18 |
|
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: 81.85 E-value: 6.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPeDENtelpHVSIS----YKPQKISPKSETTVRFMLHDk 441
Cdd:cd03229 16 LNDVSLNIEAG-----EIVALLGPSGSGKSTLLRCIAGLEEP-DSG----SILIDgedlTDLEDELPPLRRRIGMVFQD- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 442 iQNMYEHPQFKTDVMNPLmmeqlldrnvkelSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHA 521
Cdd:cd03229 85 -FALFPHLTVLENIALGL-------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQL 150
|
170 180
....*....|....*....|....*
gi 17555800 522 KKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:cd03229 151 GITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
102-287 |
7.45e-18 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 82.30 E-value: 7.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIINHFRGSEL--QNYFTRILEDTLKcvi 179
Cdd:cd03226 20 SLDLYA------GEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYvmQDVDYQLFTDSVR--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 180 kpqyvDQIPRAAKGTVEKNLTRKHdndnlnsVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLD 259
Cdd:cd03226 91 -----EELLLGLKELDAGNEQAET-------VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180
....*....|....*....|....*...
gi 17555800 260 VKQRLKAAAIIRERVSDTNYVVVVEHDL 287
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHDY 186
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
114-295 |
8.86e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 82.80 E-value: 8.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFqkeqewtTIINHFRGSELQNYFTRIledtlkCVIkPQYVDQIPRAakg 193
Cdd:COG1131 26 GEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEV-------RVLGEDVARDPAEVRRRI------GYV-PQEPALYPDL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TVEKNL---------TRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRL 264
Cdd:COG1131 89 TVRENLrffarlyglPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARR 168
|
170 180 190
....*....|....*....|....*....|.
gi 17555800 265 KAAAIIRERVSDTNYVVVVEHDLAVLDYLSD 295
Cdd:COG1131 169 ELWELLRELAAEGKTVLLSTHYLEEAERLCD 199
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
356-543 |
3.34e-17 |
|
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: 80.38 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 356 NIKYPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEdentelpHVSISYKPQKISPKS----- 430
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAG-----EIIALTGKNGAGKTTLAKILAGLIKES-------SGSILLNGKPIKAKErrksi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 431 ------------ETTVRFMLHDKIQNMYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALA--LCLGKTasLYLID 496
Cdd:cd03226 74 gyvmqdvdyqlfTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAaaLLSGKD--LLIFD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17555800 497 EPSAYLDSEQRLHAAKVIKRfIMHAKKTAFVVEHDFIMATYLADRVV 543
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRE-LAAQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
366-549 |
3.54e-17 |
|
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: 80.59 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKP-------EDENTELPHVSISYKPQKIS--P-KsetTVR 435
Cdd:cd03293 20 LEDISLSVEEG-----EFVALVGPSGCGKSTLLRIIAGLERPtsgevlvDGEPVTGPGPDRGYVFQQDAllPwL---TVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 436 --FMLHDKIQNMyEHPQFKTDVMNPLMM---EQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHA 510
Cdd:cd03293 92 dnVALGLELQGV-PKAEARERAEELLELvglSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 17555800 511 AKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEGQP 549
Cdd:cd03293 171 QEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARP 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
114-298 |
4.71e-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: 80.42 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewTTIINHfrgselqnyftRILEDTLKCVIKPQ------YVDQ- 186
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGG--------TIVLNG-----------TVLFDSRKKINLPPqqrkigLVFQq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 187 ---IPRAakgTVEKNLT-------RKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSS 256
Cdd:cd03297 84 yalFPHL---NVRENLAfglkrkrNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17555800 257 YLDVKQRLKAAAIIRERVSDTNYVVV-VEHDLAVLDYLSDFIC 298
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIfVTHDLSEAEYLADRIV 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
114-505 |
5.92e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 84.62 E-value: 5.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTiinhfrgSELQnyftrilEDtlkcvikPqyvdqiPRAAKG 193
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIV-------ARLQ-------QD-------P------PRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TV------------------------------EKNLTR------KHDNDNL-------NSVIDQMELRGllDREIDQLSG 230
Cdd:PRK11147 82 TVydfvaegieeqaeylkryhdishlvetdpsEKNLNElaklqeQLDHHNLwqlenriNEVLAQLGLDP--DAALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 231 GELQRFAIAMCCVQKADVYMFDEPSSYLDV------KQRLKA--AAIirervsdtnyvVVVEHDLAVLDYLSDFICCL-Y 301
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIetiewlEGFLKTfqGSI-----------IFISHDRSFIRNMATRIVDLdR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 302 GV----PGVYGVVTLPSG-----------------------VREGI------NmflEGFIR------TENMRFRESKLSF 342
Cdd:PRK11147 229 GKlvsyPGNYDQYLLEKEealrveelqnaefdrklaqeevwIRQGIkarrtrN---EGRVRalkalrRERSERREVMGTA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 343 KTseQQEDIKRTG-------NIKYPSMSKTL-GNFHLDVEAGDfsdseIIVMLGENGTGKTTMIKMMAGSLKPEDEN--- 411
Cdd:PRK11147 306 KM--QVEEASRSGkivfemeNVNYQIDGKQLvKDFSAQVQRGD-----KIALIGPNGCGKTTLLKLMLGQLQADSGRihc 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 412 -TELphvSISY--------KPQKI------SPKSETTV----RFMLhDKIQNMYEHPQfktDVMNPlmmeqlldrnVKEL 472
Cdd:PRK11147 379 gTKL---EVAYfdqhraelDPEKTvmdnlaEGKQEVMVngrpRHVL-GYLQDFLFHPK---RAMTP----------VKAL 441
|
490 500 510
....*....|....*....|....*....|...
gi 17555800 473 SGGELQRVALALCLGKTASLYLIDEPSAYLDSE 505
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
107-287 |
8.75e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.44 E-value: 8.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 107 RLPTprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFqkeqewttiinHFRGSELQNYFTRILEDTLKcvikpqYVDQ 186
Cdd:PRK11231 24 SLPT---GKITALIGPNGCGKSTLLKCFARLLTPQSGTV-----------FLGDKPISMLSSRQLARRLA------LLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 187 IPRAAKG-TVEK--------------NLTRKhDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMF 251
Cdd:PRK11231 84 HHLTPEGiTVRElvaygrspwlslwgRLSAE-DNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 17555800 252 DEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDL 287
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDL 198
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
364-550 |
1.05e-16 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 79.79 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 364 KTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKP---------EDENTELPHVS----ISYKPQKISPKS 430
Cdd:cd03219 14 VALDDVSFSVRPG-----EIHGLIGPNGAGKTTLFNLISGFLRPtsgsvlfdgEDITGLPPHEIarlgIGRTFQIPRLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 431 ETTVR--------------FMLHDKIQNMYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLID 496
Cdd:cd03219 89 ELTVLenvmvaaqartgsgLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17555800 497 EPSAYLDSEQRLHAAKVIKRfIMHAKKTAFVVEHD--FIMAtyLADRVVVF-------EGQPS 550
Cdd:cd03219 169 EPAAGLNPEETEELAELIRE-LRERGITVLLVEHDmdVVMS--LADRVTVLdqgrviaEGTPD 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
356-544 |
1.14e-16 |
|
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: 83.10 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 356 NIKYPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDE-----NTELPHVS-------ISYKP 423
Cdd:TIGR02857 328 SVAYPGRRPALRPVSFTVPPG-----ERVALVGPSGAGKSTLLNLLLGFVDPTEGsiavnGVPLADADadswrdqIAWVP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 424 QK--ISPKSETT-VRFMLHDKIQNMYEHPQFKTDVMN-----PLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLI 495
Cdd:TIGR02857 403 QHpfLFAGTIAEnIRLARPDASDAEIREALERAGLDEfvaalPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17555800 496 DEPSAYLDSEqrlHAAKVIKRFIMHAK-KTAFVVEHDfIMATYLADRVVV 544
Cdd:TIGR02857 483 DEPTAHLDAE---TEAEVLEALRALAQgRTVLLVTHR-LALAALADRIVV 528
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
114-288 |
2.42e-16 |
|
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: 77.94 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGN-FQKEQEWTTIINHFRGSEL--QNYftrILEDTLkcvikpqyvdqipra 190
Cdd:cd03259 26 GEFLALLGPSGCGKTTLLRLIAGLERPDSGEiLIDGRDVTGVPPERRNIGMvfQDY---ALFPHL--------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 191 akgTVEKNL---------TRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVK 261
Cdd:cd03259 88 ---TVAENIafglklrgvPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180
....*....|....*....|....*...
gi 17555800 262 QRLKAAAIIRERVSDTNY-VVVVEHDLA 288
Cdd:cd03259 165 LREELREELKELQRELGItTIYVTHDQE 192
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
112-298 |
6.00e-16 |
|
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: 77.16 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 112 RCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFqkeqewtTIINHFRGSELQNYFTRIledtlkCVIkPQYvDQIPRAA 191
Cdd:cd03263 26 YKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-------YINGYSIRTDRKAARQSL------GYC-PQF-DALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 192 kgTVE---------KNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVK- 261
Cdd:cd03263 91 --TVRehlrfyarlKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAs 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 17555800 262 QRLKAAAIIRERVSDTnyVVVVEHDLAVLDYLSDFIC 298
Cdd:cd03263 169 RRAIWDLILEVRKGRS--IILTTHSMDEAEALCDRIA 203
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
364-548 |
7.22e-16 |
|
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: 74.79 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 364 KTLGNFHLDVEAGDfsdseIIVMLGENGTGKTTMIKMMAGSLKPEDENTEL-PHVSISYKPQkispksettvrfmlhdki 442
Cdd:cd03221 14 LLLKDISLTINPGD-----RIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgSTVKIGYFEQ------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 443 qnmyehpqfktdvmnplmmeqlldrnvkeLSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFimhaK 522
Cdd:cd03221 71 -----------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY----P 117
|
170 180
....*....|....*....|....*.
gi 17555800 523 KTAFVVEHDFIMATYLADRVVVFEGQ 548
Cdd:cd03221 118 GTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
363-547 |
8.22e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 78.99 E-value: 8.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 363 SKTLGNFH------LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAG-----------------SLKPEDENTEL----- 414
Cdd:COG3842 12 SKRYGDVTalddvsLSIEPG-----EFVALLGPSGCGKTTLLRMIAGfetpdsgrilldgrdvtGLPPEKRNVGMvfqdy 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 415 ---PHVS----ISY--KPQKIsPKSE--TTVRFMLhdkiqnmyehpqfktDVMNplmMEQLLDRNVKELSGGELQRVALA 483
Cdd:COG3842 87 alfPHLTvaenVAFglRMRGV-PKAEirARVAELL---------------ELVG---LEGLADRYPHQLSGGQQQRVALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 484 LCLGKTASLYLIDEP-SAyLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:COG3842 148 RALAPEPRVLLLDEPlSA-LDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
91-302 |
8.91e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 8.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 91 ANETTHRYSQNSFK------LHRLP-TPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLG----NFQKEQEWTTiinhfr 159
Cdd:PRK10575 7 HSDTTFALRNVSFRvpgrtlLHPLSlTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGeillDAQPLESWSS------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 160 gselqNYFTRiledtlKCVIKPQyvdQIPRAAKGTVEK-----------NLTR--KHDNDNLNSVIDQMELRGLLDREID 226
Cdd:PRK10575 81 -----KAFAR------KVAYLPQ---QLPAAEGMTVRElvaigrypwhgALGRfgAADREKVEEAISLVGLKPLAHRLVD 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 227 QLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIrERVSDTN--YVVVVEHDLAVLDYLSDFICCLYG 302
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALV-HRLSQERglTVIAVLHDINMAARYCDYLVALRG 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
361-546 |
9.58e-16 |
|
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: 79.00 E-value: 9.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 361 SMSKTLGNFHLDVeAGDFSDSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTEL---------------PHV-SISYKPQ 424
Cdd:TIGR02142 4 RFSKRLGDFSLDA-DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdsrkgiflpPEKrRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 425 KISPKSETTVRF-MLHDKIQNMYEHPQFKTD-VMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYL 502
Cdd:TIGR02142 83 EARLFPHLSVRGnLRYGMKRARPSERRISFErVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17555800 503 DSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLE 206
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
102-301 |
1.06e-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: 76.71 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIinHFRGSEL-----------------Q 164
Cdd:cd03219 20 SFSVRP------GEIHGLIGPNGAGKTTLFNLISGFLRPTSG---------SV--LFDGEDItglppheiarlgigrtfQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 165 NyfTRILED--TLKCVIKPQYVDQIPRAAKGTVEKNLTRkhDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCC 242
Cdd:cd03219 83 I--PRLFPEltVLENVMVAAQARTGSGLLLARARREERE--ARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 243 VQKADVYMFDEPSSYLDVKQRLKAAAIIReRVSDTNY-VVVVEHDLAVLDYLSDFICCLY 301
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIR-ELRERGItVLLVEHDMDVVMSLADRVTVLD 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
358-576 |
1.11e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.34 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 358 KYPSMSK-TLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYK-------------- 422
Cdd:PRK13632 16 SYPNSENnALKNVSFEINEG-----EYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnlkeirkkigiifq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 423 -P--QKISPKSETTVRFMLHDKIQNMYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPS 499
Cdd:PRK13632 91 nPdnQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 500 AYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATyLADRVVVFEGQPSVKctACKPQSLLEGMNRFLKM-LDITF 576
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIA--QGKPKEILNNKEILEKAkIDSPF 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
112-287 |
1.75e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.73 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 112 RCGEVLGLVGTNGIGKSTALKILAGKQKPNLGN---FQKEqewttiINHFRGSELQNyfTR-ILedtlkcvikPQY---- 183
Cdd:PRK13548 26 RPGEVVAILGPNGAGKSTLLRALSGELSPDSGEvrlNGRP------LADWSPAELAR--RRaVL---------PQHssls 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 184 ----VDQIprAAKGTVEKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQR--FAIAMCCVQKAD----VYMFDE 253
Cdd:PRK13548 89 fpftVEEV--VAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRvqLARVLAQLWEPDgpprWLLLDE 166
|
170 180 190
....*....|....*....|....*....|....*
gi 17555800 254 PSSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDL 287
Cdd:PRK13548 167 PTSALDLAHQHHVLRLARQLAHERGLaVIVVLHDL 201
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
110-287 |
1.82e-15 |
|
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: 76.78 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 110 TPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQkeqewttiinhFRGSELQNyFTRILEDTLKCVIKPQYVDQIPR 189
Cdd:TIGR03873 23 TAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVD-----------LAGVDLHG-LSRRARARRVALVEQDSDTAVPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 190 AAKGTVEknLTR-----------KHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYL 258
Cdd:TIGR03873 91 TVRDVVA--LGRiphrslwagdsPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHL 168
|
170 180
....*....|....*....|....*....
gi 17555800 259 DVKQRLKAAAIIRERVSDTNYVVVVEHDL 287
Cdd:TIGR03873 169 DVRAQLETLALVRELAATGVTVVAALHDL 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
371-545 |
1.94e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.96 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 371 LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKP-EDENTELPHVSISYKPQKIS-PKS-ETTVR------------ 435
Cdd:NF040873 13 LTIPAG-----SLTAVVGPNGSGKSTLLKVLAGVLRPtSGTVRRAGGARVAYVPQRSEvPDSlPLTVRdlvamgrwarrg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 436 -FMLHDKiqnmyEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVI 514
Cdd:NF040873 88 lWRRLTR-----DDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALL 162
|
170 180 190
....*....|....*....|....*....|.
gi 17555800 515 KRfIMHAKKTAFVVEHDFIMATyLADRVVVF 545
Cdd:NF040873 163 AE-EHARGATVVVVTHDLELVR-RADPCVLL 191
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
366-547 |
3.31e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.96 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSI-SYKPQKIS------PKSET-TVRFM 437
Cdd:PRK13548 18 LDDVSLTLRPG-----EVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSPAELArrravlPQHSSlSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 438 LHDKIQnM--YEHPQFKTDVMNPL--MMEQ-----LLDRNVKELSGGELQRVALALCL------GKTASLYLIDEPSAYL 502
Cdd:PRK13548 93 VEEVVA-MgrAPHGLSRAEDDALVaaALAQvdlahLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17555800 503 DSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:PRK13548 172 DLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
114-292 |
3.39e-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: 74.83 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKP----------NLGNFqKEQEWTTIINH-----FRGSELQNYFTrILEDtlkcV 178
Cdd:cd03255 30 GEFVAIVGPSGSGKSTLLNILGGLDRPtsgevrvdgtDISKL-SEKELAAFRRRhigfvFQSFNLLPDLT-ALEN----V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 179 IKPQYVDQIPRaakgtveknltrKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYL 258
Cdd:cd03255 104 ELPLLLAGVPK------------KERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNL 171
|
170 180 190
....*....|....*....|....*....|....*
gi 17555800 259 DVKQRLKAAAIIRERVSDTNY-VVVVEHDLAVLDY 292
Cdd:cd03255 172 DSETGKEVMELLRELNKEAGTtIVVVTHDPELAEY 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
358-547 |
3.60e-15 |
|
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: 75.41 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 358 KYPSMSKTLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMM-------AGSLKPEDENT-ELPHV----SISYKPQK 425
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEF-----LVLIGPSGSGKTTTMKMInrlieptSGEIFIDGEDIrEQDPVelrrKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 426 ISPKSETTVRfmlhdkiQNM--------YEHPQFKTDVMNPLMM-----EQLLDRNVKELSGGELQRVALALCLGKTASL 492
Cdd:cd03295 84 IGLFPHMTVE-------ENIalvpkllkWPKEKIRERADELLALvgldpAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 493 YLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN 211
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
366-543 |
4.74e-15 |
|
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: 74.19 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMA-------GSLKPEDENTELPHVS---------ISYKPQKISPK 429
Cdd:TIGR03608 14 LDDLNLTIEKGKM-----YAIIGESGSGKSTLLNIIGllekfdsGQVYLNGQETPPLNSKkaskfrrekLGYLFQNFALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 430 SETTVRFMLH----DKIQNMYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSE 505
Cdd:TIGR03608 89 ENETVEENLDlglkYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17555800 506 QRlhaAKVIKRF--IMHAKKTAFVVEHDFIMATyLADRVV 543
Cdd:TIGR03608 169 NR---DEVLDLLleLNDEGKTIIIVTHDPEVAK-QADRVI 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
81-297 |
6.73e-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: 72.82 E-value: 6.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 81 IKIINLpanlanetTHRYSQN------SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewTTI 154
Cdd:cd03230 1 IEVRNL--------SKRYGKKtalddiSLTVEK------GEIYGLLGPNGAGKTTLIKIILGLLKPDSG--------EIK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 155 INhfrGSELQNYFTRILEdtlKCVIKPQYVDQIPRAakgTVEKNLtrkhdndnlnsvidqmelrglldreidQLSGGELQ 234
Cdd:cd03230 59 VL---GKDIKKEPEEVKR---RIGYLPEEPSLYENL---TVRENL---------------------------KLSGGMKQ 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17555800 235 RFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSDFI 297
Cdd:cd03230 103 RLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRV 165
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
371-544 |
7.67e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.80 E-value: 7.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 371 LDVEAGDFS----------DSEIIVMLGENGTGKTTMIKMMAGSLKP---------ED-ENTELPHVS--ISYKPQKISP 428
Cdd:PRK09536 9 LSVEFGDTTvldgvdlsvrEGSLVGLVGPNGAGKTTLLRAINGTLTPtagtvlvagDDvEALSARAASrrVASVPQDTSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 429 KSETTVRfmlhdKIQNMYEHPQF-------KTD------VMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLI 495
Cdd:PRK09536 89 SFEFDVR-----QVVEMGRTPHRsrfdtwtETDraaverAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17555800 496 DEPSAYLDSEQRLHAAKVIKRFImHAKKTAFVVEHDFIMATYLADRVVV 544
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVL 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
366-549 |
1.17e-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: 74.36 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKP-------EDENTELPHVSISYKPQkispksETT----- 433
Cdd:COG1116 27 LDDVSLTVAAG-----EFVALVGPSGCGKSTLLRLIAGLEKPtsgevlvDGKPVTGPGPDRGVVFQ------EPAllpwl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 434 -----VRFMLhdKIQNMyEHPQFKTDVMNPLMM---EQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEP-SAyLDS 504
Cdd:COG1116 96 tvldnVALGL--ELRGV-PKAERRERARELLELvglAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPfGA-LDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17555800 505 EQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEGQP 549
Cdd:COG1116 172 LTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARP 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
368-546 |
1.56e-14 |
|
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: 72.91 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 368 NFHLDVEagdFSDSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYkpqkiSPKSETTVRFMLHDkiQNMYE 447
Cdd:cd03298 14 PMHFDLT---FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA-----APPADRPVSMLFQE--NNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 448 HPQFKTDV---MNP---LMMEQ---------------LLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQ 506
Cdd:cd03298 84 HLTVEQNVglgLSPglkLTAEDrqaievalarvglagLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17555800 507 RLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLD 203
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
116-305 |
1.89e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.89 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 116 VLGLVGTNGIGKSTALKILAGKQKPNLG---------NFQKE------QEWTTIinhFRGSELQNYFTRILED---TLKC 177
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGavlwqgkplDYSKRgllalrQQVATV---FQDPEQQIFYTDIDSDiafSLRN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 178 VikpqyvdqipraakGTVEKNLTRKHDnDNLnSVIDQMELRgllDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSY 257
Cdd:PRK13638 106 L--------------GVPEAEITRRVD-EAL-TLVDAQHFR---HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 258 LDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSDFICCL-------YGVPG 305
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLrqgqiltHGAPG 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
380-544 |
1.96e-14 |
|
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: 72.79 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 380 DSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQKISPK-----------SETTVRFML---------- 438
Cdd:cd03266 30 PGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRlgfvsdstglyDRLTARENLeyfaglyglk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 439 ----HDKIQnmyehpqfktDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDseqrLHAAKVI 514
Cdd:cd03266 110 gdelTARLE----------ELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD----VMATRAL 175
|
170 180 190
....*....|....*....|....*....|...
gi 17555800 515 KRFIMHAK---KTAFVVEHDFIMATYLADRVVV 544
Cdd:cd03266 176 REFIRQLRalgKCILFSTHIMQEVERLCDRVVV 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
366-546 |
2.56e-14 |
|
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: 72.52 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPeDENTelphvsISYKPQKISPKSETTVRFMLHDKI--- 442
Cdd:cd03255 20 LKGVSLSIEKG-----EFVAIVGPSGSGKSTLLNILGGLDRP-TSGE------VRVDGTDISKLSEKELAAFRRRHIgfv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 443 -QNMYEHPQF--KTDVMNPLM---------------------MEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEP 498
Cdd:cd03255 88 fQSFNLLPDLtaLENVELPLLlagvpkkerreraeellervgLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17555800 499 SAYLDSEqrlHAAKVIKRFI-MHAK--KTAFVVEHDFIMATYlADRVVVFE 546
Cdd:cd03255 168 TGNLDSE---TGKEVMELLReLNKEagTTIVVVTHDPELAEY-ADRIIELR 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
356-544 |
4.09e-14 |
|
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: 74.94 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 356 NIKYPSMSKT-LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIK----------MMAGSLKPEDENT-----ELPHVSI 419
Cdd:COG1123 11 SVRYPGGDVPaVDGVSLTIAPG-----ETVALVGESGSGKSTLALalmgllphggRISGEVLLDGRDLlelseALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 420 SYKPQkiSPKS-------ETTVRFMLHDKIQNMYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASL 492
Cdd:COG1123 86 GMVFQ--DPMTqlnpvtvGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17555800 493 YLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVV 544
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVV 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
356-547 |
4.37e-14 |
|
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: 75.18 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 356 NIKYPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPED-----ENTELPHVS-------ISYKP 423
Cdd:COG4988 343 SFSYPGGRPALDGLSLTIPPG-----ERVALVGPSGAGKSTLLNLLLGFLPPYSgsiliNGVDLSDLDpaswrrqIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 424 QkispksettvrfmlhdkiqnmyeHPQ-FKTDVMNPLMM-------EQL-------------------LDRNVKE----L 472
Cdd:COG4988 418 Q-----------------------NPYlFAGTIRENLRLgrpdasdEELeaaleaagldefvaalpdgLDTPLGEggrgL 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 473 SGGELQRVALALCLGKTASLYLIDEPSAYLD--SEQRLHAAkvIKRFimHAKKTAFVVEHDfIMATYLADRVVVFEG 547
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDaeTEAEILQA--LRRL--AKGRTVILITHR-LALLAQADRILVLDD 546
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
358-547 |
4.46e-14 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 71.85 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 358 KYPSMS-KTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPED--------ENTELPHV----SISYKPQ 424
Cdd:cd03245 11 SYPNQEiPALDNVSLTIRAG-----EKVAIIGRVGSGKSTLLKLLAGLYKPTSgsvlldgtDIRQLDPAdlrrNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 425 KISPKSETtvrfmLHDKIqnMYEHPqFKTD--VMNPLMMEQL----------LDRNVKE----LSGGELQRVALALCLGK 488
Cdd:cd03245 86 DVTLFYGT-----LRDNI--TLGAP-LADDerILRAAELAGVtdfvnkhpngLDLQIGErgrgLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17555800 489 TASLYLIDEPSAYLD--SEQRLHAAkvIKRFIMHakKTAFVVEHDFIMATyLADRVVVFEG 547
Cdd:cd03245 158 DPPILLLDEPTSAMDmnSEERLKER--LRQLLGD--KTLIIITHRPSLLD-LVDRIIVMDS 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
383-547 |
5.59e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.97 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 383 IIVMLGENGTGKTTMIKMMAGSLKPED-----ENTELPHVS-------ISYKPQKISPKSETTVRFML------------ 438
Cdd:PRK11231 30 ITALIGPNGCGKSTLLKCFARLLTPQSgtvflGDKPISMLSsrqlarrLALLPQHHLTPEGITVRELVaygrspwlslwg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 439 ----HDKiqnmyehpQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVI 514
Cdd:PRK11231 110 rlsaEDN--------ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLM 181
|
170 180 190
....*....|....*....|....*....|....
gi 17555800 515 KRfiMHAK-KTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:PRK11231 182 RE--LNTQgKTVVTVLHDLNQASRYCDHLVVLAN 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
81-295 |
6.92e-14 |
|
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: 69.91 E-value: 6.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 81 IKIINLpanlanetTHRYSQN------SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQkeqewtti 154
Cdd:cd03229 1 LELKNV--------SKRYGQKtvlndvSLNIEA------GEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL-------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 155 inhFRGSELQ--NYFTRILEDTLKCVIkpqyvdqipraAKGTVEKNLTrkhdndnlnsVIDQMELRglldreidqLSGGE 232
Cdd:cd03229 59 ---IDGEDLTdlEDELPPLRRRIGMVF-----------QDFALFPHLT----------VLENIALG---------LSGGQ 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 233 LQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDLAVLDYLSD 295
Cdd:cd03229 106 QQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGItVVLVTHDLDEAARLAD 169
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
364-544 |
7.37e-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: 71.38 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 364 KTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDEntelphvSISYKPQKISPKSETTVRFMLHdKIQ 443
Cdd:cd03257 19 KALDDVSFSIKKG-----ETLGLVGESGSGKSTLARAILGLLKPTSG-------SIIFDGKDLLKLSRRLRKIRRK-EIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 444 NMYEHPQFktdVMNPLMM-----------------------------------EQLLDRNVKELSGGELQRVALALCLGK 488
Cdd:cd03257 86 MVFQDPMS---SLNPRMTigeqiaeplrihgklskkearkeavllllvgvglpEEVLNRYPHELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17555800 489 TASLYLIDEPSAYLD-SEQRLhaakvIKRFIMHAKK---TAFV-VEHDFIMATYLADRVVV 544
Cdd:cd03257 163 NPKLLIADEPTSALDvSVQAQ-----ILDLLKKLQEelgLTLLfITHDLGVVAKIADRVAV 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
362-545 |
7.39e-14 |
|
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: 69.38 E-value: 7.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 362 MSKTLGNFH------LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPeDENTelphvsISYKPQKISPKSettvr 435
Cdd:cd03216 6 ITKRFGGVKaldgvsLSVRRG-----EVHALLGENGAGKSTLMKILSGLYKP-DSGE------ILVDGKEVSFAS----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 436 fmlhdkiqnmyehpqfktdvmnPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIK 515
Cdd:cd03216 69 ----------------------PRDARRAGIAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIR 126
|
170 180 190
....*....|....*....|....*....|...
gi 17555800 516 RFimHAKKTAFV-VEHDF--IMAtyLADRVVVF 545
Cdd:cd03216 127 RL--RAQGVAVIfISHRLdeVFE--IADRVTVL 155
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
382-544 |
7.50e-14 |
|
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: 70.86 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 382 EIIVMLGENGTGKTTMIKMMAGSLKPE---------DENTELPHV--SISYKPQKISPKSETTVR--FMLHDKIQNmYEH 448
Cdd:cd03265 27 EIFGLLGPNGAGKTTTIKMLTTLLKPTsgratvaghDVVREPREVrrRIGIVFQDLSVDDELTGWenLYIHARLYG-VPG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 449 PQFKTDVMNPLMMEQLL---DRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTA 525
Cdd:cd03265 106 AERRERIDELLDFVGLLeaaDRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTI 185
|
170
....*....|....*....
gi 17555800 526 FVVEHDFIMATYLADRVVV 544
Cdd:cd03265 186 LLTTHYMEEAEQLCDRVAI 204
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
112-300 |
8.40e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 8.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 112 RCGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIinHFRGSELQNYFTRILEDTLKCVikPQ--------Y 183
Cdd:PRK09536 27 REGSLVGLVGPNGAGKTTLLRAINGTLTPTAG---------TV--LVAGDDVEALSARAASRRVASV--PQdtslsfefD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 184 VDQIPRAAKGTVEKNLTRKHDNDN--LNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVK 261
Cdd:PRK09536 94 VRQVVEMGRTPHRSRFDTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 17555800 262 QRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSDFICCL 300
Cdd:PRK09536 174 HQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLL 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
357-546 |
9.02e-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: 9.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 357 IKYPSMSKTLGNFH-LDVEAGDFSDSEIIVMLGENGTGKTTMIKMMAGSLKPED-----ENTELPHVS-----ISYKPQK 425
Cdd:cd03296 3 IEVRNVSKRFGDFVaLDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSgtilfGGEDATDVPvqernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 426 ISPKSETTVR----FMLhdKIQNMYEHP---QFKTDVMNPLMMEQL---LDRNVKELSGGELQRVALALCLGKTASLYLI 495
Cdd:cd03296 83 YALFRHMTVFdnvaFGL--RVKPRSERPpeaEIRAKVHELLKLVQLdwlADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 496 DEPSAYLDSEQRlhaaKVIKRFI--MHAKK--TAFVVEHDFIMATYLADRVVVFE 546
Cdd:cd03296 161 DEPFGALDAKVR----KELRRWLrrLHDELhvTTVFVTHDQEEALEVADRVVVMN 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
358-544 |
9.95e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.81 E-value: 9.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 358 KYPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGslkpedenteLPHVS---ISYKPQKISPKS--ET 432
Cdd:PRK10851 10 KSFGRTQVLNDISLDIPSG-----QMVALLGPSGSGKTTLLRIIAG----------LEHQTsghIRFHGTDVSRLHarDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 433 TVRFMLH-----------DKIQ------------NMYEhpqFKTDVMNPLMMEQL---LDRNVKELSGGELQRVALALCL 486
Cdd:PRK10851 75 KVGFVFQhyalfrhmtvfDNIAfgltvlprrerpNAAA---IKAKVTQLLEMVQLahlADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17555800 487 GKTASLYLIDEPSAYLDSEQRlhaaKVIKRFI--MHA--KKTAFVVEHDFIMATYLADRVVV 544
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVR----KELRRWLrqLHEelKFTSVFVTHDQEEAMEVADRVVV 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
324-547 |
1.00e-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: 74.49 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 324 LEGFIRTENMRFResklsfktseqqedikrtgnikYPSMSK-TLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMA 402
Cdd:COG2274 470 LKGDIELENVSFR----------------------YPGDSPpVLDNISLTIKPG-----ERVAIVGRSGSGKSTLLKLLL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 403 GSLKPED-----ENTELPHVS-------ISYKPQKISPkSETTVR---------------------FMLHDKIQNMyehp 449
Cdd:COG2274 523 GLYEPTSgriliDGIDLRQIDpaslrrqIGVVLQDVFL-FSGTIRenitlgdpdatdeeiieaarlAGLHDFIEAL---- 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 450 qfktdvmnPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLD--SEQRLHAAkvIKRFImhAKKTAFV 527
Cdd:COG2274 598 --------PMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDaeTEAIILEN--LRRLL--KGRTVII 665
|
250 260
....*....|....*....|.
gi 17555800 528 VEHDfiMAT-YLADRVVVFEG 547
Cdd:COG2274 666 IAHR--LSTiRLADRIIVLDK 684
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
364-507 |
1.97e-13 |
|
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: 69.53 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 364 KTLGNFHLDVEAGdfsdseIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVS-----------ISYKPQKISPKSET 432
Cdd:cd03264 14 RALDGVSLTLGPG------MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvlkqpqklrrrIGYLPQEFGVYPNF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 433 TVRFMLhDKIQNMYEHPQFKTD-----VMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQR 507
Cdd:cd03264 88 TVREFL-DYIAWLKGIPSKEVKarvdeVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEER 166
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
117-547 |
2.03e-13 |
|
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: 73.05 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 117 LGLVGTNGIGKSTALKILAGKQKPNLGN--FQK-------EQE------WTTIINHFRG-SELQNYFTRILEDTLKCVIK 180
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKDFNGEarPQPgikvgylPQEpqldptKTVRENVEEGvAEIKDALDRFNEISAKYAEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 181 PQYVDQIprAAKGTVEKNLTRKHDNDNLNSVIDQ-ME-LR---GllDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPS 255
Cdd:TIGR03719 114 DADFDKL--AAEQAELQEIIDAADAWDLDSQLEIaMDaLRcppW--DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 256 SYLD------VKQRLKaaaiirervsdtNY---VVVVEHDLAVLDYLSDFICCL---YGVP--GVYGV------------ 309
Cdd:TIGR03719 190 NHLDaesvawLERHLQ------------EYpgtVVAVTHDRYFLDNVAGWILELdrgRGIPweGNYSSwleqkqkrleqe 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 310 VTLPSGVREGINMFLEgFIRTeNMRFRESK----------LSFKTSEQQEDIK--------RTGN--IKYPSMSKTLGNf 369
Cdd:TIGR03719 258 EKEESARQKTLKRELE-WVRQ-SPKGRQAKskarlaryeeLLSQEFQKRNETAeiyippgpRLGDkvIEAENLTKAFGD- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 370 HLDVEAGDFS--DSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTEL-PHVSISYKPQKispksettvRFMLHDKiQNMY 446
Cdd:TIGR03719 335 KLLIDDLSFKlpPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQS---------RDALDPN-KTVW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 447 EHPQFKTDVMN----PLMMEQLLDR----------NVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSE--QRLHA 510
Cdd:TIGR03719 405 EEISGGLDIIKlgkrEIPSRAYVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVEtlRALEE 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 17555800 511 AkvikrfIMHAKKTAFVVEHD--FI--MATY-LA----DRVVVFEG 547
Cdd:TIGR03719 485 A------LLNFAGCAVVISHDrwFLdrIATHiLAfegdSHVEWFEG 524
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
102-300 |
2.16e-13 |
|
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: 68.56 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTI-INhfrGSELQNYFTRILEDTLKcvik 180
Cdd:cd03228 22 SLTIKP------GEKVAIVGPSGSGKSTLLKLLLRLYDPTSG---------EIlID---GVDLRDLDLESLRKNIA---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 181 pqYVDQIPRAAKGTVEKNLtrkhdndnlnsvidqmelrglldreidqLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDV 260
Cdd:cd03228 80 --YVPQDPFLFSGTIRENI----------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17555800 261 kqrlKAAAIIRE---RVSDTNYVVVVEHDLAVLDyLSDFICCL 300
Cdd:cd03228 130 ----ETEALILEalrALAKGKTVIVIAHRLSTIR-DADRIIVL 167
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
368-547 |
2.17e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.98 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 368 NFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAG-----------------SLKPEDENTEL--------PHVSIS-- 420
Cdd:PRK11000 21 DINLDIHEGEF-----VVFVGPSGCGKSTLLRMIAGleditsgdlfigekrmnDVPPAERGVGMvfqsyalyPHLSVAen 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 421 ----YKPQKISpKSEttvrfmlhdkIQNMYEHpqfktdVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLID 496
Cdd:PRK11000 96 msfgLKLAGAK-KEE----------INQRVNQ------VAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17555800 497 EPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA 209
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
98-260 |
2.28e-13 |
|
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: 69.06 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 98 YSQNSFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQewtTIINHFRGSELQNYFTRILEDTLKC 177
Cdd:cd03231 16 FSGLSFTLAA------GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---GPLDFQRDSIARGLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 178 VIkpqyvdqipraakgTVEKNLT---RKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEP 254
Cdd:cd03231 87 TL--------------SVLENLRfwhADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
....*.
gi 17555800 255 SSYLDV 260
Cdd:cd03231 153 TTALDK 158
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
81-300 |
2.77e-13 |
|
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: 69.67 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 81 IKIINLpanlanetTHRYSQN-------SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtT 153
Cdd:COG1122 1 IELENL--------SFSYPGGtpalddvSLSIEK------GEFVAIIGPNGSGKSTLLRLLNGLLKPTSG---------E 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 154 IInhFRGSElqnyftrILEDTLKCVIK-----PQYVD-QIpraAKGTVE-------KNLTRKHDN--DNLNSVIDQMELR 218
Cdd:COG1122 58 VL--VDGKD-------ITKKNLRELRRkvglvFQNPDdQL---FAPTVEedvafgpENLGLPREEirERVEEALELVGLE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 219 GLLDREIDQLSGGELQRFAIA----MccvqKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLS 294
Cdd:COG1122 126 HLADRPPHELSGGQKQRVAIAgvlaM----EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELA 201
|
....*.
gi 17555800 295 DFICCL 300
Cdd:COG1122 202 DRVIVL 207
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
357-545 |
3.05e-13 |
|
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: 69.57 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 357 IKYPSMSKTLGNFH------LDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSI----------- 419
Cdd:cd03300 1 IELENVSKFYGGFValdgvsLDIKEGEF-----FTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDItnlpphkrpvn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 420 ----SYK-------------PQKISPKSETTVRfmlhDKIQNMYEHPQfktdvmnplmMEQLLDRNVKELSGGELQRVAL 482
Cdd:cd03300 76 tvfqNYAlfphltvfeniafGLRLKKLPKAEIK----ERVAEALDLVQ----------LEGYANRKPSQLSGGQQQRVAI 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 483 ALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRfIMHAKKTAFV-VEHDFIMATYLADRVVVF 545
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLKLRKDMQLELKR-LQKELGITFVfVTHDQEEALTMSDRIAVM 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
114-272 |
3.69e-13 |
|
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: 68.54 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewTTIINHFRGSELQNYFTRILedtlkcvikpQYVDQIPrAAKG 193
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDSG--------EVRWNGTPLAEQRDEPHENI----------LYLGHLP-GLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 --TVEKNLT------RKHDNDNLNSvIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLK 265
Cdd:TIGR01189 87 elSALENLHfwaaihGGAQRTIEDA-LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
....*..
gi 17555800 266 AAAIIRE 272
Cdd:TIGR01189 166 LAGLLRA 172
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
366-549 |
4.49e-13 |
|
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: 69.07 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSIsykpQKISPKSETTVR------FM-- 437
Cdd:cd03261 16 LKGVDLDVRRG-----EILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDI----SGLSEAELYRLRrrmgmlFQsg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 438 -LHDKI---QN----MYEHPQFKTDVMNPLMMEQL--------LDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAY 501
Cdd:cd03261 87 aLFDSLtvfENvafpLREHTRLSEEEIREIVLEKLeavglrgaEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 502 LDSeqrlHAAKVIKRFIMHAKK----TAFVVEHDFIMATYLADRV-------VVFEGQP 549
Cdd:cd03261 167 LDP----IASGVIDDLIRSLKKelglTSIMVTHDLDTAFAIADRIavlydgkIVAEGTP 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
366-547 |
1.20e-12 |
|
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: 67.91 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEdentelpHVSISYKPQKISPKSE----TTVRFMLhdk 441
Cdd:COG1124 21 LKDVSLEVAPG-----ESFGLVGESGSGKSTLLRALAGLERPW-------SGEVTFDGRPVTRRRRkafrRRVQMVF--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 442 iQNMYE--HPQFKTD--VMNPL--------------MMEQ------LLDRNVKELSGGELQRVALALCLGKTASLYLIDE 497
Cdd:COG1124 86 -QDPYAslHPRHTVDriLAEPLrihglpdreeriaeLLEQvglppsFLDRYPHQLSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17555800 498 PSAYLDSEQRLHAAKVIKRfIMHAKKTAFV-VEHDFIMATYLADRVVVFEG 547
Cdd:COG1124 165 PTSALDVSVQAEILNLLKD-LREERGLTYLfVSHDLAVVAHLCDRVAVMQN 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
102-291 |
1.37e-12 |
|
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: 65.55 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQewttiinhfrgselqnyftriledtlkcVIKP 181
Cdd:cd03221 20 SLTINP------GDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------------------------TVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVDQipraakgtveknltrkhdndnlnsvidqmelrglldreidqLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVK 261
Cdd:cd03221 66 GYFEQ-----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190
....*....|....*....|....*....|
gi 17555800 262 QRlkaAAIIRERVSDTNYVVVVEHDLAVLD 291
Cdd:cd03221 105 SI---EALEEALKEYPGTVILVSHDRYFLD 131
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
356-546 |
1.54e-12 |
|
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: 66.18 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 356 NIKYPSMSKT-LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISykpqkispKSETTV 434
Cdd:cd03247 7 SFSYPEQEQQvLKNLSLELKQG-----EKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS--------DLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 435 RfmlhDKIQNMYEHPQ-FKTDVMNplmmeqlldrNV-KELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLhaaK 512
Cdd:cd03247 74 S----SLISVLNQRPYlFDTTLRN----------NLgRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER---Q 136
|
170 180 190
....*....|....*....|....*....|....*
gi 17555800 513 VIKRFIMHAK-KTAFVVEHDFIMATYlADRVVVFE 546
Cdd:cd03247 137 LLSLIFEVLKdKTLIWITHHLTGIEH-MDKILFLE 170
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
377-544 |
1.99e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 68.72 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 377 DFSDSEIIVMLGENGTGKTTMIKMMAG-----------------SLKPED-------ENTEL-PHVS----ISY--KPQK 425
Cdd:PRK11650 26 DVADGEFIVLVGPSGCGKSTLLRMVAGleritsgeiwiggrvvnELEPADrdiamvfQNYALyPHMSvrenMAYglKIRG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 426 IsPKSETTVRFMLHDKIqnmyehpqfktdvmnpLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSE 505
Cdd:PRK11650 106 M-PKAEIEERVAEAARI----------------LELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17555800 506 QRLHAAKVIKRfiMHA--KKTAFVVEHDFIMATYLADRVVV 544
Cdd:PRK11650 169 LRVQMRLEIQR--LHRrlKTTSLYVTHDQVEAMTLADRVVV 207
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
114-263 |
2.49e-12 |
|
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: 66.88 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGN-FQKEQEWTTIINHFRGSEL--QNY--FTRIledtlkcvikpqyvdqip 188
Cdd:cd03300 26 GEFFTLLGPSGCGKTTLLRLIAGFETPTSGEiLLDGKDITNLPPHKRPVNTvfQNYalFPHL------------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 189 raakgTVEKNL-----TRKHDNDNLNS----VIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLD 259
Cdd:cd03300 88 -----TVFENIafglrLKKLPKAEIKErvaeALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
....
gi 17555800 260 VKQR 263
Cdd:cd03300 163 LKLR 166
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
366-523 |
2.54e-12 |
|
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: 66.35 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPE-----------DENTELPHVSISYKPQKISPKSETTV 434
Cdd:COG4133 18 FSGLSFTLAAG-----EALALTGPNGSGKTTLLRILAGLLPPSagevlwngepiRDAREDYRRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 435 R--FMLHDKIQNMYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRlhaAK 512
Cdd:COG4133 93 RenLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV---AL 169
|
170
....*....|.
gi 17555800 513 VIKRFIMHAKK 523
Cdd:COG4133 170 LAELIAAHLAR 180
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
114-292 |
2.70e-12 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 66.61 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQ---------KEQEWTtiinHFRGSEL----QNYFtriLEDTLkcvik 180
Cdd:COG1136 34 GEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdisslSERELA----RLRRRHIgfvfQFFN---LLPEL----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 181 pqyvdqipraakgTVEKN---------LTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMF 251
Cdd:COG1136 102 -------------TALENvalplllagVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17555800 252 DEPSSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDLAVLDY 292
Cdd:COG1136 169 DEPTGNLDSKTGEEVLELLRELNRELGTtIVMVTHDPELAAR 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
90-272 |
4.97e-12 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 65.85 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 90 LANETTHRYSQNSFKLHRLP----TPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNfqkeqewttiinhfrgselqn 165
Cdd:cd03266 3 TADALTKRFRDVKKTVQAVDgvsfTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGF--------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 166 yftrILEDTLKCVIKPQYVDQ---IPRAAKG-----TVEKN---------LTRKHDNDNLNSVIDQMELRGLLDREIDQL 228
Cdd:cd03266 62 ----ATVDGFDVVKEPAEARRrlgFVSDSTGlydrlTARENleyfaglygLKGDELTARLEELADRLGMEELLDRRVGGF 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17555800 229 SGGELQRFAIAMCCVQKADVYMFDEPSSYLDVkqrlKAAAIIRE 272
Cdd:cd03266 138 STGMRQKVAIARALVHDPPVLLLDEPTTGLDV----MATRALRE 177
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
102-288 |
5.24e-12 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 65.63 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIINHFR-------GSELQNYFTRILEDT 174
Cdd:cd03220 42 SFEVPR------GERIGLIGRNGAGKSTLLRLLAGIYPPDSG---------TVTVRGRvssllglGGGFNPELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 175 LKCVIkpqyvdqipraakgtveKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQR--FAIAMCcvQKADVYMFD 252
Cdd:cd03220 107 LNGRL-----------------LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARlaFAIATA--LEPDILLID 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 17555800 253 EPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLA 288
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS 203
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
359-550 |
5.72e-12 |
|
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: 66.05 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 359 YPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPeDENTelphVSIS-YKPQKISPKSETTVR-- 435
Cdd:cd03256 10 YPNGKKALKDVSLSINPG-----EFVALIGPSGAGKSTLLRCLNGLVEP-TSGS----VLIDgTDINKLKGKALRQLRrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 436 ----FMLHDKIQNMY-----------EHPQFKT--------DVMNPLmmeQLLDR---------NVKELSGGELQRVALA 483
Cdd:cd03256 80 igmiFQQFNLIERLSvlenvlsgrlgRRSTWRSlfglfpkeEKQRAL---AALERvglldkayqRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 484 LCLGKTASLYLIDEPSAYLD---SEQRLHaakVIKRFIMHAKKTAFVVEHDFIMATYLADRVV-------VFEGQPS 550
Cdd:cd03256 157 RALMQQPKLILADEPVASLDpasSRQVMD---LLKRINREEGITVIVSLHQVDLAREYADRIVglkdgriVFDGPPA 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
114-313 |
6.13e-12 |
|
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: 65.57 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIINHFRGSELQNY----FTRILEDTLkcvikpqyvdqIPR 189
Cdd:cd03293 30 GEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQQDallpWLTVLDNVA-----------LGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 190 AAKGtveknLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAI 269
Cdd:cd03293 99 ELQG-----VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17555800 270 IRERVSDTNY-VVVVEHDL--AVldYLSDFICCLYGVPG-VYGVVTLP 313
Cdd:cd03293 174 LLDIWRETGKtVLLVTHDIdeAV--FLADRVVVLSARPGrIVAEVEVD 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
114-286 |
6.44e-12 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 65.35 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEwttIINHFRGSE------LQNYftriledtlkcVIKPQYvdqi 187
Cdd:cd03301 26 GEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR---DVTDLPPKDrdiamvFQNY-----------ALYPHM---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 188 praakgTVEKNLT-----RKHDNDNLN----SVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYL 258
Cdd:cd03301 88 ------TVYDNIAfglklRKVPKDEIDervrEVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190
....*....|....*....|....*....|.
gi 17555800 259 DVKQRLKAAAIIR---ERVSDTnyVVVVEHD 286
Cdd:cd03301 162 DAKLRVQMRAELKrlqQRLGTT--TIYVTHD 190
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
358-553 |
7.58e-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: 65.22 E-value: 7.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 358 KYPSMSKT-LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKP---------EDENTELPHV--SISYKPQK 425
Cdd:cd03263 9 TYKKGTKPaVDDLSLNVYKG-----EIFGLLGHNGAGKTTTLKMLTGELRPtsgtayingYSIRTDRKAArqSLGYCPQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 426 ISPKSETTVR--FMLHDKIQNMYEHPQFK--TDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAY 501
Cdd:cd03263 84 DALFDELTVRehLRFYARLKGLPKSEIKEevELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 502 LDSeqrlhaakVIKRFI------MHAKKTAFVVEHDFIMATYLADRVVVF-EGQpsVKC 553
Cdd:cd03263 164 LDP--------ASRRAIwdlileVRKGRSIILTTHSMDEAEALCDRIAIMsDGK--LRC 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
116-287 |
9.22e-12 |
|
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: 64.52 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 116 VLGLVGTNGIGKSTALKILAGKQKPNLGNF---------QKE----------QEWTtIINHFRGSELQNYFTRiledtLK 176
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPSSGTIridgqdvlkQPQklrrrigylpQEFG-VYPNFTVREFLDYIAW-----LK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 177 CVIKPQYVDQIPRAakgtveknltrkhdndnlnsvidqMELRGLLDRE---IDQLSGGELQRFAIAMCCVQKADVYMFDE 253
Cdd:cd03264 101 GIPSKEVKARVDEV------------------------LELVNLGDRAkkkIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190
....*....|....*....|....*....|....
gi 17555800 254 PSSYLDVKQRLKAAAIIRErVSDTNYVVVVEHDL 287
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSE-LGEDRIVILSTHIV 189
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
91-295 |
1.05e-11 |
|
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: 65.60 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 91 ANETTHRYSQNSF--KLHRLP-------TPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQkeqewttiinhFRG- 160
Cdd:TIGR02769 5 VRDVTHTYRTGGLfgAKQRAPvltnvslSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVS-----------FRGq 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 161 --SELQNYFTRILEDTLKCVIKPQYVDQIPRAAKGTV----EKNLTRKHDNDNLNSVIDQMELRGL----LDREIDQLSG 230
Cdd:TIGR02769 74 dlYQLDRKQRRAFRRDVQLVFQDSPSAVNPRMTVRQIigepLRHLTSLDESEQKARIAELLDMVGLrsedADKLPRQLSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 231 GELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRE--RVSDTNYVVVVeHDLAVLDYLSD 295
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFIT-HDLRLVQSFCQ 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
366-548 |
1.16e-11 |
|
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: 63.39 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISykpqkispksettvRFMLHDKIQNM 445
Cdd:cd03246 18 LRNVSFSIEPGES-----LAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS--------------QWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 446 YEHPQfktDVmnplmmeQLLDRNVKE--LSGGELQRVALALCLGKTASLYLIDEPSAYLDS--EQRLHAAkvIKRFIMhA 521
Cdd:cd03246 79 GYLPQ---DD-------ELFSGSIAEniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVegERALNQA--IAALKA-A 145
|
170 180
....*....|....*....|....*...
gi 17555800 522 KKTAFVVEHDfiMATY-LADRVVVFEGQ 548
Cdd:cd03246 146 GATRIVIAHR--PETLaSADRILVLEDG 171
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
366-552 |
1.19e-11 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 64.79 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPEdentelpHVSISYKPQKIS-PKSETTVRFmlhdkiQN 444
Cdd:TIGR01184 1 LKGVNLTIQQGEF-----ISLIGHSGCGKSTLLNLISGLAQPT-------SGGVILEGKQITePGPDRMVVF------QN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 445 --------MYEHPQFKTDVMNPLM----MEQLLDRNVK-------------ELSGGELQRVALALCLGKTASLYLIDEPS 499
Cdd:TIGR01184 63 ysllpwltVRENIALAVDRVLPDLskseRRAIVEEHIAlvglteaadkrpgQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17555800 500 AYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEGQPSVK 552
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAAN 195
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
359-546 |
1.45e-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: 64.35 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 359 YPSMSKTLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQKISPKSETTVRFML 438
Cdd:cd03292 10 YPNGTAALDGINISISAGEF-----VFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 439 HDKI----QNMYEHPQFKTDVMN----------PLMMEQLLDRNVK-----ELSGGELQRVALALCLGKTASLYLIDEPS 499
Cdd:cd03292 85 QDFRllpdRNVYENVAFALEVTGvppreirkrvPAALELVGLSHKHralpaELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17555800 500 AYLDSEqrlHAAKVIKRF--IMHAKKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:cd03292 165 GNLDPD---TTWEIMNLLkkINKAGTTVVVATHAKELVDTTRHRVIALE 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
114-290 |
1.57e-11 |
|
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: 67.17 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNfqkeqewttI-INhfrGSELQNYFTRILEDTLKcvikpqYVDQIPRAAK 192
Cdd:COG2274 501 GERVAIVGRSGSGKSTLLKLLLGLYEPTSGR---------IlID---GIDLRQIDPASLRRQIG------VVLQDVFLFS 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 193 GTVEKNLT--RKHDND----------NLNSVIDQMELRglLDREI----DQLSGGELQRFAIAMCCVQKADVYMFDEPSS 256
Cdd:COG2274 563 GTIRENITlgDPDATDeeiieaarlaGLHDFIEALPMG--YDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17555800 257 YLD------VKQRLKaaAIIRERvsdTnyVVVVEHDLAVL 290
Cdd:COG2274 641 ALDaeteaiILENLR--RLLKGR---T--VIIIAHRLSTI 673
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
91-295 |
1.80e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.56 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 91 ANETTHRYSQN------SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIINHFRGSELQ 164
Cdd:PRK11701 9 VRGLTKLYGPRkgcrdvSFDLYP------GEVLGIVGESGSGKTTLLNALSARLAPDAG---------EVHYRMRDGQLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 165 NYFT------RILEDTlkcviKPQYVDQIPR-------AAKGTVEKNL----TRKHDNdnlnsvIDQMELRGLLDREID- 226
Cdd:PRK11701 74 DLYAlseaerRRLLRT-----EWGFVHQHPRdglrmqvSAGGNIGERLmavgARHYGD------IRATAGDWLERVEIDa 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 227 --------QLSGGELQRFAIAMCCVQKAD-VYMfDEPSSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDLAVLDYLSD 295
Cdd:PRK11701 143 ariddlptTFSGGMQQRLQIARNLVTHPRlVFM-DEPTGGLDVSVQARLLDLLRGLVRELGLaVVIVTHDLAVARLLAH 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
382-544 |
2.52e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 65.63 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 382 EIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQKISPKS--------------ETTVRFML-HDKIQNMy 446
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINmmfqsyalfphmtvEQNIAFGLkQDKLPKA- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 447 EHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQR----LHAAKVIKRfimhAK 522
Cdd:PRK11607 125 EIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdrmqLEVVDILER----VG 200
|
170 180
....*....|....*....|..
gi 17555800 523 KTAFVVEHDFIMATYLADRVVV 544
Cdd:PRK11607 201 VTCVMVTHDQEEAMTMAGRIAI 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
363-535 |
2.53e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.36 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 363 SKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPH-VSISYKPQKIS--PKSETTV-RFM- 437
Cdd:PRK09544 17 RRVLSDVSLELKPG-----KILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGkLRIGYVPQKLYldTTLPLTVnRFLr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 438 LHDKIQnmyehpqfKTDVMNPLMMEQ---LLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVI 514
Cdd:PRK09544 92 LRPGTK--------KEDILPALKRVQaghLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
|
170 180
....*....|....*....|...
gi 17555800 515 KRFIMHAKKTAFVVEHD--FIMA 535
Cdd:PRK09544 164 DQLRRELDCAVLMVSHDlhLVMA 186
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
114-286 |
2.78e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 65.48 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTI------INH-----------FrgselQNYftrILEDTLk 176
Cdd:COG3839 29 GEFLVLLGPSGCGKSTLLRMIAGLEDPTSG---------EIliggrdVTDlppkdrniamvF-----QSY---ALYPHM- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 177 cvikpqyvdqipraakgTVEKNLT-----RKHDNDNLNSVIDQM----ELRGLLDREIDQLSGGELQRFAIAMCCVQKAD 247
Cdd:COG3839 91 -----------------TVYENIAfplklRKVPKAEIDRRVREAaellGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17555800 248 VYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVV-VEHD 286
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIyVTHD 193
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
114-287 |
2.95e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.24 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWttiINHFRGSEL--------QNYFTRILEDTLKCVIKPQYVD 185
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH---IQHYASKEVarrigllaQNATTPGDITVQELVARGRYPH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 186 QiPRAAKgtveknlTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLK 265
Cdd:PRK10253 110 Q-PLFTR-------WRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
|
170 180
....*....|....*....|...
gi 17555800 266 AAAIIRERVSDTNYVV-VVEHDL 287
Cdd:PRK10253 182 LLELLSELNREKGYTLaAVLHDL 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
369-548 |
2.98e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.83 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 369 FHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPE-------------------------DENTELPHVSISykp 423
Cdd:PRK10771 18 FDLTVERG-----ERVAILGPSGAGKSTLLNLIAGFLTPAsgsltlngqdhtttppsrrpvsmlfQENNLFSHLTVA--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 424 QKIS----P--KSETTVRFMLHDKIQNMYehpqfktdvmnplmMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDE 497
Cdd:PRK10771 90 QNIGlglnPglKLNAAQREKLHAIARQMG--------------IEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17555800 498 PSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADR-VVVFEGQ 548
Cdd:PRK10771 156 PFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRsLVVADGR 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
360-607 |
3.17e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.42 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 360 PSMSKTLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKP---------QKIS--- 427
Cdd:PRK13646 17 PYEHQAIHDVNTEFEQGKY-----YAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyirpvrKRIGmvf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 428 --PKSEttvrfMLHDKIQN--MYEHPQFKTDVMN------PLMMEQLLDRNVKELS-----GGELQRVALALCLGKTASL 492
Cdd:PRK13646 92 qfPESQ-----LFEDTVEReiIFGPKNFKMNLDEvknyahRLLMDLGFSRDVMSQSpfqmsGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 493 YLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVF-EGQPSVKCTackPQSLLEGMNRFLKM 571
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMkEGSIVSQTS---PKELFKDKKKLADW 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 17555800 572 -LDItfrrdqetyrPRINKLDsvKDVDQKKSGQFFFL 607
Cdd:PRK13646 244 hIGL----------PEIVQLQ--YDFEQKYQTKLKDI 268
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
359-574 |
3.31e-11 |
|
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: 65.94 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 359 YPSMSKT-LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEdentelpHVSISYKPQKISPKSETTVRfm 437
Cdd:COG4987 343 YPGAGRPvLDGLSLTLPPG-----ERVAIVGPSGSGKSTLLALLLRFLDPQ-------SGSITLGGVDLRDLDEDDLR-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 438 lhdkiQNMYEHPQ----FKTDVMNPLMM-------EQL-------------------LDRNVKE----LSGGELQRVALA 483
Cdd:COG4987 409 -----RRIAVVPQrphlFDTTLRENLRLarpdatdEELwaalervglgdwlaalpdgLDTWLGEggrrLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 484 LCLGKTASLYLIDEPSAYLDSEQrlhAAKVIKRFIMHAK-KTAFVVEHDFIMATyLADRVVVFE-GQPSVKCTackPQSL 561
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAAT---EQALLADLLEALAgRTVLLITHRLAGLE-RMDRILVLEdGRIVEQGT---HEEL 556
|
250
....*....|...
gi 17555800 562 LEGMNRFLKMLDI 574
Cdd:COG4987 557 LAQNGRYRQLYQR 569
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
368-549 |
4.15e-11 |
|
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: 63.46 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 368 NFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDEntelphvSISYKPQKISPKSETTvRFMLHDKI----- 442
Cdd:COG1127 23 GVSLDVPRG-----EILAIIGGSGSGKSVLLKLIIGLLRPDSG-------EILVDGQDITGLSEKE-LYELRRRIgmlfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 443 -----------QN----MYEHPQFKTDVMNPLMMEQL--------LDRNVKELSGGELQRVALA--LCLgkTASLYLIDE 497
Cdd:COG1127 90 ggalfdsltvfENvafpLREHTDLSEAEIRELVLEKLelvglpgaADKMPSELSGGMRKRVALAraLAL--DPEILLYDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17555800 498 PSAYLDSEqrlhAAKVIKRFIMHAKK----TAFVVEHD----FIMATY---LADRVVVFEGQP 549
Cdd:COG1127 168 PTAGLDPI----TSAVIDELIRELRDelglTSVVVTHDldsaFAIADRvavLADGKIIAEGTP 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
80-287 |
4.91e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.47 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 80 AIKIINLPANLANETTHRYSQNSFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGN---FQKE--QEWTTI 154
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINE------GEYVAILGHNGSGKSTISKILTGLLKPQSGEikiDGITisKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 155 INHFRGSELQNYFTRILEDTLKcvikpqyvDQIpraAKGTVEKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQ 234
Cdd:PRK13632 81 IRKKIGIIFQNPDNQFIGATVE--------DDI---AFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17555800 235 RFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRE-RVSDTNYVVVVEHDL 287
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlRKTRKKTLISITHDM 203
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
368-547 |
5.11e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 368 NFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLK--PEDENTELPHVSISykpqkispkSETTVrfmlhdkIQNM 445
Cdd:COG2401 48 DLNLEIEPG-----EIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG---------REASL-------IDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 446 YEHPQFKtDVMNPLMMEQLLD-----RNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMH 520
Cdd:COG2401 107 GRKGDFK-DAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARR 185
|
170 180
....*....|....*....|....*..
gi 17555800 521 AKKTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:COG2401 186 AGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
20-83 |
7.85e-11 |
|
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: 59.72 E-value: 7.85e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 20 AIVEKDRCKpkNCGLaCKRACPVNrqgkqCIVVEATSTISqISEILCIGCGICVKKCPYDAIKI 83
Cdd:cd10549 73 AEIDEEKCI--GCGL-CVKVCPVD-----AITLEDELEIV-IDKEKCIGCGICAEVCPVNAIKL 127
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
366-545 |
8.71e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.81 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAG-----------------SLKPEDE--NTEL------PHVSI- 419
Cdd:PRK09452 30 ISNLDLTINNGEF-----LTLLGPSGCGKTTVLRLIAGfetpdsgrimldgqditHVPAENRhvNTVFqsyalfPHMTVf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 420 -----SYKPQKIsPKSETTVRfmlhdkiqnmyehpqfktdVMNPLMM---EQLLDRNVKELSGGELQRVALALCLGKTAS 491
Cdd:PRK09452 105 envafGLRMQKT-PAAEITPR-------------------VMEALRMvqlEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17555800 492 LYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVF 545
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
366-549 |
9.50e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 62.57 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISykpqkiSPKSETTVRFMLH------ 439
Cdd:COG4525 23 LQDVSLTIESGEF-----VVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT------GPGADRGVVFQKDallpwl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 440 DKIQNM-----------YEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRL 508
Cdd:COG4525 92 NVLDNVafglrlrgvpkAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTRE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17555800 509 HAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEGQP 549
Cdd:COG4525 172 QMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGP 212
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
366-546 |
1.05e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 61.98 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKP----------------EDENTELPHVSISYKPQK---I 426
Cdd:COG1136 24 LRGVSLSIEAGEF-----VAIVGPSGSGKSTLLNILGGLDRPtsgevlidgqdisslsERELARLRRRHIGFVFQFfnlL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 427 SpksETTVRfmlhdkiQNmyehpqfktdVMNPLM---------------------MEQLLDRNVKELSGGELQRVALALC 485
Cdd:COG1136 99 P---ELTAL-------EN----------VALPLLlagvsrkerrerarellervgLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17555800 486 LGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYlADRVVVFE 546
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLR 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
114-287 |
1.48e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 62.02 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIinHFRGSELQNYFTRILEDTLKcvIKPQYVDQIPRAakg 193
Cdd:COG4604 27 GGITALIGPNGAGKSTLLSMISRLLPPDSG---------EV--LVDGLDVATTPSRELAKRLA--ILRQENHINSRL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TVEK------------NLTrKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVK 261
Cdd:COG4604 91 TVRElvafgrfpyskgRLT-AEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMK 169
|
170 180 190
....*....|....*....|....*....|..
gi 17555800 262 QrlkAAAIIR--ERVSD----TnyVVVVEHDL 287
Cdd:COG4604 170 H---SVQMMKllRRLADelgkT--VVIVLHDI 196
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
348-550 |
1.53e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.34 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 348 QEDIKRTGNI--KYPSMSK-TLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISykpq 424
Cdd:PRK13635 2 KEEIIRVEHIsfRYPDAATyALKDVSFSVYEG-----EWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 425 kispksETTVrFMLHDKIQNMYEHP--QF-----KTDV---------------------MNPLMMEQLLDRNVKELSGGE 476
Cdd:PRK13635 73 ------EETV-WDVRRQVGMVFQNPdnQFvgatvQDDVafglenigvpreemvervdqaLRQVGMEDFLNREPHRLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 477 LQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYlADRVVVF-------EGQP 549
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMnkgeileEGTP 224
|
.
gi 17555800 550 S 550
Cdd:PRK13635 225 E 225
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
114-507 |
1.60e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.04 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTiinhfrgsELQNYFTRILE-DTLKCVIK-PQYVDQIPRAA 191
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQL--------AWVNQETPALPqPALEYVIDgDREYRQLEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 192 KGTVEKNltRKHDNDNLNSVIDQME-----------LRGL------LDREIDQLSGGELQRFAIAMCCVQKADVYMFDEP 254
Cdd:PRK10636 99 HDANERN--DGHAIATIHGKLDAIDawtirsraaslLHGLgfsneqLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 255 SSYLDVKqrlkaAAIIRER--VSDTNYVVVVEHDLAVLDYLSDFIC-----CLYGVPGVYGVVTLPSGVR--EGINMF-- 323
Cdd:PRK10636 177 TNHLDLD-----AVIWLEKwlKSYQGTLILISHDRDFLDPIVDKIIhieqqSLFEYTGNYSSFEVQRATRlaQQQAMYes 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 324 -------LEGFIRtenmRFReSKLSfKTSEQQEDIKRTGNIKYPSMSKTLGNFHLD----------------VEAGdFSD 380
Cdd:PRK10636 252 qqervahLQSYID----RFR-AKAT-KAKQAQSRIKMLERMELIAPAHVDNPFHFSfrapeslpnpllkmekVSAG-YGD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 381 SEI-------------IVMLGENGTGKTTMIKMMAGSLKPEDENTELPhvsisyKPQKISPKSETTVRFMLHDkiqnmyE 447
Cdd:PRK10636 325 RIIldsiklnlvpgsrIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------KGIKLGYFAQHQLEFLRAD------E 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 448 HPQFKTDVMNPLMMEQLL-----------DR---NVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQR 507
Cdd:PRK10636 393 SPLQHLARLAPQELEQKLrdylggfgfqgDKvteETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
114-290 |
1.61e-10 |
|
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: 63.84 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewTTIINhfrGSELqnyfTRILEDTLKCVIKpqYVDQIPRAAKG 193
Cdd:TIGR02857 348 GERVALVGPSGAGKSTLLNLLLGFVDPTEG--------SIAVN---GVPL----ADADADSWRDQIA--WVPQHPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TVEKNL---TRKHDNDNLNSVIDQM-------ELRGLLDREIDQ----LSGGELQRFAIAMCCVQKADVYMFDEPSSYLD 259
Cdd:TIGR02857 411 TIAENIrlaRPDASDAEIREALERAgldefvaALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180 190
....*....|....*....|....*....|...
gi 17555800 260 vkqRLKAAAIIR--ERVSDTNYVVVVEHDLAVL 290
Cdd:TIGR02857 491 ---AETEAEVLEalRALAQGRTVLLVTHRLALA 520
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
349-570 |
1.72e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.44 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 349 EDIKRTGNIKYPSMSKTLGNFHLDVEAGDFSdseiiVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISY--KPQKI 426
Cdd:PRK13643 5 EKVNYTYQPNSPFASRALFDIDLEVKKGSYT-----ALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 427 SP-KSETTVRFMLHDkiQNMYEHPQFKTDVMNPL---------------------MMEQLLDRNVKELSGGELQRVALAL 484
Cdd:PRK13643 80 KPvRKKVGVVFQFPE--SQLFEETVLKDVAFGPQnfgipkekaekiaaeklemvgLADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 485 CLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRfIMHAKKTAFVVEHDFIMATYLADRVVVFEGQPSVKCTAckPQSLLEG 564
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT--PSDVFQE 234
|
....*.
gi 17555800 565 MNrFLK 570
Cdd:PRK13643 235 VD-FLK 239
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
359-550 |
1.77e-10 |
|
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: 61.55 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 359 YPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSIsykpQKISPKSETTVR--- 435
Cdd:TIGR02315 11 YPNGKQALKNINLNINPG-----EFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDI----TKLRGKKLRKLRrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 436 ---FMLHDKIQNMY-----------EHPQFKT--------DVMNPLmmeQLLDR---------NVKELSGGELQRVALAL 484
Cdd:TIGR02315 82 gmiFQHYNLIERLTvlenvlhgrlgYKPTWRSllgrfseeDKERAL---SALERvgladkayqRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17555800 485 CLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVV-------VFEGQPS 550
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVglkageiVFDGAPS 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
102-287 |
1.79e-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: 59.75 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIinHFRGSELQNYftriledtlkcvikp 181
Cdd:cd03216 20 SLSVRR------GEVHALLGENGAGKSTLMKILSGLYKPDSG---------EI--LVDGKEVSFA--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 qyvdqIPRAAK----GTVeknltrkHdndnlnsvidqmelrglldreidQLSGGELQRFAIAMCCVQKADVYMFDEPSSY 257
Cdd:cd03216 68 -----SPRDARragiAMV-------Y-----------------------QLSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190
....*....|....*....|....*....|
gi 17555800 258 LDVKQRLKAAAIIRERVSDTNYVVVVEHDL 287
Cdd:cd03216 113 LTPAEVERLFKVIRRLRAQGVAVIFISHRL 142
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
362-547 |
1.86e-10 |
|
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: 61.01 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 362 MSKTLGNFH------LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQKISP-KSETTV 434
Cdd:cd03262 6 LHKSFGDFHvlkgidLTVKKG-----EVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 435 RFmlhdkiQ--NMYEHPQFKTDVMNPLMM-------------EQLLDRnV----------KELSGGELQRVALALCLGKT 489
Cdd:cd03262 81 VF------QqfNLFPHLTVLENITLAPIKvkgmskaeaeeraLELLEK-VgladkadaypAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 490 ASLYLIDEPSAYLDSEQRLHAAKVIKRfIMHAKKTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKD-LAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
361-517 |
1.91e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.49 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 361 SMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENT-------ELPHVSIS----YKPQKISPK 429
Cdd:PRK03695 7 AVSTRLGPLSAEVRAG-----EILHLVGPNGAGKSTLLARMAGLLPGSGSIQfagqpleAWSAAELArhraYLSQQQTPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 430 SETTVRFML----HDKIQNmYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALA-LCL------GKTASLYLIDEP 498
Cdd:PRK03695 82 FAMPVFQYLtlhqPDKTRT-EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAaVVLqvwpdiNPAGQLLLLDEP 160
|
170
....*....|....*....
gi 17555800 499 SAYLDSEQRLHAAKVIKRF 517
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSEL 179
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
339-576 |
2.02e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.06 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 339 KLSFKTSEQQEdikrtgniKYpsmskTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPED-----ENTE 413
Cdd:PRK13650 9 NLTFKYKEDQE--------KY-----TLNDVSFHVKQG-----EWLSIIGHNGSGKSTTVRLIDGLLEAESgqiiiDGDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 414 LPHVSISYKPQKIS-----PKS-------ETTVRFMLHDK---IQNMYEHPQfktDVMNPLMMEQLLDRNVKELSGGELQ 478
Cdd:PRK13650 71 LTEENVWDIRHKIGmvfqnPDNqfvgatvEDDVAFGLENKgipHEEMKERVN---EALELVGMQDFKEREPARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 479 RVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATyLADRVVVF-EGQpsVKCTAcK 557
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMkNGQ--VESTS-T 223
|
250 260
....*....|....*....|
gi 17555800 558 PQSLLEGMNRFLKM-LDITF 576
Cdd:PRK13650 224 PRELFSRGNDLLQLgLDIPF 243
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
15-84 |
2.03e-10 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 56.66 E-value: 2.03e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 15 VPLRIAIVEKDRCKpkNCGLaCKRACPVNrqgkqCIVVEATSTIsQISEILCIGCGICVKKCPYDAIKII 84
Cdd:COG1149 1 VKRKIPVIDEEKCI--GCGL-CVEVCPEG-----AIKLDDGGAP-VVDPDLCTGCGACVGVCPTGAITLE 61
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
114-291 |
2.07e-10 |
|
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: 63.63 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTI------INHFRGSELQNYFTriledtlkcvikpqYVDQI 187
Cdd:COG4987 361 GERVAIVGPSGSGKSTLLALLLRFLDPQSG---------SItlggvdLRDLDEDDLRRRIA--------------VVPQR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 188 PRAAKGTVEKNLT--RKH-DNDNLNSVIDQMELRGLLDREID-----------QLSGGELQRFAIAMCCVQKADVYMFDE 253
Cdd:COG4987 418 PHLFDTTLRENLRlaRPDaTDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDE 497
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17555800 254 PSSYLDvkqRLKAAAI---IRERVSD-TnyVVVVEHDLAVLD 291
Cdd:COG4987 498 PTEGLD---AATEQALladLLEALAGrT--VLLITHRLAGLE 534
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
114-302 |
2.41e-10 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 60.63 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFqkeqewttiinHFRGSELQNYFTRIledtlkcvikpQYVDQ------- 186
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTV-----------KVAGASPGKGWRHI-----------GYVPQrhefawd 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 187 IPRAAKGTVEKNLT---------RKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSY 257
Cdd:TIGR03771 64 FPISVAHTVMSGRTghigwlrrpCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17555800 258 LDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSDFICCLYG 302
Cdd:TIGR03771 144 LDMPTQELLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLLNG 188
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
12-84 |
2.70e-10 |
|
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: 59.19 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 12 ETDVPLRIAIVEKDRC----KPKNCGlACKRACPVnrQGKQcIVVEATSTISQISEILCIGCGICVKKCP---YDAIKII 84
Cdd:cd16373 78 EQKVKMGVAVIDKDRClawqGGTDCG-VCVEACPT--EAIA-IVLEDDVLRPVVDEDKCVGCGLCEYVCPvepPKAIVVE 153
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
114-300 |
3.22e-10 |
|
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: 60.53 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIInhFRGSELQNyftriledtlkcviKPQYVdqipRAAKG 193
Cdd:cd03224 26 GEIVALLGRNGAGKTTLLKTIMGLLPPRSG---------SIR--FDGRDITG--------------LPPHE----RARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 --------------TVEKNLT---RKHDNDNLNSVIDQM-----ELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMF 251
Cdd:cd03224 77 igyvpegrrifpelTVEENLLlgaYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 252 DEPSSYL------DVKQRLKaaAIIRERVSdtnyVVVVEHDL-AVLDyLSDFICCL 300
Cdd:cd03224 157 DEPSEGLapkiveEIFEAIR--ELRDEGVT----ILLVEQNArFALE-IADRAYVL 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
371-550 |
3.28e-10 |
|
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: 60.53 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 371 LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKP---------EDENTELPH----VSISYKPQ--KISPksETTVR 435
Cdd:cd03224 21 LTVPEG-----EIVALLGRNGAGKTTLLKTIMGLLPPrsgsirfdgRDITGLPPHerarAGIGYVPEgrRIFP--ELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 436 fmlhdkiQN--MYEHPQFKTDVmnPLMMEQLLDR--NVKE--------LSGGELQRVALALCLGKTASLYLIDEPSAYLd 503
Cdd:cd03224 94 -------ENllLGAYARRRAKR--KARLERVYELfpRLKErrkqlagtLSGGEQQMLAIARALMSRPKLLLLDEPSEGL- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 504 seqrlhAAKVIK---RFIMHAKK---TAFVVEHDFIMATYLADRV-------VVFEGQPS 550
Cdd:cd03224 164 ------APKIVEeifEAIRELRDegvTILLVEQNARFALEIADRAyvlergrVVLEGTAA 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
114-291 |
3.45e-10 |
|
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: 60.30 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewttiinhfrgselqnyftRILEDTLKC-VIKPQ-------YVD 185
Cdd:cd03245 30 GEKVAIIGRVGSGKSTLLKLLAGLYKPTSG-------------------------SVLLDGTDIrQLDPAdlrrnigYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 186 QIPRAAKGTVEKNLTRKHDNDNLNSVIDQMELRGL----------LDREI----DQLSGGELQRFAIAMCCVQKADVYMF 251
Cdd:cd03245 85 QDVTLFYGTLRDNITLGAPLADDERILRAAELAGVtdfvnkhpngLDLQIgergRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17555800 252 DEPSSYLD------VKQRLKaaaiiRERVSDTnyVVVVEHDLAVLD 291
Cdd:cd03245 165 DEPTSAMDmnseerLKERLR-----QLLGDKT--LIIITHRPSLLD 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
363-547 |
3.60e-10 |
|
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: 62.04 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 363 SKTLGNFHLDVeAGDFSDSEIIVMLGENGTGKTTMIKMMAGSLKPE------------DENTEL---------------- 414
Cdd:COG4148 8 RLRRGGFTLDV-DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDsgrirlggevlqDSARGIflpphrrrigyvfqea 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 415 ---PHVSIS----YKpQKISPKSETTVRFmlhDKIQNMyehpqfktdvmnpLMMEQLLDRNVKELSGGELQRVALALCLG 487
Cdd:COG4148 87 rlfPHLSVRgnllYG-RKRAPRAERRISF---DEVVEL-------------LGIGHLLDRRPATLSGGERQRVAIGRALL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17555800 488 KTASLYLIDEPSAYLDSE---------QRLHaakviKRF---IMHakktafvVEHDFIMATYLADRVVVFEG 547
Cdd:COG4148 150 SSPRLLLMDEPLAALDLArkaeilpylERLR-----DELdipILY-------VSHSLDEVARLADHVVLLEQ 209
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
365-535 |
3.84e-10 |
|
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: 58.91 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 365 TLGNF--HLDVEAGDFSDSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTelpHVSISYKPQKISPKSETTVRFMLHdki 442
Cdd:cd03227 3 VLGRFpsYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSAT---RRRSGVKAGCIVAAVSAELIFTRL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 443 qnmyehpqfktdvmnplmmeqlldrnvkELSGGELQRVALALCLG----KTASLYLIDEPSAYLDSEQRLHAAKVIKRFI 518
Cdd:cd03227 77 ----------------------------QLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHL 128
|
170
....*....|....*..
gi 17555800 519 MHaKKTAFVVEHDFIMA 535
Cdd:cd03227 129 VK-GAQVIVITHLPELA 144
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
102-287 |
5.01e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.80 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQ-------KEQEWTT-----II-----NHFRGSELQ 164
Cdd:PRK13635 27 SFSVYE------GEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmvlsEETVWDVrrqvgMVfqnpdNQFVGATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 165 NYFTRILEDtlkcvikpqyvDQIPRaakgtvEKNLTRKHDndnlnsVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQ 244
Cdd:PRK13635 101 DDVAFGLEN-----------IGVPR------EEMVERVDQ------ALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17555800 245 KADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVV-VEHDL 287
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLsITHDL 201
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
386-547 |
5.26e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.57 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 386 MLGENGTGKTTMIKMMAGSLKP------------EDENTELPHVSISYKPQKISPKSETTVRFML-------HDKIQNMY 446
Cdd:PRK10575 42 LIGHNGSGKSTLLKMLGRHQPPsegeilldaqplESWSSKAFARKVAYLPQQLPAAEGMTVRELVaigrypwHGALGRFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 447 EHPQFKTDVMNPLM-MEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTA 525
Cdd:PRK10575 122 AADREKVEEAISLVgLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTV 201
|
170 180
....*....|....*....|..
gi 17555800 526 FVVEHDFIMATYLADRVVVFEG 547
Cdd:PRK10575 202 IAVLHDINMAARYCDYLVALRG 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
371-550 |
5.49e-10 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 60.07 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 371 LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSIsykpQKISPKSETTVR---FMLHDK------ 441
Cdd:COG3638 24 LEIERG-----EFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDV----TALRGRALRRLRrriGMIFQQfnlvpr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 442 ---IQN-----MYEHPQFKT--------DVMNPL-------MMEQLLDRnVKELSGGELQRVALALCLGKTASLYLIDEP 498
Cdd:COG3638 95 lsvLTNvlagrLGRTSTWRSllglfppeDRERALealervgLADKAYQR-ADQLSGGQQQRVAIARALVQEPKLILADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17555800 499 SAYLD---SEQRLHaakVIKRFIMHAKKTAFVVEHDFIMATYLADRV-------VVFEGQPS 550
Cdd:COG3638 174 VASLDpktARQVMD---LLRRIAREDGITVVVNLHQVDLARRYADRIiglrdgrVVFDGPPA 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
97-297 |
5.59e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 59.43 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 97 RYSQNSFKLHRLP-----TPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQ-KEQEWTTIINHFRGSEL----QNY 166
Cdd:cd03298 2 RLDKIRFSYGEQPmhfdlTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLiNGVDVTAAPPADRPVSMlfqeNNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 167 FTRIledtlkcvikpqyvdqipraakgTVEKNLT---------RKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFA 237
Cdd:cd03298 82 FAHL-----------------------TVEQNVGlglspglklTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 238 IAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDT-NYVVVVEH---DLAVLDYLSDFI 297
Cdd:cd03298 139 LARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkMTVLMVTHqpeDAKRLAQRVVFL 202
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
366-527 |
5.63e-10 |
|
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: 59.20 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKP-EDENTELPHVSISYKPQKISPKSETtvrfmlhdkIQN 444
Cdd:cd03233 23 LKDFSGVVKPG-----EMVLVLGRPGSGCSTLLKALANRTEGnVSVEGDIHYNGIPYKEFAEKYPGEI---------IYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 445 MYEHPQFKTdvmnpLMMEQLLD--------RNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKR 516
Cdd:cd03233 89 SEEDVHFPT-----LTVRETLDfalrckgnEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRT 163
|
170
....*....|.
gi 17555800 517 FIMHAKKTAFV 527
Cdd:cd03233 164 MADVLKTTTFV 174
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
114-285 |
8.17e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.73 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIINHFRGSELQNYFTRI--------LEDTLkcvikpqyvd 185
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAG---------TIKLDGGDIDDPDVAEAChylghrnaMKPAL---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 186 qipraakgTVEKNLT--RKHDNDNLNSV---IDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDV 260
Cdd:PRK13539 89 --------TVAENLEfwAAFLGGEELDIaaaLEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....*.
gi 17555800 261 K-QRLkAAAIIRERVSDTNYVVVVEH 285
Cdd:PRK13539 161 AaVAL-FAELIRAHLAQGGIVIAATH 185
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
465-545 |
9.20e-10 |
|
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: 58.10 E-value: 9.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 465 LDRNVKELSGGELQRVALALCLGKTA--SLYLIDEPSAYLDSEQRLHAAKVIKRFImHAKKTAFVVEHDFIMATYlADRV 542
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLI-DLGNTVILIEHNLDVLSS-ADWI 158
|
...
gi 17555800 543 VVF 545
Cdd:cd03238 159 IDF 161
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
168-297 |
9.29e-10 |
|
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: 58.10 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 168 TRILEDTLKCVIKPQYVDQIPRAAKgtveknltrkhdndNLNSVIDQMEL---RGL----LDREIDQLSGGELQRFAIA- 239
Cdd:cd03238 35 STLVNEGLYASGKARLISFLPKFSR--------------NKLIFIDQLQFlidVGLgyltLGQKLSTLSGGELQRVKLAs 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 240 -MCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYlSDFI 297
Cdd:cd03238 101 eLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWI 158
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
364-531 |
9.75e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.96 E-value: 9.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 364 KTLGNFHLDVEAGDFSdseiiVMLGENGTGKTTMIKMMAGSLKPED-----ENTELPHVSISYKPQKISPKSETTVRF-- 436
Cdd:PRK10247 21 KILNNISFSLRAGEFK-----LITGPSGCGKSTLLKIVASLISPTSgtllfEGEDISTLKPEIYRQQVSYCAQTPTLFgd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 437 MLHDKI----QNMYEHPQ---FKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLH 509
Cdd:PRK10247 96 TVYDNLifpwQIRNQQPDpaiFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHN 175
|
170 180
....*....|....*....|..
gi 17555800 510 AAKVIKRFIMHAKKTAFVVEHD 531
Cdd:PRK10247 176 VNEIIHRYVREQNIAVLWVTHD 197
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
20-93 |
1.01e-09 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 55.12 E-value: 1.01e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 20 AIVEKDRCKpkNCGlACKRACPVNrqgkqCIVVEatSTISQISEILCIGCGICVKKCPYDAIKIINLPANLANE 93
Cdd:COG2768 6 PYVDEEKCI--GCG-ACVKVCPVG-----AISIE--DGKAVIDPEKCIGCGACIEVCPVGAIKIEWEEDEEFQE 69
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
24-83 |
1.04e-09 |
|
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: 54.75 E-value: 1.04e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17555800 24 KDRCKpkNCGLaCKRACPVNrqgkqCIVVEAT--STISQISEILCIGCGICVKKCPYDAIKI 83
Cdd:COG1143 1 EDKCI--GCGL-CVRVCPVD-----AITIEDGepGKVYVIDPDKCIGCGLCVEVCPTGAISM 54
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
114-295 |
1.06e-09 |
|
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: 59.27 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIInhFRGSELQNyftriledtlkcvIKPQ-----YVDQ-- 186
Cdd:cd03299 25 GDYFVILGPTGSGKSVLLETIAGFIKPDSG---------KIL--LNGKDITN-------------LPPEkrdisYVPQny 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 187 --IPRAakgTVEKNLT-----RKHDNDNLNSVIDQM-ELRG---LLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPS 255
Cdd:cd03299 81 alFPHM---TVYKNIAyglkkRKVDKKEIERKVLEIaEMLGidhLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17555800 256 SYLDVKQRLKAAAIIRERVSDTNYVVV-VEHDLAVLDYLSD 295
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALAD 198
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
102-300 |
1.24e-09 |
|
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: 58.45 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGN--FQKEQEWTTIINHF------RG-------SELQNY 166
Cdd:cd03269 20 SFSVEK------GEIFGLLGPNGAGKTTTIRMILGIILPDSGEvlFDGKPLDIAARNRIgylpeeRGlypkmkvIDQLVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 167 FTRIledtlkcvikpqyvdqipraakgtveKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKA 246
Cdd:cd03269 94 LAQL--------------------------KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17555800 247 DVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSDFICCL 300
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
114-289 |
1.31e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.87 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQ---KEQEWTTIINHFRGSEL--------QNY-----FTrILEDTLKC 177
Cdd:COG4161 28 GETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiagHQFDFSQKPSEKAIRLLrqkvgmvfQQYnlwphLT-VMENLIEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 178 VIKPQyvdqipraakgtvekNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSY 257
Cdd:COG4161 107 PCKVL---------------GLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190
....*....|....*....|....*....|...
gi 17555800 258 LDVKQRLKAAAIIRErVSDTNYV-VVVEHDLAV 289
Cdd:COG4161 172 LDPEITAQVVEIIRE-LSQTGITqVIVTHEVEF 203
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
8-89 |
1.35e-09 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 58.97 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 8 IKNNETDVPLRIAIVEKDRCKpkNCGLaCKRACPVNrqgkqCIVVEATSTISQISEILCIGCGICVKKCPYDAIKIINLP 87
Cdd:COG1145 165 EEELKIAIKKAKAVIDAEKCI--GCGL-CVKVCPTG-----AIRLKDGKPQIVVDPDKCIGCGACVKVCPVGAISLEPKE 236
|
..
gi 17555800 88 AN 89
Cdd:COG1145 237 IE 238
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
361-550 |
1.40e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.08 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 361 SMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDE----NTELPHVSI-------SYKPQKISPK 429
Cdd:COG4138 7 AVAGRLGPISAQVNAG-----ELIHLIGPNGAGKSTLLARMAGLLPGQGEillnGRPLSDWSAaelarhrAYLSQQQSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 430 SETTVrF---MLHdkiQNMYEHPQFKTDVMN----PLMMEQLLDRNVKELSGGELQRVALALCL-------GKTASLYLI 495
Cdd:COG4138 82 FAMPV-FqylALH---QPAGASSEAVEQLLAqlaeALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptiNPEGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17555800 496 DEPSAYLDSEQRLHAAKVIKRFImHAKKTAFVVEHDFIMATYLADRV-------VVFEGQPS 550
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVwllkqgkLVASGETA 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
97-287 |
1.45e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 58.61 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 97 RYSQNSFKLHRLPTPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGN-FQKEQEWTTIINHFRG-SEL---QNYFTRIl 171
Cdd:COG3840 8 TYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRiLWNGQDLTALPPAERPvSMLfqeNNLFPHL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 172 edtlkcvikpqyvdqipraakgTVEKN----------LTRKhDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMC 241
Cdd:COG3840 87 ----------------------TVAQNiglglrpglkLTAE-QRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17555800 242 CVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDL 287
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLtVLMVTHDP 190
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
366-546 |
1.47e-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: 58.35 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSlkpEDENTELPHV-SISYKPQKISPKSETTVR--------- 435
Cdd:cd03260 16 LKDISLDIPKG-----EITALIGPSGCGKSTLLRLLNRL---NDLIPGAPDEgEVLLDGKDIYDLDVDVLElrrrvgmvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 436 ---FMLH----------DKIQNMYEHPQFKTDVMNPLMMEQLLDR-----NVKELSGGELQRVALALCLGKTASLYLIDE 497
Cdd:cd03260 88 qkpNPFPgsiydnvaygLRLHGIKLKEELDERVEEALRKAALWDEvkdrlHALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17555800 498 PSAYLDSeqrlHAAKVIKRFIMHAKK--TAFVVEHDFIMATYLADRVVVFE 546
Cdd:cd03260 168 PTSALDP----ISTAKIEELIAELKKeyTIVIVTHNMQQAARVADRTAFLL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
112-286 |
1.47e-09 |
|
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: 58.89 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 112 RCGEVLGLVGTNGIGKSTALKILAGKQKPNLGN-FQKEQEWTTIINHFR--GSELQNY--FTRI-LEDTLKCVIKPQYVD 185
Cdd:cd03296 26 PSGELVALLGPSGSGKTTLLRLIAGLERPDSGTiLFGGEDATDVPVQERnvGFVFQHYalFRHMtVFDNVAFGLRVKPRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 186 QIPRAAKgtveknLTRKhdndnLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLK 265
Cdd:cd03296 106 ERPPEAE------IRAK-----VHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180
....*....|....*....|..
gi 17555800 266 AAAIIRERVSDTNYV-VVVEHD 286
Cdd:cd03296 175 LRRWLRRLHDELHVTtVFVTHD 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
370-503 |
1.54e-09 |
|
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: 58.71 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 370 HLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPE------DEN--TELP-----HVSISYKPQKISPKSETTVRF 436
Cdd:cd03218 20 SLSVKQG-----EIVGLLGPNGAGKTTTFYMIVGLVKPDsgkillDGQdiTKLPmhkraRLGIGYLPQEASIFRKLTVEE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17555800 437 MLHDKIQNMYEHPQFKTDVMNPLM----MEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLD 503
Cdd:cd03218 95 NILAVLEIRGLSKKEREEKLEELLeefhITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
108-272 |
1.63e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 59.73 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 108 LPTPRcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTiinhfrGSELQNyftrilEDTlkCVIKPQYV--- 184
Cdd:PRK11432 27 LTIKQ-GTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT------HRSIQQ------RDI--CMVFQSYAlfp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 185 -----DQIpraAKGTVEKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLD 259
Cdd:PRK11432 92 hmslgENV---GYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170
....*....|...
gi 17555800 260 VKQRLKAAAIIRE 272
Cdd:PRK11432 169 ANLRRSMREKIRE 181
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
350-545 |
1.78e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 350 DIKRTGNIKYPSMSKTLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPEDENTElphvsISYKPQKISPK 429
Cdd:PRK13651 7 NIVKIFNKKLPTELKALDNVSVEINQGEF-----IAIIGQTGSGKTTFIEHLNALLLPDTGTIE-----WIFKDEKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 430 SETTVRFMLHDKIQNMY---------------------EHPQFKT----DVM-NPLMM---------------------E 462
Cdd:PRK13651 77 TKEKEKVLEKLVIQKTRfkkikkikeirrrvgvvfqfaEYQLFEQtiekDIIfGPVSMgvskeeakkraakyielvgldE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 463 QLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRfiMHAK-KTAFVVEHDFIMATYLADR 541
Cdd:PRK13651 157 SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDN--LNKQgKTIILVTHDLDNVLEWTKR 234
|
....
gi 17555800 542 VVVF 545
Cdd:PRK13651 235 TIFF 238
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
366-549 |
1.81e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.56 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEdentelpHVSISYKPQKIS-PKSETTVRFMlHDKI-- 442
Cdd:PRK11248 17 LEDINLTLESG-----ELLVVLGPSGCGKTTLLNLIAGFVPYQ-------HGSITLDGKPVEgPGAERGVVFQ-NEGLlp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 443 -QNMYEHPQF---------------KTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQ 506
Cdd:PRK11248 84 wRNVQDNVAFglqlagvekmqrleiAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17555800 507 RLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEGQP 549
Cdd:PRK11248 164 REQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGP 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
114-301 |
1.82e-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: 58.35 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGkqkpnLGNFQKEQEWTTIInHFRGSELQNYFTRILEdtLKCVIkpQYVDQIPRAAKG 193
Cdd:cd03260 26 GEITALIGPSGCGKSTLLRLLNR-----LNDLIPGAPDEGEV-LLDGKDIYDLDVDVLE--LRRRV--GMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TVEKN------LTRKHDNDNLNSVIDQMELRGLLDREID------QLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVK 261
Cdd:cd03260 96 SIYDNvayglrLHGIKLKEELDERVEEALRKAALWDEVKdrlhalGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17555800 262 QRLKAAAIIRERVSDTNyVVVVEHDLAVLDYLSDFICCLY 301
Cdd:cd03260 176 STAKIEELIAELKKEYT-IVIVTHNMQQAARVADRTAFLL 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
102-285 |
1.94e-09 |
|
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: 58.25 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHrlptPrcGEVLGLVGTNGIGKSTALKILAgkqkpnlgNFQKEQEWTTIINhfrGSELQNYFTRILEDtlkcviKP 181
Cdd:cd03248 34 SFTLH----P--GEVTALVGPSGSGKSTVVALLE--------NFYQPQGGQVLLD---GKPISQYEHKYLHS------KV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVDQIPRAAKGTVEKNL------------TRKHDNDNLNSVIDQMELRglLDREID----QLSGGELQRFAIAMCCVQK 245
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIayglqscsfecvKEAAQKAHAHSFISELASG--YDTEVGekgsQLSGGQKQRVAIARALIRN 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17555800 246 ADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEH 285
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHR 208
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
20-83 |
2.66e-09 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 53.89 E-value: 2.66e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 20 AIVEKDRCKpkNCGlACKRACPVnrqgkqcIVVEATSTISQISEILCIGCGICVKKCPYDAIKI 83
Cdd:COG4231 17 YVIDEDKCT--GCG-ACVKVCPA-------DAIEEGDGKAVIDPDLCIGCGSCVQVCPVDAIKL 70
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
102-301 |
2.90e-09 |
|
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: 57.90 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEwttIINHFRGSELQNYFTRI--------LED 173
Cdd:cd03261 20 DLDVRR------GEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE---DISGLSEAELYRLRRRMgmlfqsgaLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 174 TLkcvikpqyvdqipraakgTVEKNLT---RKHDNDNLNSV-------IDQMELRGLLDREIDQLSGGELQRFAIAMCCV 243
Cdd:cd03261 91 SL------------------TVFENVAfplREHTRLSEEEIreivlekLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 244 QKADVYMFDEPSSYLDVKQRLKAAAIIReRVSDT--NYVVVVEHDLAVLDYLSDFICCLY 301
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIR-SLKKElgLTSIMVTHDLDTAFAIADRIAVLY 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
358-546 |
2.97e-09 |
|
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: 58.21 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 358 KYPSMSK-TLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPEDEntelpHVSISykpqKISPKSETTVRF 436
Cdd:TIGR04520 9 SYPESEKpALKNVSLSIEKGEF-----VAIIGHNGSGKSTLAKLLNGLLLPTSG-----KVTVD----GLDTLDEENLWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 437 mLHDKI----QNmyehP--QF------------------KTDVMNPLM--------MEQLLDRNVKELSGGELQRVALA- 483
Cdd:TIGR04520 75 -IRKKVgmvfQN----PdnQFvgatveddvafglenlgvPREEMRKRVdealklvgMEDFRDREPHLLSGGQKQRVAIAg 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 484 -LCLGKTaslYLI-DEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATyLADRVVVFE 546
Cdd:TIGR04520 150 vLAMRPD---IIIlDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMN 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
356-548 |
3.26e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 356 NIKYPSMSKTLGNFH-LDVEAGDFSDSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQKISP----KS 430
Cdd:PRK13645 11 NVSYTYAKKTPFEFKaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEvkrlRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 431 ETTVRF------MLHDKI---------------QNMYEH-PQFKTDVMNPlmmEQLLDRNVKELSGGELQRVALALCLGK 488
Cdd:PRK13645 91 EIGLVFqfpeyqLFQETIekdiafgpvnlgenkQEAYKKvPELLKLVQLP---EDYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17555800 489 TASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVF-EGQ 548
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMhEGK 228
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
8-83 |
3.32e-09 |
|
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: 55.10 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 8 IKNNETDVPLRIAIVEKDRCKpkNCGlACKRACPVN----RQGKQCIVVEATSTIsqISEILCIGCGICVKKCPYDAIKI 83
Cdd:cd10549 23 IELGPNGAIARGPEIDEDKCV--FCG-ACVEVCPTGaielTPEGKEYVPKEKEAE--IDEEKCIGCGLCVKVCPVDAITL 97
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
366-546 |
3.61e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.77 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPEDE-----NTELPHVsisykpqkispKSETtvRFMLHD 440
Cdd:PRK11247 28 LNQLDLHIPAGQF-----VAVVGRSGCGKSTLLRLLAGLETPSAGellagTAPLAEA-----------REDT--RLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 441 K--------IQN--MYEHPQFKTDVMNPLMMEQLLDRnVKE----LSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQ 506
Cdd:PRK11247 90 ArllpwkkvIDNvgLGLKGQWRDAALQALAAVGLADR-ANEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17555800 507 RLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:PRK11247 169 RIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIE 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
366-546 |
3.63e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 57.72 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMM-------AGSLKPEDEntelpHVSISYKPqkispkSETTVRfML 438
Cdd:COG4161 18 LFDINLECPSG-----ETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGH-----QFDFSQKP------SEKAIR-LL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 439 HDK----------------IQNMYEHP-----------QFKTD-VMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTA 490
Cdd:COG4161 81 RQKvgmvfqqynlwphltvMENLIEAPckvlglskeqaREKAMkLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 491 SLYLIDEPSAYLDSEQRLHAAKVIKRfIMHAKKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRE-LSQTGITQVIVTHEVEFARKVASQVVYME 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
114-286 |
3.66e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.08 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewttiinhfrgselqnyftRILEDTLKCVIKPQYVDQIPRAAKG 193
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGFEQPTAG-------------------------QIMLDGVDLSHVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 -------TVEKN---------LTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSY 257
Cdd:PRK11607 100 yalfphmTVEQNiafglkqdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190
....*....|....*....|....*....|...
gi 17555800 258 LDVKQR----LKAAAIIrERVSDTnyVVVVEHD 286
Cdd:PRK11607 180 LDKKLRdrmqLEVVDIL-ERVGVT--CVMVTHD 209
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
112-259 |
3.74e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.19 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 112 RCGEVLGLVGTNGIGKSTALKILAGKQKPNLGN--FQKEQewttiINHFRGSE---LQNYFTRILEDTLKCVIKPQYVD- 185
Cdd:PRK10908 26 RPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKiwFSGHD-----ITRLKNREvpfLRRQIGMIFQDHHLLMDRTVYDNv 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 186 QIPRAAKGTVEKNLTRKhdndnLNSVIDQMelrGLLDREID---QLSGGELQRFAIAMCCVQKADVYMFDEPSSYLD 259
Cdd:PRK10908 101 AIPLIIAGASGDDIRRR-----VSAALDKV---GLLDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
114-300 |
4.24e-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: 56.17 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQkeqewttiinhFRGSELQNYftrilEDTLKCVIKpqYVDQIPRAAKG 193
Cdd:cd03247 28 GEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-----------LDGVPVSDL-----EKALSSLIS--VLNQRPYLFDT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TVEKNLTRkhdndnlnsvidqmelrglldreidQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRER 273
Cdd:cd03247 90 TLRNNLGR-------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEV 144
|
170 180
....*....|....*....|....*..
gi 17555800 274 VSDTNyVVVVEHDLAVLDYLsDFICCL 300
Cdd:cd03247 145 LKDKT-LIWITHHLTGIEHM-DKILFL 169
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
102-548 |
4.38e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKS-TALKIL-----AG--------------KQKPNLGNFQKEQewttiINHFRGS 161
Cdd:PRK10261 36 SFSLQR------GETLAIVGESGSGKSvTALALMrlleqAGglvqcdkmllrrrsRQVIELSEQSAAQ-----MRHVRGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 162 ELQNYFTRILEDtlkcvIKPQYV--DQIPRAAKgtVEKNLTRKHDNDNLNSVIDQM---ELRGLLDREIDQLSGGELQRF 236
Cdd:PRK10261 105 DMAMIFQEPMTS-----LNPVFTvgEQIAESIR--LHQGASREEAMVEAKRMLDQVripEAQTILSRYPHQLSGGMRQRV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 237 AIAMCCVQKADVYMFDEPSSYLDVK---QRLKAAAIIRERVSDTnyVVVVEHDLAVLDYLSDFICCLYGVPGVygvvtlP 313
Cdd:PRK10261 178 MIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLQKEMSMG--VIFITHDMGVVAEIADRVLVMYQGEAV------E 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 314 SGVREGI---------NMFLEGFIRTENM-------RF----------RESKLSFKTSEQQEDIKRTGNI--KYPSMSKT 365
Cdd:PRK10261 250 TGSVEQIfhapqhpytRALLAAVPQLGAMkgldyprRFplislehpakQEPPIEQDTVVDGEPILQVRNLvtRFPLRSGL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEA-----GDFSDSEIIVMLGENGTGKTT-------MIKMMAGslkpedentelphvSISYKPQKISPKSETT 433
Cdd:PRK10261 330 LNRVTREVHAvekvsFDLWPGETLSLVGESGSGKSTtgrallrLVESQGG--------------EIIFNGQRIDTLSPGK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 434 VRFMLHDkIQNMYEHPQFKTD--------VMNPLMMEQLLD-----------------------RNVKELSGGELQRVAL 482
Cdd:PRK10261 396 LQALRRD-IQFIFQDPYASLDprqtvgdsIMEPLRVHGLLPgkaaaarvawllervgllpehawRYPHEFSGGQRQRICI 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 483 ALCLGKTASLYLIDEPSAYLDSEQRlhaAKVIKRFIMHAKK--TAFV-VEHDFIMATYLADRV-VVFEGQ 548
Cdd:PRK10261 475 ARALALNPKVIIADEAVSALDVSIR---GQIINLLLDLQRDfgIAYLfISHDMAVVERISHRVaVMYLGQ 541
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
110-313 |
4.80e-09 |
|
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: 57.09 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 110 TPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIINHFRGSELQNYFT---RILEDTLKCVikpqyVDQ 186
Cdd:TIGR01184 7 TIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLlpwLTVRENIALA-----VDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 187 IPRAAKGTVEKNLTRKHdndnlnsvIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDvkqrlka 266
Cdd:TIGR01184 82 VLPDLSKSERRAIVEEH--------IALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD------- 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 267 aAIIRERVSDT---------NYVVVVEHDLAVLDYLSDFICCLYGVPGVY--GVVTLP 313
Cdd:TIGR01184 147 -ALTRGNLQEElmqiweehrVTVLMVTHDVDEALLLSDRVVMLTNGPAANigQILEVP 203
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
114-287 |
4.95e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.82 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTI-----INHFRGSELQNyftriledtlkcvikP--QYVDq 186
Cdd:PRK13650 33 GEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenvwdIRHKIGMVFQN---------------PdnQFVG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 187 ipraakGTVEKNLTRKHDNDNL------NSVIDQMELRGLLD---REIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSY 257
Cdd:PRK13650 97 ------ATVEDDVAFGLENKGIpheemkERVNEALELVGMQDfkeREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190
....*....|....*....|....*....|.
gi 17555800 258 LDVKQRLKAAAIIRERVSDTNYVVV-VEHDL 287
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDYQMTVIsITHDL 201
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
377-548 |
7.89e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.55 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 377 DFSDSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYK----PQKISPKSETTVRFM-LHDKIQNMYEHPQ- 450
Cdd:PRK13631 48 TFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKknnhELITNPYSKKIKNFKeLRRRVSMVFQFPEy 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 451 --FKTDVMNPLMM--------------------------EQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYL 502
Cdd:PRK13631 128 qlFKDTIEKDIMFgpvalgvkkseakklakfylnkmgldDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGL 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17555800 503 DSEqrlhAAKVIKRFIMHAK---KTAFVVEHDFIMATYLADRVVVF-EGQ 548
Cdd:PRK13631 208 DPK----GEHEMMQLILDAKannKTVFVITHTMEHVLEVADEVIVMdKGK 253
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
465-543 |
8.24e-09 |
|
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: 56.11 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 465 LDRNVKELSGGELQRVALALCLGK--TASLYLIDEPSAYL---DSEQRLHAAKVIKrfimHAKKTAFVVEHD--FIMAty 537
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLATQIGSglTGVLYVLDEPSIGLhprDNDRLIETLKRLR----DLGNTVLVVEHDedTIRA-- 204
|
....*.
gi 17555800 538 lADRVV 543
Cdd:cd03270 205 -ADHVI 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
348-547 |
8.61e-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: 56.88 E-value: 8.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 348 QEDIKRTGnikypsmsKTLGNFH--LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEdentelpHVSISYKPQK 425
Cdd:cd03294 28 EEILKKTG--------QTVGVNDvsLDVREG-----EIFVIMGLSGSGKSTLLRCINRLIEPT-------SGKVLIDGQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 426 ISPKSETTVRFMLHDKI----QNMYEHPQFK-----------------------TDVMNPLMMEQLLDRNVKELSGGELQ 478
Cdd:cd03294 88 IAAMSRKELRELRRKKIsmvfQSFALLPHRTvlenvafglevqgvpraereeraAEALELVGLEGWEHKYPDELSGGMQQ 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 479 RVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:cd03294 168 RVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKD 236
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
366-549 |
1.01e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDEntelpHVSISYKPQKISPKSettvRFMLH------ 439
Cdd:PRK13543 27 FGPLDFHVDAG-----EALLVQGDNGAGKTTLLRVLAGLLHVESG-----QIQIDGKTATRGDRS----RFMAYlghlpg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 440 -----DKIQNMY-------EHP-QFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEq 506
Cdd:PRK13543 93 lkadlSTLENLHflcglhgRRAkQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17555800 507 rlhAAKVIKRFI---MHAKKTAFVVEHDFIMATYLADRVVVFEGQP 549
Cdd:PRK13543 172 ---GITLVNRMIsahLRGGGAALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
386-546 |
1.15e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 56.73 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 386 MLGENGTGKTTMIKMMAGSLKPEDenteLPHVSISYKPQKISPKSETTVRfmlhDKIQNMYEHP--QFK----------- 452
Cdd:PRK13640 38 LIGHNGSGKSTISKLINGLLLPDD----NPNSKITVDGITLTAKTVWDIR----EKVGIVFQNPdnQFVgatvgddvafg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 453 ---------------TDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRF 517
Cdd:PRK13640 110 lenravprpemikivRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKL 189
|
170 180
....*....|....*....|....*....
gi 17555800 518 IMHAKKTAFVVEHDfIMATYLADRVVVFE 546
Cdd:PRK13640 190 KKKNNLTVISITHD-IDEANMADQVLVLD 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
114-302 |
1.19e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWT------TIINHFRGSELQNY-FTRILEDTlkcVIKPQYvdq 186
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrqalqkNLVAYVPQSEEVDWsFPVLVEDV---VMMGRY--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 187 iprAAKGTVEKnlTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKA 266
Cdd:PRK15056 107 ---GHMGWLRR--AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 17555800 267 AAIIRERVSDTNYVVVVEHDLAVLDYLSDFICCLYG 302
Cdd:PRK15056 182 ISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
21-84 |
1.20e-08 |
|
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: 52.36 E-value: 1.20e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 21 IVEKDRCKpkNCGLaCKRACPVNrqgkqCIVVEATSTIsQISEILCIGCGICVKKCPYDAIKII 84
Cdd:COG1144 26 VVDEDKCI--GCGL-CWIVCPDG-----AIRVDDGKYY-GIDYDYCKGCGICAEVCPVKAIEMV 80
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
102-290 |
1.41e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.86 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIINH---FRGsEL---QN-YFT-RILed 173
Cdd:COG1134 46 SFEVER------GESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELgagFHP-ELtgrENiYLNgRLL-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 174 tlkcvikpqyvdqipraakgtvekNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQR--FAIAMCcvQKADVYMF 251
Cdd:COG1134 117 ------------------------GLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARlaFAVATA--VDPDILLV 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 17555800 252 DEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVL 290
Cdd:COG1134 171 DEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAV 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
359-531 |
1.52e-08 |
|
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: 57.64 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 359 YPSMSKTLGNFHLDVeagdFSDSEIIVmLGENGTGKTTMIKMMAGSLKP-EDENTELPHVSISYKPQKISPKSETTVR-- 435
Cdd:TIGR03719 14 VPPKKEILKDISLSF----FPGAKIGV-LGLNGAGKSTLLRIMAGVDKDfNGEARPQPGIKVGYLPQEPQLDPTKTVRen 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 436 -----------FMLHDKIQNMYEHPqfkTDVMNPLMMEQL-------------LDR----------------NVKELSGG 475
Cdd:TIGR03719 89 veegvaeikdaLDRFNEISAKYAEP---DADFDKLAAEQAelqeiidaadawdLDSqleiamdalrcppwdaDVTKLSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 476 ELQRVALALCLGKTASLYLIDEPSAYLDSEqrlhAAKVIKRFIMHAKKTAFVVEHD 531
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAE----SVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
114-261 |
1.53e-08 |
|
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: 55.65 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGN-FQKEQEwttiINHFRGSELQNYFTRI--------LedtlkcvIKPQYV 184
Cdd:cd03256 27 GEFVALIGPSGAGKSTLLRCLNGLVEPTSGSvLIDGTD----INKLKGKALRQLRRQIgmifqqfnL-------IERLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 185 DQ---IPRAAKGTVEKNLTR---KHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYL 258
Cdd:cd03256 96 LEnvlSGRLGRRSTWRSLFGlfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASL 175
|
...
gi 17555800 259 DVK 261
Cdd:cd03256 176 DPA 178
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
114-287 |
1.60e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 55.62 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAG----------KQKPnlgnfqkeqewttiINHFRGSEL---QNYFtriledtlkcvik 180
Cdd:COG4138 22 GELIHLIGPNGAGKSTLLARMAGllpgqgeillNGRP--------------LSDWSAAELarhRAYL------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 181 PQyvDQIPRAAKGT-------VEKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQ-------KA 246
Cdd:COG4138 75 SQ--QQSPPFAMPVfqylalhQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17555800 247 DVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDL 287
Cdd:COG4138 153 QLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDL 193
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
328-544 |
1.62e-08 |
|
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: 55.42 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 328 IRTENMRFresklSFKTSEQQEDIKRTG----NIKYPSMsKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAG 403
Cdd:cd03267 1 IEVSNLSK-----SYRVYSKEPGLIGSLkslfKRKYREV-EALKGISFTIEKG-----EIVGFIGPNGAGKTTTLKILSG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 404 SLKP-EDENTELPHVSISYKPQ---KIS-------------PKSETtvrFMLHDKIQNMyEHPQFKTDV---MNPLMMEQ 463
Cdd:cd03267 70 LLQPtSGEVRVAGLVPWKRRKKflrRIGvvfgqktqlwwdlPVIDS---FYLLAAIYDL-PPARFKKRLdelSELLDLEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 464 LLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDseqrLHAAKVIKRFIMHAKK----TAFVVEHDFIMATYLA 539
Cdd:cd03267 146 LLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD----VVAQENIRNFLKEYNRergtTVLLTSHYMKDIEALA 221
|
....*
gi 17555800 540 DRVVV 544
Cdd:cd03267 222 RRVLV 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
114-288 |
1.64e-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: 55.23 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGN--------FQKEQEWTTIINHFrGSELQNY--FTR--ILEDtlkCVIKP 181
Cdd:cd03262 26 GEVVVIIGPSGSGKSTLLRCINLLEEPDSGTiiidglklTDDKKNINELRQKV-GMVFQQFnlFPHltVLEN---ITLAP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVDQIPRA-AKGTVEKNLTRkhdndnlnsVidqmelrGLLDRE---IDQLSGGELQRFAIAMCCVQKADVYMFDEPSSY 257
Cdd:cd03262 102 IKVKGMSKAeAEERALELLEK---------V-------GLADKAdayPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190
....*....|....*....|....*....|....
gi 17555800 258 LD---VKQRLKaaaIIRERVSDTNYVVVVEHDLA 288
Cdd:cd03262 166 LDpelVGEVLD---VMKDLAEEGMTMVVVTHEMG 196
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
366-547 |
1.65e-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: 55.97 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENtelphvsISYKPQ---KISPKSETTVRFMLHDKI 442
Cdd:TIGR02769 27 LTNVSLSIEEG-----ETVGLLGRSGCGKSTLARLLLGLEKPAQGT-------VSFRGQdlyQLDRKQRRAFRRDVQLVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 443 QNMYE--HPQFKTD--VMNPL--------------------MME---QLLDRNVKELSGGELQRVALALCLGKTASLYLI 495
Cdd:TIGR02769 95 QDSPSavNPRMTVRqiIGEPLrhltsldeseqkariaelldMVGlrsEDADKLPRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17555800 496 DEPSAYLDSEQRLHAAKVIKRfIMHAKKTAFV-VEHDFIMATYLADRVVVFEG 547
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRK-LQQAFGTAYLfITHDLRLVQSFCQRVAVMDK 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
114-287 |
1.73e-08 |
|
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: 55.42 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQ--KEQEWTTIINHFR------GSELQNYFTRILEDTLKcVIKPQYvD 185
Cdd:cd03267 47 GEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaGLVPWKRRKKFLRrigvvfGQKTQLWWDLPVIDSFY-LLAAIY-D 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 186 QIPRAAKGTVEKnltrkhdndnlnsVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLK 265
Cdd:cd03267 125 LPPARFKKRLDE-------------LSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180
....*....|....*....|...
gi 17555800 266 AAAIIRERVSDTN-YVVVVEHDL 287
Cdd:cd03267 192 IRNFLKEYNRERGtTVLLTSHYM 214
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
359-574 |
1.87e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 55.76 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 359 YPSMSKTLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPED-----------ENTELPH----VSISYKp 423
Cdd:PRK13644 11 YPDGTPALENINLVIKKGEY-----IGIIGKNGSGKSTLALHLNGLLRPQKgkvlvsgidtgDFSKLQGirklVGIVFQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 424 qkiSPKSETTVRFMLHDKI---QNMYEHP-QFKTDVMNPLM---MEQLLDRNVKELSGGELQRVALALCLGKTASLYLID 496
Cdd:PRK13644 85 ---NPETQFVGRTVEEDLAfgpENLCLPPiEIRKRVDRALAeigLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 497 EPSAYLDSEQRLHAAKVIKRfiMHAK-KTAFVVEHDfIMATYLADRV-------VVFEGQP-------SVKCTACKPQSL 561
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKK--LHEKgKTIVYITHN-LEELHDADRIivmdrgkIVLEGEPenvlsdvSLQTLGLTPPSL 238
|
250
....*....|...
gi 17555800 562 LEGMNRfLKMLDI 574
Cdd:PRK13644 239 IELAEN-LKMHGV 250
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
21-84 |
1.95e-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: 53.17 E-value: 1.95e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 21 IVEKDRCKpkNCGlACKRACPVNrqgkqCIVVE---ATSTISQISEILCIGCGICVKKCPYDAIKII 84
Cdd:cd10549 2 KYDPEKCI--GCG-ICVKACPTD-----AIELGpngAIARGPEIDEDKCVFCGACVEVCPTGAIELT 60
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
377-545 |
2.14e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.78 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 377 DFSDSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQKIspksettvrFMLHDKIQNMYEHPQ---FKT 453
Cdd:PRK13638 23 DFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGL---------LALRQQVATVFQDPEqqiFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 454 DV--------MNPLMMEQLLDRNVKE-----------------LSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRL 508
Cdd:PRK13638 94 DIdsdiafslRNLGVPEAEITRRVDEaltlvdaqhfrhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 17555800 509 HAAKVIKRFIMHAKKTAfVVEHDFIMATYLADRVVVF 545
Cdd:PRK13638 174 QMIAIIRRIVAQGNHVI-ISSHDIDLIYEISDAVYVL 209
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
18-91 |
2.37e-08 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 55.71 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 18 RIAIVEKDRCKpkNCGlACKRACPVN----RQGKQCIVVEATS-----TISQISEILCIGCGICVKKCPYDAIKIINlpa 88
Cdd:PRK07118 161 GLPVVDEDKCT--GCG-ACVKACPRNvielIPKSARVFVACNSkdkgkAVKKVCEVGCIGCGKCVKACPAGAITMEN--- 234
|
...
gi 17555800 89 NLA 91
Cdd:PRK07118 235 NLA 237
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
371-522 |
2.39e-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: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 371 LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPE-------DEN-TELP-----HVSISYKPQKISPKSETTVRfm 437
Cdd:TIGR04406 22 LSVKSG-----EIVGLLGPNGAGKTTSFYMIVGLVRPDagkilidGQDiTHLPmheraRLGIGYLPQEASIFRKLTVE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 438 lhDKIQNMYEH-----PQFKTDVMNPLMME----QLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSeqrl 508
Cdd:TIGR04406 95 --ENIMAVLEIrkdldRAEREERLEALLEEfqisHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDP---- 168
|
170
....*....|....
gi 17555800 509 HAAKVIKRFIMHAK 522
Cdd:TIGR04406 169 IAVGDIKKIIKHLK 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
364-528 |
2.80e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.90 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 364 KTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMM-------AGSLKPEDENTEL------PHVSISYKPQKISPKS 430
Cdd:PRK10895 17 RVVEDVSLTVNSG-----EIVGLLGPNGAGKTTTFYMVvgivprdAGNIIIDDEDISLlplharARRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 431 ETTVRFMLHDKIQ-----NMYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSE 505
Cdd:PRK10895 92 RLSVYDNLMAVLQirddlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180
....*....|....*....|...
gi 17555800 506 QRLHaakvIKRFIMHAKKTAFVV 528
Cdd:PRK10895 172 SVID----IKRIIEHLRDSGLGV 190
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
358-557 |
2.88e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.47 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 358 KYPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENtelphVSISYKPQKISPKSETTVRFM 437
Cdd:PRK13639 10 SYPDGTEALKGINFKAEKG-----EMVALLGPNGAGKSTLFLHFNGILKPTSGE-----VLIKGEPIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 438 LHDKIQNMYEH---PQFKTDV----MNPLMMEQLLDRNVKE-----------------LSGGELQRVALALCLGKTASLY 493
Cdd:PRK13639 80 VGIVFQNPDDQlfaPTVEEDVafgpLNLGLSKEEVEKRVKEalkavgmegfenkpphhLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 494 LIDEPSAYLDSeqrLHAAKVIKRFIMHAKK--TAFVVEHDFIMATYLADRVVVFEGQPSVKCTACK 557
Cdd:PRK13639 160 VLDEPTSGLDP---MGASQIMKLLYDLNKEgiTIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
102-260 |
2.93e-08 |
|
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: 56.48 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLhrlptPRcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFqkeqewttiinhfrgselqnyftrILEDTlkcvIKP 181
Cdd:TIGR03719 342 SFKL-----PP-GGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI------------------------EIGET----VKL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVDQIPRA--AKGTVEKNLTRKHDNDNLNSVidQMELRGLLDR----------EIDQLSGGELQRFAIAMCCVQKADVY 249
Cdd:TIGR03719 388 AYVDQSRDAldPNKTVWEEISGGLDIIKLGKR--EIPSRAYVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170
....*....|.
gi 17555800 250 MFDEPSSYLDV 260
Cdd:TIGR03719 466 LLDEPTNDLDV 476
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
114-259 |
3.08e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.59 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFqkeqeWTTIINHFRGSELQ----------NYFTRIledtlkcvikpqy 183
Cdd:PRK10771 25 GERVAILGPSGAGKSTLLNLIAGFLTPASGSL-----TLNGQDHTTTPPSRrpvsmlfqenNLFSHL------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 184 vdqipraakgTVEKN--------LTRKHDN-DNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEP 254
Cdd:PRK10771 87 ----------TVAQNiglglnpgLKLNAAQrEKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
....*
gi 17555800 255 SSYLD 259
Cdd:PRK10771 157 FSALD 161
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
115-295 |
3.24e-08 |
|
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: 55.89 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 115 EVLGLVGTNGIGKSTALKILAGKQKPNLGNFqkeqewttiinHFRGselqnyftRILEDTLKCVIKPQ------YVDQIP 188
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI-----------VLNG--------RTLFDSRKGIFLPPekrrigYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 189 R-----AAKGTVEKNLTR---KHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDV 260
Cdd:TIGR02142 85 RlfphlSVRGNLRYGMKRarpSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 17555800 261 KQRlkaAAIIR--ERVSDTNY--VVVVEHDLAVLDYLSD 295
Cdd:TIGR02142 165 PRK---YEILPylERLHAEFGipILYVSHSLQEVLRLAD 200
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
360-546 |
3.27e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 360 PSMSKTLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPEDEntelphvSISYKPQKISPKSETTVRFMLH 439
Cdd:PRK13641 17 PMEKKGLDNISFELEEGSF-----VALVGHTGSGKSTLMQHFNALLKPSSG-------TITIAGYHITPETGNKNLKKLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 440 DKIQNMYEHPQ---FKTDVMNPLMM--------------------------EQLLDRNVKELSGGELQRVALALCLGKTA 490
Cdd:PRK13641 85 KKVSLVFQFPEaqlFENTVLKDVEFgpknfgfsedeakekalkwlkkvglsEDLISKSPFELSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 491 SLYLIDEPSAYLDSEQRLHAAKVIKRFiMHAKKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLE 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
112-287 |
3.47e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.94 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 112 RCGEVLGLVGTNGIGKSTALKILAGkqkpnLGNFQKEQewttiinHFRGSELQNYFTRIL---EDTLKCVIKP------- 181
Cdd:PRK03695 20 RAGEILHLVGPNGAGKSTLLARMAG-----LLPGSGSI-------QFAGQPLEAWSAAELarhRAYLSQQQTPpfampvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVdQIPRAAKGTVEKnltrkhDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQ-------KADVYMFDEP 254
Cdd:PRK03695 88 QYL-TLHQPDKTRTEA------VASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|...
gi 17555800 255 SSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDL 287
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDL 193
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
112-297 |
3.64e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 112 RCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQ---KEQEWTT----------IINHfrgsELQnyftRILEDTlkcV 178
Cdd:PRK11288 28 RAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILidgQEMRFASttaalaagvaIIYQ----ELH----LVPEMT---V 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 179 IKPQYVDQIPRAAkGTVEKNLTRKHdndnlnsVIDQMELRGLldrEID------QLSGGELQRFAIAMCCVQKADVYMFD 252
Cdd:PRK11288 97 AENLYLGQLPHKG-GIVNRRLLNYE-------AREQLEHLGV---DIDpdtplkYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17555800 253 EPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSDFI 297
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAI 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
360-544 |
3.95e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.05 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 360 PSMSKTLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQKISPksettvrfmLH 439
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEF-----VGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSD---------IR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 440 DKIQNMYEHPQFK-------TDV---------------------MN--PLMMEQLLDRNVKELSGGELQRVALALCLGKT 489
Cdd:PRK13637 83 KKVGLVFQYPEYQlfeetieKDIafgpinlglseeeienrvkraMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 490 ASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVV 544
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIV 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
366-544 |
3.99e-08 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 54.74 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPED-----ENTELPHvsisYKPQKIS------PKSeTTV 434
Cdd:COG4559 17 LDDVSLTLRPG-----ELTAIIGPNGAGKSTLLKLLTGELTPSSgevrlNGRPLAA----WSPWELArrravlPQH-SSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 435 RF--------ML----HDKiqnmyEHPQFKTDVMNplMMEQ-----LLDRNVKELSGGELQRVALA--LC-----LGKTA 490
Cdd:COG4559 87 AFpftveevvALgrapHGS-----SAAQDRQIVRE--ALALvglahLAGRSYQTLSGGEQQRVQLArvLAqlwepVDGGP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17555800 491 SLYLIDEPSAYLDSEQRLHAAKVIKRFiMHAKKTAFVVEHDFIMATYLADRVVV 544
Cdd:COG4559 160 RWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRILL 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
359-505 |
4.05e-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: 56.21 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 359 YPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQKISPKsetTVRFML 438
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPG-----ERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR---RVSVCA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 439 HDKiqnmyeHpQFKTDVMNPL-----------MMEQL---------------LDRNVKE----LSGGELQRVALALCLGK 488
Cdd:TIGR02868 416 QDA------H-LFDTTVRENLrlarpdatdeeLWAALervgladwlralpdgLDTVLGEggarLSGGERQRLALARALLA 488
|
170
....*....|....*..
gi 17555800 489 TASLYLIDEPSAYLDSE 505
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAE 505
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
357-563 |
4.11e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.61 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 357 IKYPSMSKTLGNfHLDVEAGDFSDS--EIIVMLGENGTGKTTMIKMMAGSLKPEDEN-----------TELPHVSISYKP 423
Cdd:PRK13536 42 IDLAGVSKSYGD-KAVVNGLSFTVAsgECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlgvpvparARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 424 QKISPKSETTVR--FMLHDKIQNMyeHPQFKTDVMNPLM----MEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDE 497
Cdd:PRK13536 121 QFDNLDLEFTVRenLLVFGRYFGM--STREIEAVIPSLLefarLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 498 PSAYLDSeqrlHAAKVI---KRFIMHAKKTAFVVEHDFIMATYLADRVVVFEGqpSVKCTACKPQSLLE 563
Cdd:PRK13536 199 PTTGLDP----HARHLIwerLRSLLARGKTILLTTHFMEEAERLCDRLCVLEA--GRKIAEGRPHALID 261
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
363-546 |
4.13e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.64 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 363 SKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMM-------AGSLKPEDENTELPhvsisykpQKISPKSETTVR 435
Cdd:PRK11124 15 HQALFDITLDCPQG-----ETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFDFS--------KTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 436 F---MLHDK---------IQNMYEHP---------QFKTDVM---NPLMMEQLLDRNVKELSGGELQRVALALCLGKTAS 491
Cdd:PRK11124 82 RnvgMVFQQynlwphltvQQNLIEAPcrvlglskdQALARAEkllERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 492 LYLIDEPSAYLDSEQRLHAAKVIKRfIMHAKKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYME 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
359-545 |
4.18e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.78 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 359 YPSMSKTLGNFHLDveagdFSDSEIIVMLGENGTGKTTMIKMM--AGSLKPEDENTElphvSISYKPQKI-SPKSETTvr 435
Cdd:PRK14239 14 YYNKKKALNSVSLD-----FYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITG----SIVYNGHNIySPRTDTV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 436 fMLHDKIQNMYEHPqfktdvmNPLMM-----------------EQLLDRNVKE---------------------LSGGEL 477
Cdd:PRK14239 83 -DLRKEIGMVFQQP-------NPFPMsiyenvvyglrlkgikdKQVLDEAVEKslkgasiwdevkdrlhdsalgLSGGQQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 478 QRVALALCLGKTASLYLIDEPSAYLDSeqrLHAAKVIKR-FIMHAKKTAFVVEHDFIMATYLADRVVVF 545
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDP---ISAGKIEETlLGLKDDYTMLLVTRSMQQASRISDRTGFF 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
114-289 |
4.33e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLG---------NFQKEQEWTTIINHFR--GSELQNY-----FTrILEDTLKC 177
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlniagnhfDFSKTPSDKAIRELRRnvGMVFQQYnlwphLT-VQQNLIEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 178 VIKPQYVDQipRAAKGTVEKNLTRkhdndnlnsvidqMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSY 257
Cdd:PRK11124 107 PCRVLGLSK--DQALARAEKLLER-------------LRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190
....*....|....*....|....*....|...
gi 17555800 258 LDVKQRLKAAAIIRErVSDTNYV-VVVEHDLAV 289
Cdd:PRK11124 172 LDPEITAQIVSIIRE-LAETGITqVIVTHEVEV 203
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
114-292 |
5.30e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 54.31 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQkeqewttiinhFRGSEL-------QNYFTR----ILEDTLKCVIKPQ 182
Cdd:PRK10419 38 GETVALLGRSGCGKSTLARLLVGLESPSQGNVS-----------WRGEPLaklnraqRKAFRRdiqmVFQDSISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 183 YVDQIPRAAKgtveKNLTRKHDNDNL---NSVIDQMELR-GLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYL 258
Cdd:PRK10419 107 TVREIIREPL----RHLLSLDKAERLaraSEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 17555800 259 DVKQRLKAAAIIRE--RVSDTNYVVVVeHDLAVLDY 292
Cdd:PRK10419 183 DLVLQAGVIRLLKKlqQQFGTACLFIT-HDLRLVER 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
368-504 |
5.31e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.72 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 368 NFHLdvEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPE-------DENTELPHV--SISYKPQKISPKSETTVRfml 438
Cdd:PRK13539 22 SFTL--AAG-----EALVLTGPNGSGKTTLLRLIAGLLPPAagtikldGGDIDDPDVaeACHYLGHRNAMKPALTVA--- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 439 hdkiqnmyEHPQFKTDVMN--PLMMEQ---------LLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDS 504
Cdd:PRK13539 92 --------ENLEFWAAFLGgeELDIAAaleavglapLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
112-297 |
5.70e-08 |
|
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: 53.53 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 112 RCGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewTTIINHFRgselqnyftrILEDTLKCVIKPQYVDQIPraa 191
Cdd:cd03265 24 RRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG--------RATVAGHD----------VVREPREVRRRIGIVFQDL--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 192 kgTVEKNLT---------------RKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSS 256
Cdd:cd03265 83 --SVDDELTgwenlyiharlygvpGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17555800 257 YLDVKQRLKAAAIIRERVSDTNY-VVVVEHDLAVLDYLSDFI 297
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMtILLTTHYMEEAEQLCDRV 202
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
22-83 |
6.97e-08 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 49.66 E-value: 6.97e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17555800 22 VEKDRCKpkNCGLaCKRACPVNrqgkqCIVVEATStiSQISEILCIGCGICVKKCPYDAIKI 83
Cdd:COG2221 12 IDEEKCI--GCGL-CVAVCPTG-----AISLDDGK--LVIDEEKCIGCGACIRVCPTGAIKG 63
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
107-297 |
7.93e-08 |
|
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: 53.10 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 107 RLPTprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQkeqeWTTIINHFRGSELQNYFTRIledtlkcviKPQYVDQ 186
Cdd:cd03290 23 RIPT---GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH----WSNKNESEPSFEATRSRNRY---------SVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 187 IPRAAKGTVEKNLT--RKHDNDNLNSVIDQMELRGLLD-------REIDQ----LSGGELQRFAIAMCCVQKADVYMFDE 253
Cdd:cd03290 87 KPWLLNATVEENITfgSPFNKQRYKAVTDACSLQPDIDllpfgdqTEIGErginLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17555800 254 PSSYLDV--KQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYlSDFI 297
Cdd:cd03290 167 PFSALDIhlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPH-ADWI 211
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
214-298 |
8.77e-08 |
|
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: 52.99 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 214 QMELRGLLDREIDQLSGGE------LQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKA-AAIIRERVSDTNY-VVVVEH 285
Cdd:cd03240 102 QGESNWPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENIEESlAEIIEERKSQKNFqLIVITH 181
|
90
....*....|...
gi 17555800 286 DLAVLDYLSDFIC 298
Cdd:cd03240 182 DEELVDAADHIYR 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
102-302 |
9.53e-08 |
|
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: 54.29 E-value: 9.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPN-------------LGNFQKEQewttiINHFRGSELQ---- 164
Cdd:COG0444 25 SFDVRR------GETLGLVGESGSGKSTLARAILGLLPPPgitsgeilfdgedLLKLSEKE-----LRKIRGREIQmifq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 165 ------N-YFT--RILEDTLkcvikpqyvdqipRAAKGTVEKNLTRKhdndnlnsVIDQMELRGLLDRE--ID----QLS 229
Cdd:COG0444 94 dpmtslNpVMTvgDQIAEPL-------------RIHGGLSKAEARER--------AIELLERVGLPDPErrLDryphELS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 230 GGELQRFAIAMCCVQKADVYMFDEPSSYLDV---KQRLKaaaIIRERVSDTNY-VVVVEHDLAVLDYLSDFICCLYG 302
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVtiqAQILN---LLKDLQRELGLaILFITHDLGVVAEIADRVAVMYA 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
118-505 |
9.82e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 118 GLVGTNGIGKSTALKILAGKQKPNLGN--FQK-------EQE------WTTIINHFRG-SELQNYFTRILEDTLKCVIKP 181
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEarPAPgikvgylPQEpqldpeKTVRENVEEGvAEVKAALDRFNEIYAAYAEPD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVDQIprAAKGTVEKNLTRKHDNDNLNSVIDQ-ME-LRglL---DREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSS 256
Cdd:PRK11819 117 ADFDAL--AAEQGELQEIIDAADAWDLDSQLEIaMDaLR--CppwDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTN 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 257 YLD------VKQRLKaaaiirervsdtNY---VVVVEHDLAVLDYLSDFICCL---YGVP--GVYgvvtlpSG------- 315
Cdd:PRK11819 193 HLDaesvawLEQFLH------------DYpgtVVAVTHDRYFLDNVAGWILELdrgRGIPweGNY------SSwleqkak 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 316 --VREG---------INMFLEgFIRTeNMRFRESK----------LSFKTSEQQED-----I---KRTGN--IKYPSMSK 364
Cdd:PRK11819 255 rlAQEEkqeaarqkaLKRELE-WVRQ-SPKARQAKskarlaryeeLLSEEYQKRNEtneifIppgPRLGDkvIEAENLSK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 365 TLG------NFHLDVEAGDfsdseIIVMLGENGTGKTTMIKMMAGSLKPEDENTEL-PHVSISYKPQ---KISPKSetTV 434
Cdd:PRK11819 333 SFGdrllidDLSFSLPPGG-----IVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAYVDQsrdALDPNK--TV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 435 RFML---HDKIQ-NMYEHPQ--------FK-TDvmnplmmEQlldRNVKELSGGELQRVALALCLGKTASLYLIDEPSAY 501
Cdd:PRK11819 406 WEEIsggLDIIKvGNREIPSrayvgrfnFKgGD-------QQ---KKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTND 475
|
....
gi 17555800 502 LDSE 505
Cdd:PRK11819 476 LDVE 479
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
114-259 |
1.11e-07 |
|
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: 53.04 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQkPNLGNFQKEqewttIInhFRGSELQNYFTRiledtlKCVikpQYVDQIPRAAKG 193
Cdd:cd03234 33 GQVMAILGSSGSGKTTLLDAISGRV-EGGGTTSGQ-----IL--FNGQPRKPDQFQ------KCV---AYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 -TVEKNLT--------RKHDNDNLNSVIDQMELRGLLDREI-----DQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLD 259
Cdd:cd03234 96 lTVRETLTytailrlpRKSSDAIRKKRVEDVLLRDLALTRIggnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
119-287 |
1.17e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.60 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 119 LVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTiinhfrgselQNYFTRILEDTLKCVIKP--QYVDQIPRAAKGTVE 196
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT----------DDNFEKLRKHIGIVFQNPdnQFVGSIVKYDVAFGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 197 KNLTRKHDN--DNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERV 274
Cdd:PRK13648 110 ENHAVPYDEmhRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVK 189
|
170
....*....|....
gi 17555800 275 SDTNYVVV-VEHDL 287
Cdd:PRK13648 190 SEHNITIIsITHDL 203
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
363-546 |
1.30e-07 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 54.00 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 363 SKTLGNFHL--DVEAgDFSDSEIIVMLGENGTGKTTMIKMMAGSLKP---------EDENTEL----------------- 414
Cdd:COG1118 9 SKRFGSFTLldDVSL-EIASGELVALLGPSGSGKTTLLRIIAGLETPdsgrivlngRDLFTNLpprerrvgfvfqhyalf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 415 PHVS----ISYKPQKISP-KSE--TTVRFMLhDKIQnmyehpqfktdvmnplmMEQLLDRNVKELSGGELQRVALALCLG 487
Cdd:COG1118 88 PHMTvaenIAFGLRVRPPsKAEirARVEELL-ELVQ-----------------LEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 488 KTASLYLIDEP-SAyLDS----EQRLHAAKVIKRFimhaKKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:COG1118 150 VEPEVLLLDEPfGA-LDAkvrkELRRWLRRLHDEL----GGTTVFVTHDQEEALELADRVVVMN 208
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
19-83 |
1.31e-07 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 48.94 E-value: 1.31e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 19 IAIVEKDRCKpkNCGlACKRACPVN-----RQGKQCIVVEATStisqiseilCIGCGICVKKCPYDAIKI 83
Cdd:COG1146 2 MPVIDTDKCI--GCG-ACVEVCPVDvleldEEGKKALVINPEE---------CIGCGACELVCPVGAITV 59
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
114-288 |
1.44e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.83 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQ------------KEQEwtTIINHFR---GSELQNYFTRILEDTLKCV 178
Cdd:PRK11264 29 GEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarslSQQK--GLIRQLRqhvGFVFQNFNLFPHRTVLENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 179 IK-PQYVDQIPRAAKGTVEKNLTRKhdndnlnsvidqMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSY 257
Cdd:PRK11264 107 IEgPVIVKGEPKEEATARARELLAK------------VGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190
....*....|....*....|....*....|.
gi 17555800 258 LDVKQRLKAAAIIRERVSDTNYVVVVEHDLA 288
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
366-530 |
1.61e-07 |
|
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: 54.53 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDenTELPHVS-ISYKPQK--ISPKsetTVRfmlhDKI 442
Cdd:TIGR01271 442 LKNISFKLEKG-----QLLAVAGSTGSGKSSLLMMIMGELEPSE--GKIKHSGrISFSPQTswIMPG---TIK----DNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 443 QNMYEHPQFK-TDVMNPLMMEQ------------LLDRNVKeLSGGELQRVALALCLGKTASLYLIDEPSAYLD--SEQR 507
Cdd:TIGR01271 508 IFGLSYDEYRyTSVIKACQLEEdialfpekdktvLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFTHLDvvTEKE 586
|
170 180
....*....|....*....|....*..
gi 17555800 508 LHAAKVIKrfiMHAKKTAFVV----EH 530
Cdd:TIGR01271 587 IFESCLCK---LMSNKTRILVtsklEH 610
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
18-85 |
1.75e-07 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 53.88 E-value: 1.75e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 18 RIAIVEKDRCKPKNCGlACKRACPVNrqgkqciVVEATSTISQISEILCIGCGICVKKCPYDAIKIIN 85
Cdd:COG4624 82 RGPSIIRDKEKCKNCY-PCVRACPVK-------AIKVDDGKAEIDEEKCISCGQCVAVCPFGAITEKS 141
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
114-254 |
1.82e-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: 52.55 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewttiinhfrgselqnyftRILedtlkcvIKPQYVDQIP---RA 190
Cdd:cd03218 26 GEIVGLLGPNGAGKTTTFYMIVGLVKPDSG-------------------------KIL-------LDGQDITKLPmhkRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 191 AKG--------------TVEKNL---------TRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKAD 247
Cdd:cd03218 74 RLGigylpqeasifrklTVEENIlavleirglSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
....*..
gi 17555800 248 VYMFDEP 254
Cdd:cd03218 154 FLLLDEP 160
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
368-543 |
1.85e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 368 NFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPED------ENTelphvSISYKPQkispksETTVRFmlhDK 441
Cdd:PRK15064 337 NLNLLLEAG-----ERLAIIGENGVGKTTLLRTLVGELEPDSgtvkwsENA-----NIGYYAQ------DHAYDF---EN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 442 IQNMYE-HPQFKTDVMNPLMMEQLLDR----------NVKELSGGELQRVALA-LCLGKTASLyLIDEPSAYLDSE--QR 507
Cdd:PRK15064 398 DLTLFDwMSQWRQEGDDEQAVRGTLGRllfsqddikkSVKVLSGGEKGRMLFGkLMMQKPNVL-VMDEPTNHMDMEsiES 476
|
170 180 190
....*....|....*....|....*....|....*.
gi 17555800 508 LHAAkvIKRFimhaKKTAFVVEHDFIMATYLADRVV 543
Cdd:PRK15064 477 LNMA--LEKY----EGTLIFVSHDREFVSSLATRII 506
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
114-259 |
1.93e-07 |
|
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: 52.02 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewTTIIN-----HFRGSELQnYFTR----ILEDtLKCVIKPQYV 184
Cdd:cd03292 27 GEFVFLVGPSGAGKSTLLKLIYKEELPTSG--------TIRVNgqdvsDLRGRAIP-YLRRkigvVFQD-FRLLPDRNVY 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 185 DQIPRAAKGTVEKnltRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLD 259
Cdd:cd03292 97 ENVAFALEVTGVP---PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
380-555 |
2.44e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.30 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 380 DSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTEL--PHVS----------ISYKPQKISPKSETTVRFMLhdkIQNMYE 447
Cdd:PRK10253 32 DGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgEHIQhyaskevarrIGLLAQNATTPGDITVQELV---ARGRYP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 448 H-PQFK----------TDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKR 516
Cdd:PRK10253 109 HqPLFTrwrkedeeavTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSE 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17555800 517 FIMHAKKTAFVVEHDFIMATYLA-------DRVVVFEGQPSVKCTA 555
Cdd:PRK10253 189 LNREKGYTLAAVLHDLNQACRYAshlialrEGKIVAQGAPKEIVTA 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
102-291 |
2.65e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 51.59 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKP----------NLGNFQKEQewttiINHFR---GSELQNYft 168
Cdd:COG2884 22 SLEIEK------GEFVFLTGPSGAGKSTLLKLLYGEERPtsgqvlvngqDLSRLKRRE-----IPYLRrriGVVFQDF-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 169 RILEDtlkcvikpqyvdqipRaakgTVEKNL---------TRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIA 239
Cdd:COG2884 89 RLLPD---------------R----TVYENValplrvtgkSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17555800 240 MCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRE--RVSDTnyVVVVEHDLAVLD 291
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEinRRGTT--VLIATHDLELVD 201
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
101-286 |
2.99e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 101 NSFKLHRLPTPRcgevLGLVGTNGIGKSTALKILAGKQKPNLGNfqkeqewttiINHFRGSELqNYFTRILEDTLKCVIK 180
Cdd:PRK10636 329 DSIKLNLVPGSR----IGLLGRNGAGKSTLIKLLAGELAPVSGE----------IGLAKGIKL-GYFAQHQLEFLRADES 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 181 PqyVDQIPRAAKGTVEKNLtrkhdNDNL-------NSVIDQMElrglldreidQLSGGELQRFAIAMCCVQKADVYMFDE 253
Cdd:PRK10636 394 P--LQHLARLAPQELEQKL-----RDYLggfgfqgDKVTEETR----------RFSGGEKARLVLALIVWQRPNLLLLDE 456
|
170 180 190
....*....|....*....|....*....|....*
gi 17555800 254 PSSYLDV--KQRLKAAAIIRErvsdtNYVVVVEHD 286
Cdd:PRK10636 457 PTNHLDLdmRQALTEALIDFE-----GALVVVSHD 486
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
102-295 |
3.13e-07 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 51.67 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLH-----RLP-------TPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGN--FQKEQEWTTI-------INHFRG 160
Cdd:COG4778 13 TFTLHlqggkRLPvldgvsfSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWVDLaqaspreILALRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 161 SEL----QnyFTRILE--DTLKCVIKPQYVDQIPRA-AKGTVEKNLTRkhdndnLNsvidqmelrglLDREIDQL----- 228
Cdd:COG4778 93 RTIgyvsQ--FLRVIPrvSALDVVAEPLLERGVDREeARARARELLAR------LN-----------LPERLWDLppatf 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 229 SGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSD 295
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVAD 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
365-548 |
3.50e-07 |
|
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: 53.21 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 365 TLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPE------D-------ENTEL-PHvsISYKPQKIS--P 428
Cdd:COG4618 347 ILRGVSFSLEPG-----EVLGVIGPSGSGKSTLARLLVGVWPPTagsvrlDgadlsqwDREELgRH--IGYLPQDVElfD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 429 kseTTV-----RFM---------------LHDKIQNMyehPQ-FKTDV-MNPLMmeqlldrnvkeLSGGELQRVALALCL 486
Cdd:COG4618 420 ---GTIaeniaRFGdadpekvvaaaklagVHEMILRL---PDgYDTRIgEGGAR-----------LSGGQRQRIGLARAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 487 GKTASLYLIDEPSAYLDS--EQRLHAAkvikrfIMHAKK---TAFVVEHDF-IMAtyLADRVVVF-EGQ 548
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDegEAALAAA------IRALKArgaTVVVITHRPsLLA--AVDKLLVLrDGR 543
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
357-537 |
3.67e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 51.21 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 357 IKYPSMSKTLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPE-------DEN-TELPHVSISYKPQKISp 428
Cdd:COG2884 9 KRYPGGREALSDVSLEIEKGEF-----VFLTGPSGAGKSTLLKLLYGEERPTsgqvlvnGQDlSRLKRREIPYLRRRIG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 429 ksettVRF----MLHDK--IQNM--------YEHPQFKTDVMNPLMM---EQLLDRNVKELSGGELQRVALALCLGKTAS 491
Cdd:COG2884 83 -----VVFqdfrLLPDRtvYENValplrvtgKSRKEIRRRVREVLDLvglSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17555800 492 LYLIDEPSAYLDSEQRLHAAKVIKRFimHAKKTAfvvehdFIMATY 537
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEI--NRRGTT------VLIATH 195
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
340-546 |
4.39e-07 |
|
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: 50.99 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 340 LSFKTS-EQQEDIKRTGNIKYPSMSKT---LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPeDENTelp 415
Cdd:cd03220 8 KSYPTYkGGSSSLKKLGILGRKGEVGEfwaLKDVSFEVPRG-----ERIGLIGRNGAGKSTLLRLLAGIYPP-DSGT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 416 hVSISykpQKISP--------KSETTVRfmlhdkiQNMYehpqfktdvMNPLMM--------------------EQLLDR 467
Cdd:cd03220 79 -VTVR---GRVSSllglgggfNPELTGR-------ENIY---------LNGRLLglsrkeidekideiiefselGDFIDL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 468 NVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAkKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:cd03220 139 PVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQG-KTVILVSHDPSSIKRLCDRALVLE 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
359-547 |
4.70e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 52.86 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 359 YPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPED-----ENTELPHVS-------ISYKPQKI 426
Cdd:COG1132 349 YPGDRPVLKDISLTIPPG-----ETVALVGPSGSGKSTLVNLLLRFYDPTSgriliDGVDIRDLTleslrrqIGVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 427 spksettvrFMLHDKI-QNM-YEHP--------------QFKTDVMNplmMEQLLDRNVKE----LSGGELQRVALA--- 483
Cdd:COG1132 424 ---------FLFSGTIrENIrYGRPdatdeeveeaakaaQAHEFIEA---LPDGYDTVVGErgvnLSGGQRQRIAIAral 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 484 LclgKTASLYLIDEPSAYLD--SEQRLHAAkvIKRFImhAKKTAFVVEHDF--IMAtylADRVVVFEG 547
Cdd:COG1132 492 L---KDPPILILDEATSALDteTEALIQEA--LERLM--KGRTTIVIAHRLstIRN---ADRILVLDD 549
|
|
| FDH_beta_like |
cd16366 |
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ... |
8-83 |
5.76e-07 |
|
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: 49.71 E-value: 5.76e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 8 IKNNETDVPLRIAiveKDRCKpkNCGLA-CKRACPVNrqgkqCIVVEATSTISQISEiLCIGCGICVKKCPYDAIKI 83
Cdd:cd16366 54 VEKPGGDLSWLFR---KDQCM--HCTDAgCLAACPTG-----AIIRTETGTVVVDPE-TCIGCGYCVNACPFDIPRF 119
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
84-260 |
6.20e-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: 52.43 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 84 INLPANL-ANETTHRYSQNSFKLHRLP-TPRCGEVLGLVGTNGIGKSTALKILAgkqkpnlgNFQKEQEWTTIINHFrgs 161
Cdd:TIGR01193 468 NNLNGDIvINDVSYSYGYGSNILSDISlTIKMNSKTTIVGMSGSGKSTLAKLLV--------GFFQARSGEILLNGF--- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 162 ELQNyftrILEDTLKCVIkpQYVDQIPRAAKGTVEKNL----TRKHDNDNLNSVIDQMELR--------GL---LDREID 226
Cdd:TIGR01193 537 SLKD----IDRHTLRQFI--NYLPQEPYIFSGSILENLllgaKENVSQDEIWAACEIAEIKddienmplGYqteLSEEGS 610
|
170 180 190
....*....|....*....|....*....|....
gi 17555800 227 QLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDV 260
Cdd:TIGR01193 611 SISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
382-507 |
6.81e-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: 49.29 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 382 EIIVMLGENGTGKTTMIKMMAGSLKPedentelphvsisykpqkispkseTTVRFMLHDkiqnmyehPQFKTDVMNPLMM 461
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGP------------------------PGGGVIYID--------GEDILEEVLDQLL 50
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 17555800 462 EQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQR 507
Cdd:smart00382 51 LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQE 96
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
386-544 |
6.90e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.91 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 386 MLGENGTGKTTMIKMMAGSLKPEDENtelphvsISYKPQKISPKSETTVRFMLHDKIQN--------------------- 444
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIEKVKSGE-------IFYNNQAITDDNFEKLRKHIGIVFQNpdnqfvgsivkydvafglenh 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 445 MYEHPQFKTDVMNPLMMEQLLDRNVKE---LSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHA 521
Cdd:PRK13648 113 AVPYDEMHRRVSEALKQVDMLERADYEpnaLSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEH 192
|
170 180
....*....|....*....|...
gi 17555800 522 KKTAFVVEHDFIMATYlADRVVV 544
Cdd:PRK13648 193 NITIISITHDLSEAME-ADHVIV 214
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
384-505 |
7.00e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 384 IVMLGENGTGKTTMIKMMAGSLKP-EDENTELPHVSISYKPQKisPK--SETTV----------------RFmlhDKIQN 444
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEfEGEARPAPGIKVGYLPQE--PQldPEKTVrenveegvaevkaaldRF---NEIYA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 445 MYEHPqfkTDVMNPLMMEQ--L-----------LDR----------------NVKELSGGELQRVALALCLGKTASLYLI 495
Cdd:PRK11819 111 AYAEP---DADFDALAAEQgeLqeiidaadawdLDSqleiamdalrcppwdaKVTKLSGGERRRVALCRLLLEKPDMLLL 187
|
170
....*....|
gi 17555800 496 DEPSAYLDSE 505
Cdd:PRK11819 188 DEPTNHLDAE 197
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
460-507 |
7.28e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.15 E-value: 7.28e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 17555800 460 MMEQLLDRNVKE----LSGGELQRVALALCLGKTASLYLIDEPSAYLD--SEQR 507
Cdd:PRK11174 470 LLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDahSEQL 523
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
359-543 |
7.73e-07 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 50.32 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 359 YPSMSKTLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKP---------EDENT----ELP----HVSISY 421
Cdd:TIGR02673 11 YPGGVAALHDVSLHIRKGEF-----LFLTGPSGAGKTTLLKLLYGALTPsrgqvriagEDVNRlrgrQLPllrrRIGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 422 KPQKISPKSET--TVRFMLH------DKIQNMYEHpqfktdVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLY 493
Cdd:TIGR02673 86 QDFRLLPDRTVyeNVALPLEvrgkkeREIQRRVGA------ALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17555800 494 LIDEPSAYLDSEQRLHAAKVIKRFIMHAkKTAFVVEHDFIMATYLADRVV 543
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRG-TTVIVATHDLSLVDRVAHRVI 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
352-544 |
7.74e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.64 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 352 KRTGNikypsmSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKP---------ED------ENTEL-- 414
Cdd:PRK11432 14 KRFGS------NTVIDNLNLTIKQG-----TMVTLLGPSGCGKTTVLRLVAGLEKPtegqifidgEDvthrsiQQRDIcm 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 415 --------PHVSI----SY--KPQKIsPKSETtvrfmlhdkiqnmyehpqfKTDVMNPLMMEQLL---DRNVKELSGGEL 477
Cdd:PRK11432 83 vfqsyalfPHMSLgenvGYglKMLGV-PKEER-------------------KQRVKEALELVDLAgfeDRYVDQISGGQQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 478 QRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVV 544
Cdd:PRK11432 143 QRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIV 209
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
102-287 |
8.35e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.03 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHrlptPrcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIINHfrgselqNYFTRiledtlkcviKP 181
Cdd:TIGR00958 501 TFTLH----P--GEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH-------HYLHR----------QV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVDQIPRAAKGTVEKN----LTRKHDNDNLNSVIDQ------MELRGLLDREID----QLSGGELQRFAIAMCCVQKAD 247
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENiaygLTDTPDEEIMAAAKAAnahdfiMEFPNGYDTEVGekgsQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17555800 248 VYMFDEPSSYLDVkQRLKAAAIIRERVSDTnyVVVVEHDL 287
Cdd:TIGR00958 638 VLILDEATSALDA-ECEQLLQESRSRASRT--VLLIAHRL 674
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
465-549 |
9.29e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.95 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 465 LDRNVKELSGGELQRVALALCLGK--TASLYLIDEPSAyldseqRLHA---AKVIKrfIMHAKK----TAFVVEHD--FI 533
Cdd:COG0178 479 LDRSAGTLSGGEAQRIRLATQIGSglVGVLYVLDEPSI------GLHQrdnDRLIE--TLKRLRdlgnTVIVVEHDedTI 550
|
90 100
....*....|....*....|....*....
gi 17555800 534 MAtylADRV-------------VVFEGQP 549
Cdd:COG0178 551 RA---ADYIidigpgagehggeVVAQGTP 576
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
114-301 |
9.67e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 50.35 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGN--------------------FQKEQ------EWTTIINHFrgsELQNYF 167
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSivvngqtinlvrdkdgqlkvADKNQlrllrtRLTMVFQHF---NLWSHM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 168 TrILEDTLkcvikpqyvdQIPRAAKGtVEKNLTRKHDNDNLNSVidqmelrGLLDREIDQ----LSGGELQRFAIAMCCV 243
Cdd:PRK10619 108 T-VLENVM----------EAPIQVLG-LSKQEARERAVKYLAKV-------GIDERAQGKypvhLSGGQQQRVSIARALA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 244 QKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSDFICCLY 301
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLH 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
366-545 |
9.81e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.56 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPeDENTelphvsISYKPQKISPKS--------------- 430
Cdd:COG1129 20 LDGVSLELRPG-----EVHALLGENGAGKSTLMKILSGVYQP-DSGE------ILLDGEPVRFRSprdaqaagiaiihqe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 431 -----ETTVRfmlhdkiQNMY-EHPQFKTDVMNPLMM----EQLLDR---------NVKELSGGELQRVALALCLGKTAS 491
Cdd:COG1129 88 lnlvpNLSVA-------ENIFlGREPRRGGLIDWRAMrrraRELLARlgldidpdtPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 492 LyLI-DEPSAYLDSE--QRLHaaKVIKRFimHAKKTAFV-VEHDF--IMAtyLADRVVVF 545
Cdd:COG1129 161 V-LIlDEPTASLTERevERLF--RIIRRL--KAQGVAIIyISHRLdeVFE--IADRVTVL 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
371-547 |
9.87e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 50.52 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 371 LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSI----SYKPQK-ISPKSETTVRFMLHDKiqNM 445
Cdd:PRK11264 24 LEVKPG-----EVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarSLSQQKgLIRQLRQHVGFVFQNF--NL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 446 YEHPQFKTDVMN-PLMME------------QLL---------DRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLD 503
Cdd:PRK11264 97 FPHRTVLENIIEgPVIVKgepkeeatararELLakvglagkeTSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17555800 504 SEQRLHAAKVIkRFIMHAKKTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:PRK11264 177 PELVGEVLNTI-RQLAQEKRTMVIVTHEMSFARDVADRAIFMDQ 219
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
3-84 |
1.00e-06 |
|
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: 49.03 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 3 RKGPLIKNNETDVPLRIAIVEKDRCKpkNCGlACKRACPVNrqgkqcIVVEATSTISQISEILCIGCGICVKKCPYDAIK 82
Cdd:TIGR01944 91 IPQPLDADAGTIQPPMVALIDEDNCI--GCT-KCIQACPVD------AIVGAAKAMHTVIADECTGCDLCVEPCPTDCIE 161
|
..
gi 17555800 83 II 84
Cdd:TIGR01944 162 MI 163
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
114-301 |
1.02e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.86 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNF---------QKEQEWTTIinhfRgSELQnyftRILEDTLKCVIKPQYV 184
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkdllgMKDDEWRAV----R-SDIQ----MIFQDPLASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 185 DQIPRAAKGTVEKNLTRKHDNDNLNSVIDQMELR-GLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQR 263
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
|
170 180 190
....*....|....*....|....*....|....*....
gi 17555800 264 LKAAAIIRERVSDTNY-VVVVEHDLAVLDYLSDFICCLY 301
Cdd:PRK15079 198 AQVVNLLQQLQREMGLsLIFIAHDLAVVKHISDRVLVMY 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
384-546 |
1.02e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.57 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 384 IVMLGENGTGKTTMIKMMAGSLKPEDEntelphvSISYKPQKISPKSETTVRFMLHDKIQNMYEH---PQFKTDV----- 455
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSG-------SVLIRGEPITKENIREVRKFVGLVFQNPDDQifsPTVEQDIafgpi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 456 ----------------MNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIM 519
Cdd:PRK13652 106 nlgldeetvahrvssaLHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPE 185
|
170 180
....*....|....*....|....*..
gi 17555800 520 HAKKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:PRK13652 186 TYGMTVIFSTHQLDLVPEMADYIYVMD 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
114-277 |
1.10e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.26 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIInhFRGSELQNYFT-RILEDTLKCVIKPQYVdqiprAAK 192
Cdd:PRK11614 31 GEIVTLIGANGAGKTTLLGTLCGDPRATSG---------RIV--FDGKDITDWQTaKIMREAVAIVPEGRRV-----FSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 193 GTVEKNLT-------RKHDNDNLNSVIDQMELrgLLDREIDQ---LSGGELQRFAIAMCCVQKADVYMFDEPSsyldvkq 262
Cdd:PRK11614 95 MTVEENLAmggffaeRDQFQERIKWVYELFPR--LHERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLDEPS------- 165
|
170
....*....|....*
gi 17555800 263 rLKAAAIIRERVSDT 277
Cdd:PRK11614 166 -LGLAPIIIQQIFDT 179
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
18-84 |
1.23e-06 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 48.11 E-value: 1.23e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 18 RIAIVEKD------RCKpkNCGLA-CKRACPVN--RQGKQCIVVEATstisqiseiLCIGCGICVKKCPYDAIKII 84
Cdd:COG1142 37 RIRVVRKAgvsapvQCR--HCEDApCAEVCPVGaiTRDDGAVVVDEE---------KCIGCGLCVLACPFGAITMV 101
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
114-347 |
1.23e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.80 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGkqkpnlgnfqkeqewttiinhfrgselqnyftriLED--TLKCVIKPQYVDQIPRAA 191
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAG----------------------------------LEDitSGDLFIGEKRMNDVPPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 192 KG--------------TVEKNL--------TRKHDNDN-LNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADV 248
Cdd:PRK11000 75 RGvgmvfqsyalyphlSVAENMsfglklagAKKEEINQrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 249 YMFDEPSSYLDVKQRLKAAAII---RERVSDTnyVVVVEHDLAVLDYLSDFICCLYG--VPGVYGVVTL---PSgvregi 320
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEIsrlHKRLGRT--MIYVTHDQVEAMTLADKIVVLDAgrVAQVGKPLELyhyPA------ 226
|
250 260
....*....|....*....|....*..
gi 17555800 321 NMFLEGFIRTENMRFRESKLSFKTSEQ 347
Cdd:PRK11000 227 NRFVAGFIGSPKMNFLPVKVTATAIEQ 253
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
216-286 |
1.37e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.61 E-value: 1.37e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 216 ELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRE---RVSDTNyvVVVEHD 286
Cdd:PRK11650 123 ELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRlhrRLKTTS--LYVTHD 194
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
221-296 |
1.48e-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: 49.56 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 221 LDREIDQLSGGELQRFAIAMCCVQKAD--VYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVL---DYLSD 295
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIraaDHVID 210
|
.
gi 17555800 296 F 296
Cdd:cd03270 211 I 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
114-263 |
1.51e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 50.72 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEwttIINHFRGSE------LQNY--FTR--ILEDT---LKCVIK 180
Cdd:PRK09452 40 GEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ---DITHVPAENrhvntvFQSYalFPHmtVFENVafgLRMQKT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 181 PQyvDQI-PRAAkgtveknltrkhdnDNLNSVidqmELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLD 259
Cdd:PRK09452 117 PA--AEItPRVM--------------EALRMV----QLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
....
gi 17555800 260 VKQR 263
Cdd:PRK09452 177 YKLR 180
|
|
| DMSOR_beta_like |
cd16371 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
35-83 |
1.63e-06 |
|
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: 47.94 E-value: 1.63e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 17555800 35 ACKRACPVN-----RQGkqcIVVeatstisqISEILCIGCGICVKKCPYDAIKI 83
Cdd:cd16371 61 ACVKVCPTGaitkrEDG---IVV--------VDQDKCIGCGYCVWACPYGAPQY 103
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
102-270 |
1.64e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.79 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIinHFRGSELQnyFTRILEDT-LKCVIK 180
Cdd:COG1129 24 SLELRP------GEVHALLGENGAGKSTLMKILSGVYQPDSG---------EI--LLDGEPVR--FRSPRDAQaAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 181 PQYVDQIPRAakgTVEKNL------TRKHdndnlnsVIDQMELR----GLLDR---EID------QLSGGELQRFAIAMC 241
Cdd:COG1129 85 HQELNLVPNL---SVAENIflgrepRRGG-------LIDWRAMRrrarELLARlglDIDpdtpvgDLSVAQQQLVEIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17555800 242 CVQKADVYMFDEPSSYLDVKQ---------RLKA--AAII 270
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREverlfriirRLKAqgVAII 194
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
366-547 |
1.66e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.09 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPED--------ENTELPHV-------------------- 417
Cdd:PRK13633 26 LDDVNLEVKKGEF-----LVILGRNGSGKSTIAKHMNALLIPSEgkvyvdglDTSDEENLwdirnkagmvfqnpdnqiva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 418 -----SISYKPQKIS-PKSETTVRFMLHDKIQNMYEHPQFKtdvmnPLMmeqlldrnvkeLSGGELQRVALALCLGKTAS 491
Cdd:PRK13633 101 tiveeDVAFGPENLGiPPEEIRERVDESLKKVGMYEYRRHA-----PHL-----------LSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 492 LYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHdFIMATYLADRVVVFEG 547
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITH-YMEEAVEADRIIVMDS 219
|
|
| RLI |
pfam04068 |
Possible Fer4-like domain in RNase L inhibitor, RLI; Possible metal-binding domain in ... |
17-47 |
1.69e-06 |
|
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: 44.81 E-value: 1.69e-06
10 20 30
....*....|....*....|....*....|....
gi 17555800 17 LRIAIVEKDRCKPKNC-GLACKRACPV--NRQGK 47
Cdd:pfam04068 1 MRLAIVDFDQCDPKKCtGRKCIRFCPVreVRTGK 34
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
114-300 |
1.84e-06 |
|
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: 49.54 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAgkqkpnlgNFQKEQEWTTIINHFRGSEL-QNYFTR----------ILEDTLKCVIKPQ 182
Cdd:cd03253 27 GKKVAIVGPSGSGKSTILRLLF--------RFYDVSSGSILIDGQDIREVtLDSLRRaigvvpqdtvLFNDTIGYNIRYG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 183 YVD----QIPRAAKgtveknLTRKHD-----NDNLNSVIDQmelRGLldreidQLSGGELQRFAIAMCCVQKADVYMFDE 253
Cdd:cd03253 99 RPDatdeEVIEAAK------AAQIHDkimrfPDGYDTIVGE---RGL------KLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17555800 254 PSSYLDV-KQRLKAAAIirERVSDTNYVVVVEHDLA-VLDylSDFICCL 300
Cdd:cd03253 164 ATSALDThTEREIQAAL--RDVSKGRTTIVIAHRLStIVN--ADKIIVL 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
367-548 |
1.91e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.43 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 367 GNFHLDV-EAGDFS--DSEIIVMLGENGTGKTTMIKMMAGSLKPEDENtelphvsISYKPQKISPKSETTVRFMLHDKIQ 443
Cdd:PRK11629 18 GSVQTDVlHNVSFSigEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGD-------VIFNGQPMSKLSSAAKAELRNQKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 444 NMYE--H--PQFKT--DVMNPLMM-------------EQL----LDRNVK----ELSGGELQRVALALCLGKTASLYLID 496
Cdd:PRK11629 91 FIYQfhHllPDFTAleNVAMPLLIgkkkpaeinsralEMLaavgLEHRANhrpsELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 497 EPSAYLDseQRlhAAKVIKRFIMH---AKKTAF-VVEHDFIMATYLADRVVVFEGQ 548
Cdd:PRK11629 171 EPTGNLD--AR--NADSIFQLLGElnrLQGTAFlVVTHDLQLAKRMSRQLEMRDGR 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
114-317 |
1.95e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.60 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIInhFRGSELQNYFTRILedTLKCVIKP-QYVdqipRAAK 192
Cdd:PRK11300 31 QEIVSLIGPNGAGKTTVFNCLTGFYKPTGG---------TIL--LRGQHIEGLPGHQI--ARMGVVRTfQHV----RLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 193 G-TVEKNL---TRKHDNDNLNS---------------------VIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKAD 247
Cdd:PRK11300 94 EmTVIENLlvaQHQQLKTGLFSgllktpafrraesealdraatWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17555800 248 VYMFDEPSSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDLAVLDYLSDFICCL-YGVPGVYGvvtLPSGVR 317
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVtVLLIEHDMKLVMGISDRIYVVnQGTPLANG---TPEEIR 242
|
|
| HycB_like |
cd10554 |
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ... |
36-81 |
1.96e-06 |
|
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: 47.64 E-value: 1.96e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 17555800 36 CKRACPVN--RQGKQCIvveatstisQISEILCIGCGICVKKCPYDAI 81
Cdd:cd10554 64 CANVCPVGaiSQEDGVV---------QVDEERCIGCKLCVLACPFGAI 102
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
117-297 |
2.01e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.80 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 117 LGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIIN-----HFRGSELQNYFTRILEDTLKCVIkpqyvdqipraA 191
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENirevrKFVGLVFQNPDDQIFSPTVEQDI-----------A 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 192 KGTVEKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIR 271
Cdd:PRK13652 102 FGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLN 181
|
170 180
....*....|....*....|....*..
gi 17555800 272 ERVSDTNYVVVVE-HDLAVLDYLSDFI 297
Cdd:PRK13652 182 DLPETYGMTVIFStHQLDLVPEMADYI 208
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
16-83 |
2.05e-06 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 49.68 E-value: 2.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17555800 16 PLRIAiVEKDRCKpkNCGLaCKRACPVN---RQGKqcivveatstISQISeilCIGCGICVKKCPYDAIKI 83
Cdd:COG0348 202 TLRVR-YDRGDCI--DCGL-CVKVCPMGidiRKGE----------INQSE---CINCGRCIDACPKDAIRF 255
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
363-547 |
2.24e-06 |
|
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: 48.62 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 363 SKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHvSISYKPQK--ISPkseTTVRfmlhD 440
Cdd:cd03250 18 SFTLKDINLEVPKG-----ELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIAYVSQEpwIQN---GTIR----E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 441 KI-------QNMYEHP----QFKTDvmnplmMEQLLDRNVKE-------LSGGELQRVALALCLGKTASLYLIDEPSAYL 502
Cdd:cd03250 85 NIlfgkpfdEERYEKVikacALEPD------LEILPDGDLTEigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17555800 503 DSeqrlH-AAKVIKRFIMHA---KKTAFVVEH--DFIMAtylADRVVVFEG 547
Cdd:cd03250 159 DA----HvGRHIFENCILGLllnNKTRILVTHqlQLLPH---ADQIVVLDN 202
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
362-546 |
2.32e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.87 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 362 MSKTLGNFHLDVEAgDFSDSEIIVMLGENGTGKTTMIKMMAGSLKPE--------------DENTELP--HVSISYKPQK 425
Cdd:PRK11144 6 FKQQLGDLCLTVNL-TLPAQGITAIFGRSGAGKTSLINAISGLTRPQkgrivlngrvlfdaEKGICLPpeKRRIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 426 ispksettVRFMLHDKIQ-NM------YEHPQFKtDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEP 498
Cdd:PRK11144 85 --------ARLFPHYKVRgNLrygmakSMVAQFD-KIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 499 SAYLD----SE-----QRLhaAKVIKRFIMHakktafvVEH--DFIMatYLADRVVVFE 546
Cdd:PRK11144 156 LASLDlprkREllpylERL--AREINIPILY-------VSHslDEIL--RLADRVVVLE 203
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
363-528 |
2.90e-06 |
|
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: 49.47 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 363 SKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDenTELPHVS-ISYKPQK--ISPKS--ETTVRFM 437
Cdd:cd03291 50 APVLKNINLKIEKG-----EMLAITGSTGSGKTSLLMLILGELEPSE--GKIKHSGrISFSSQFswIMPGTikENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 438 LHD--KIQNMYEHPQFKTDVMN-PLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLD--SEQRLHAAK 512
Cdd:cd03291 123 SYDeyRYKSVVKACQLEEDITKfPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfTEKEIFESC 202
|
170
....*....|....*.
gi 17555800 513 VIKrfiMHAKKTAFVV 528
Cdd:cd03291 203 VCK---LMANKTRILV 215
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
465-549 |
3.01e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 465 LDRNVKELSGGELQRVALALCLGKTAS--LYLIDEPSAYLDSEQRLHAAKVIKRfIMHAKKTAFVVEHDFIMATyLADRV 542
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKK-LRDQGNTVLLVEHDEQMIS-LADRI 547
|
90 100
....*....|....*....|
gi 17555800 543 -------------VVFEGQP 549
Cdd:PRK00635 548 idigpgagifggeVLFNGSP 567
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
377-550 |
3.10e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.88 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 377 DFSDSEIIVMLGENGTGKTTMIKMM------AGSLKPE------DENTELPHVSISYKPQKIS---PKSeTTVRFMLHDK 441
Cdd:PRK14258 29 EIYQSKVTAIIGPSGCGKSTFLKCLnrmnelESEVRVEgrveffNQNIYERRVNLNRLRRQVSmvhPKP-NLFPMSVYDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 442 IQNMYE----HPQFKTD--VMNPLMMEQLLD-------RNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRL 508
Cdd:PRK14258 108 VAYGVKivgwRPKLEIDdiVESALKDADLWDeikhkihKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASM 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17555800 509 HAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVVFEGQPS 550
Cdd:PRK14258 188 KVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNEN 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
114-287 |
3.27e-06 |
|
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: 50.05 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewTTIINHFRGSELQnyftrilEDTLKCVIKpqYVDQIPRAAKG 193
Cdd:TIGR02868 361 GERVAILGPSGSGKSTLLATLAGLLDPLQG--------EVTLDGVPVSSLD-------QDEVRRRVS--VCAQDAHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TVEKNL--TRKH-DNDNLNSVIDQMELRGLLDREID-----------QLSGGELQRFAIAMCCVQKADVYMFDEPSSYLD 259
Cdd:TIGR02868 424 TVRENLrlARPDaTDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180 190
....*....|....*....|....*....|
gi 17555800 260 VKqrlKAAAIIRE--RVSDTNYVVVVEHDL 287
Cdd:TIGR02868 504 AE---TADELLEDllAALSGRTVVLITHHL 530
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
386-563 |
3.30e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.42 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 386 MLGENGTGKTTMIKMM-------AGSLK----PEDENTELPHVSISYKPQKISPKSETTVRFMLHDKIQNMYEHPQFKTD 454
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLlglthpdAGSISlcgePVPSRARHARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 455 VMNPLM----MEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRlHAAKVIKRFIMHAKKTAFVVEH 530
Cdd:PRK13537 118 LVPPLLefakLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR-HLMWERLRSLLARGKTILLTTH 196
|
170 180 190
....*....|....*....|....*....|...
gi 17555800 531 DFIMATYLADRVVVFEGqpSVKCTACKPQSLLE 563
Cdd:PRK13537 197 FMEEAERLCDRLCVIEE--GRKIAEGAPHALIE 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
114-287 |
3.30e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 49.01 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQewTTIINHFRGSELQNYFTRIledtlkcvikpQYVDQIPRAA-- 191
Cdd:PRK13646 33 GKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD--ITITHKTKDKYIRPVRKRI-----------GMVFQFPESQlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 192 KGTVEKNLT--RKHDNDNLNSVIDQ-----MEL---RGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVK 261
Cdd:PRK13646 100 EDTVEREIIfgPKNFKMNLDEVKNYahrllMDLgfsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180
....*....|....*....|....*..
gi 17555800 262 QRLKAAAIIRE-RVSDTNYVVVVEHDL 287
Cdd:PRK13646 180 SKRQVMRLLKSlQTDENKTIILVSHDM 206
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
353-548 |
3.41e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.91 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 353 RTGNIKYPSMSKT-LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEdentelpHVSISYKPQKISPKSE 431
Cdd:PRK10419 14 AHGGLSGKHQHQTvLNNVSLSLKSG-----ETVALLGRSGCGKSTLARLLVGLESPS-------QGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 432 T-------TVRFMLHDKIQNMyeHPQFKTD--VMNPL-----------------MMEQ------LLDRNVKELSGGELQR 479
Cdd:PRK10419 82 AqrkafrrDIQMVFQDSISAV--NPRKTVReiIREPLrhllsldkaerlaraseMLRAvdlddsVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17555800 480 VALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRfIMHAKKTAFV-VEHDFIMATYLADRVVVF-EGQ 548
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKK-LQQQFGTACLfITHDLRLVERFCQRVMVMdNGQ 229
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
35-83 |
3.68e-06 |
|
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: 46.61 E-value: 3.68e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 17555800 35 ACKRACPVNrqgkqCIVVEATSTISqISEILCIGCGICVKKCPYDAIKI 83
Cdd:cd04410 57 PCVKACPTG-----AIYKDEDGIVL-IDEDKCIGCGSCVEACPYGAIVF 99
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
471-547 |
3.77e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 48.55 E-value: 3.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 471 ELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRfIMHAKKTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:PRK09493 136 ELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQD-LAEEGMTMVIVTHEIGFAEKVASRLIFIDK 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
112-323 |
4.01e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.57 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 112 RCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTiinhfrGSELQNYFtriLEDTLkcvikPQYVDQIPRAA 191
Cdd:PRK09544 28 KPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRI------GYVPQKLY---LDTTL-----PLTVNRFLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 192 KGTveknltRKHDndnLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIR 271
Cdd:PRK09544 94 PGT------KKED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLID 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 272 ERVSDTNY-VVVVEHDL----AVLDY---LSDFICClYGVPGVygVVTLPsgvrEGINMF 323
Cdd:PRK09544 165 QLRRELDCaVLMVSHDLhlvmAKTDEvlcLNHHICC-SGTPEV--VSLHP----EFISMF 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
365-504 |
4.05e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 365 TLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQkISPKSETTVRfmlhDKI-- 442
Cdd:PLN03130 632 TLSNINLDVPVGSL-----VAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVPQ-VSWIFNATVR----DNIlf 701
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 443 -----QNMYEHPQFKTDVMNPLmmeQLL---------DRNVKeLSGGELQRVALALCLGKTASLYLIDEPSAYLDS 504
Cdd:PLN03130 702 gspfdPERYERAIDVTALQHDL---DLLpggdlteigERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
216-302 |
4.34e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.49 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 216 ELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRE-RVSDTNYVVVVEHDLAVLDYLS 294
Cdd:PRK14258 139 EIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSlRLRSELTMVIVSHNLHQVSRLS 218
|
....*...
gi 17555800 295 DFICCLYG 302
Cdd:PRK14258 219 DFTAFFKG 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
378-544 |
4.48e-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: 50.01 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 378 FSDSEIIVMLGENGTGKTTMIKMMAGSLKP---------EDENTELPHV--SISYKPQ-KISPKSETTVRFMLhdkiqnM 445
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGLLPPtsgtvlvggKDIETNLDAVrqSLGMCPQhNILFHHLTVAEHIL------F 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 446 YEHPQFKTDVMNPLMMEQLLD-------RN--VKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKR 516
Cdd:TIGR01257 1027 YAQLKGRSWEEAQLEMEAMLEdtglhhkRNeeAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK 1106
|
170 180
....*....|....*....|....*...
gi 17555800 517 FimHAKKTAFVVEHDFIMATYLADRVVV 544
Cdd:TIGR01257 1107 Y--RSGRTIIMSTHHMDEADLLGDRIAI 1132
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
3-93 |
4.59e-06 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 49.25 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 3 RKGPLIKNNETDVPLRIAIVEKDRCKPKNCGLACKRACPVNRQGKQCIVVEATSTISQISEILCIGCGICVKKCPYDAIK 82
Cdd:COG4624 30 RIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIK 109
|
90
....*....|.
gi 17555800 83 IINLPANLANE 93
Cdd:COG4624 110 VDDGKAEIDEE 120
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
355-546 |
4.64e-06 |
|
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: 48.20 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 355 GNIKYPSMSktlgNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPEDEntelphvSISYKPQ-------KIS 427
Cdd:COG4778 20 GGKRLPVLD----GVSFSVAAGEC-----VALTGPSGAGKSTLLKCIYGNYLPDSG-------SILVRHDggwvdlaQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 428 PksettvRFMLH---DKI----QNMYEHPQFKTD--VMNPLMM------------EQLLDR-NVKE---------LSGGE 476
Cdd:COG4778 84 P------REILAlrrRTIgyvsQFLRVIPRVSALdvVAEPLLErgvdreeararaRELLARlNLPErlwdlppatFSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 477 LQRVALALCLGKTASLYLIDEPSAYLDSEQRlhaAKVIKrfIMHAKK---TAFV-VEHDF-IMATyLADRVVVFE 546
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANR---AVVVE--LIEEAKargTAIIgIFHDEeVREA-VADRVVDVT 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
114-294 |
4.70e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 48.27 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGN-FQKEQEWTTIINHFRgSELQNY-------FTRILED--TLKCVIKPQY 183
Cdd:PRK11629 35 GEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvIFNGQPMSKLSSAAK-AELRNQklgfiyqFHHLLPDftALENVAMPLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 184 VDQIPRAAkgtveknlTRKHDNDNLNSVidQMELRGllDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDvkqr 263
Cdd:PRK11629 114 IGKKKPAE--------INSRALEMLAAV--GLEHRA--NHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD---- 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 17555800 264 LKAAAIIRERVSDTNY-----VVVVEHDLAVLDYLS 294
Cdd:PRK11629 178 ARNADSIFQLLGELNRlqgtaFLVVTHDLQLAKRMS 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
114-259 |
4.77e-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: 47.96 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEqewTTIINHFRGSELQNYFTRI--------LEDTLKCVIKPQYVD 185
Cdd:cd03258 31 GEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD---GTDLTLLSGKELRKARRRIgmifqhfnLLSSRTVFENVALPL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 186 QIPRAAKGTVEKNltrkhdndnlnsVIDQMELRGLLDRE---IDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLD 259
Cdd:cd03258 108 EIAGVPKAEIEER------------VLELLELVGLEDKAdayPAQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
388-503 |
4.82e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.64 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 388 GENGTGKTTMIKMMAGSLKPEDENTELPHVSI-----SYKPQ--------KISPKseTTVR----FMLHDKIQNMYehpq 450
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlcTYQKQlcfvghrsGINPY--LTLRenclYDIHFSPGAVG---- 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 17555800 451 fKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLD 503
Cdd:PRK13540 108 -ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
359-587 |
5.10e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 48.58 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 359 YPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMikmmagslkpedenteLPHVSISYKPQK---------ISPK 429
Cdd:PRK13647 14 YKDGTKALKGLSLSIPEG-----SKTALLGPNGAGKSTL----------------LLHLNGIYLPQRgrvkvmgreVNAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 430 SETTVRFML-------HDKI-------------QNM----YEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALC 485
Cdd:PRK13647 73 NEKWVRSKVglvfqdpDDQVfsstvwddvafgpVNMgldkDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 486 LGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFimHAK-KTAFVVEHDFIMATYLADRVVVF-------EGQPSVkctaCK 557
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRL--HNQgKTVIVATHDVDLAAEWADQVIVLkegrvlaEGDKSL----LT 226
|
250 260 270
....*....|....*....|....*....|
gi 17555800 558 PQSLLEGMNRFLKMLDITFRRDQETYRPRI 587
Cdd:PRK13647 227 DEDIVEQAGLRLPLVAQIFEDLPELGQSKL 256
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
31-81 |
5.33e-06 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 43.70 E-value: 5.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 17555800 31 NCGlACKRACPVNRQGKQCIVVEAtstISQISEILCIGCGICVKKCPYDAI 81
Cdd:pfam13187 4 GCG-ACVAACPAGAIVPDLVGQTI---RGDIAGLACIGCGACVDACPRGAI 50
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
225-308 |
5.56e-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: 46.97 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 225 IDQLSGGELQRFAIAM----CCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSDFICCL 300
Cdd:cd03227 75 RLQLSGGEKELSALALilalASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
....*...
gi 17555800 301 YGVPGVYG 308
Cdd:cd03227 155 KVITGVYK 162
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
380-546 |
5.93e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 48.88 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 380 DSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISykpqKISPKSETTVR------------FMLHDKIQN--- 444
Cdd:PRK10070 53 EGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIA----KISDAELREVRrkkiamvfqsfaLMPHMTVLDnta 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 445 ---------MYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIK 515
Cdd:PRK10070 129 fgmelaginAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|.
gi 17555800 516 RFIMHAKKTAFVVEHDFIMATYLADRVVVFE 546
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
114-289 |
6.34e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 49.34 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQ-KEQEWTTIIN---------HFrGSELQNYftrileDTLKCVIKPQY 183
Cdd:PRK10535 34 GEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRvAGQDVATLDAdalaqlrreHF-GFIFQRY------HLLSHLTAAQN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 184 VdQIPRAAKGtVEKNLTRKHDNDNLNSVidqmelrGLLDR---EIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDV 260
Cdd:PRK10535 107 V-EVPAVYAG-LERKQRLLRAQELLQRL-------GLEDRveyQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180
....*....|....*....|....*....
gi 17555800 261 KQRLKAAAIIRERVSDTNYVVVVEHDLAV 289
Cdd:PRK10535 178 HSGEEVMAILHQLRDRGHTVIIVTHDPQV 206
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
437-544 |
7.04e-06 |
|
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: 47.61 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 437 MLHDKIQNMYEhpQFKTDVMnplmmeqllDRNVKeLSGGELQRVALALCLGKTASLYLIDEPSAYLDS--EQRLHAA--K 512
Cdd:cd03253 115 QIHDKIMRFPD--GYDTIVG---------ERGLK-LSGGEKQRVAIARAILKNPPILLLDEATSALDThtEREIQAAlrD 182
|
90 100 110
....*....|....*....|....*....|....
gi 17555800 513 VIKRfimhakKTAFVVEHDF--IMAtylADRVVV 544
Cdd:cd03253 183 VSKG------RTTIVIAHRLstIVN---ADKIIV 207
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
465-540 |
7.15e-06 |
|
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: 49.24 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 465 LDRNVKELSGGELQRVALALCLGKTA---SLYLIDEPSAYLDSEQRLHAAKVIKRFImHAKKTAFVVEH--DFI-MATYL 538
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVLQRLV-DKGNTVVVIEHnlDVIkTADYI 901
|
..
gi 17555800 539 AD 540
Cdd:TIGR00630 902 ID 903
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
6-84 |
7.77e-06 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 47.87 E-value: 7.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 6 PLIKNNETDVPLRIAIVEKDRCKpkNCGLaCKRACPVNrqgkqcIVVEATSTISQISEILCIGCGICVKKCPYDAIKII 84
Cdd:PRK06991 66 PLDPANGVERPRAVAVIDEQLCI--GCTL-CMQACPVD------AIVGAPKQMHTVLADLCTGCDLCVPPCPVDCIDMV 135
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
462-550 |
7.81e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.82 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 462 EQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRfIMHAKKTAFVVEHdfIM---ATYl 538
Cdd:PRK13649 136 ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKK-LHQSGMTIVLVTH--LMddvANY- 211
|
90
....*....|....*....
gi 17555800 539 ADRVVVFE-------GQPS 550
Cdd:PRK13649 212 ADFVYVLEkgklvlsGKPK 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
110-286 |
8.04e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.40 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 110 TPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIInhFRGSELQNYftriledtlkcviKPQ------- 182
Cdd:PRK10247 29 SLRAGEFKLITGPSGCGKSTLLKIVASLISPTSG---------TLL--FEGEDISTL-------------KPEiyrqqvs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 183 YVDQIPRAAKGTVEKNLT-------RKHDNDNLNSVIDQMEL-RGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEP 254
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIfpwqirnQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190
....*....|....*....|....*....|...
gi 17555800 255 SSYLDVKQRLKAAAIIRERVSDTNYVVV-VEHD 286
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLwVTHD 197
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
188-301 |
8.27e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.73 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 188 PRAAKGTVEKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAA 267
Cdd:PRK14246 114 PLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIE 193
|
90 100 110
....*....|....*....|....*....|....
gi 17555800 268 AIIRERVSDTNyVVVVEHDLAVLDYLSDFICCLY 301
Cdd:PRK14246 194 KLITELKNEIA-IVIVSHNPQQVARVADYVAFLY 226
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
378-507 |
8.53e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 378 FSDSEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSI--------SYKPQKISPKSETTVrfmlhdkiqnmYEHP 449
Cdd:PRK13541 23 FLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniakpycTYIGHNLGLKLEMTV-----------FENL 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 450 QFKTDVMNP----------LMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQR 507
Cdd:PRK13541 92 KFWSEIYNSaetlyaaihyFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
31-80 |
9.65e-06 |
|
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: 42.90 E-value: 9.65e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 17555800 31 NCGlACKRACPVNRQGKQCIVVEATSTISQISEILCIGCGICVKKCPYDA 80
Cdd:pfam12838 3 GCG-ACVAACPVGAITLDEVGEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
66-85 |
1.00e-05 |
|
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: 45.08 E-value: 1.00e-05
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
114-263 |
1.01e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.74 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFqkeqewttIINHFRGSELQNYFTRILEDTLKCVIKPQYvdQIpraAKG 193
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI--------IIDGVDITDKKVKLSDIRKKVGLVFQYPEY--QL---FEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TVEKNLTRKHDNDNL------NSVIDQMELRGL-----LDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQ 262
Cdd:PRK13637 100 TIEKDIAFGPINLGLseeeieNRVKRAMNIVGLdyedyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
.
gi 17555800 263 R 263
Cdd:PRK13637 180 R 180
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
114-287 |
1.01e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.20 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIIN-HFRGSELQNY-------FTRI-LEDTLKCVIKpqyv 184
Cdd:PRK10895 29 GEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYlpqeasiFRRLsVYDNLMAVLQ---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 185 dqipraakgtVEKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRL 264
Cdd:PRK10895 105 ----------IRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180
....*....|....*....|....
gi 17555800 265 KAAAIIrERVSDTNY-VVVVEHDL 287
Cdd:PRK10895 175 DIKRII-EHLRDSGLgVLITDHNV 197
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
465-549 |
1.13e-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: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 465 LDRNVKELSGGELQRVALALCLGK--TASLYLIDEPSAYLDSEQRLHAAKVIKRfIMHAKKTAFVVEHDFIMATyLADRV 542
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSglTGVLYVLDEPSIGLHQRDNRRLINTLKR-LRDLGNTLIVVEHDEDTIR-AADYV 559
|
90 100
....*....|....*....|
gi 17555800 543 -------------VVFEGQP 549
Cdd:TIGR00630 560 idigpgagehggeVVASGTP 579
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
102-287 |
1.15e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.49 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPN---------LG-NFQKEQEWTT-----II-----NHFRGS 161
Cdd:PRK13640 27 SFSIPR------GSWTALIGHNGSGKSTISKLINGLLLPDdnpnskitvDGiTLTAKTVWDIrekvgIVfqnpdNQFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 162 ELQNYFTRILEDTlkcvikpqyvdQIPRAAKGTVeknltrkhdndnLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMC 241
Cdd:PRK13640 101 TVGDDVAFGLENR-----------AVPRPEMIKI------------VRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17555800 242 CVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVV-VEHDL 287
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVIsITHDI 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
110-267 |
1.17e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.42 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 110 TPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIIN-----HFRGSELQN--YFTRILEDTLKcVIKPQ 182
Cdd:PRK13657 357 EAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTraslrRNIAVVFQDagLFNRSIEDNIR-VGRPD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 183 YVD-QIPRAAKGT-----VEKNLtrkhdnDNLNSVIDQmelRGLldreidQLSGGELQRFAIAMCCVQKADVYMFDEPSS 256
Cdd:PRK13657 436 ATDeEMRAAAERAqahdfIERKP------DGYDTVVGE---RGR------QLSGGERQRLAIARALLKDPPILILDEATS 500
|
170
....*....|...
gi 17555800 257 YLDV--KQRLKAA 267
Cdd:PRK13657 501 ALDVetEAKVKAA 513
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
32-90 |
1.19e-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: 47.30 E-value: 1.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17555800 32 CGLaCKRACPVNrqgkqCIVVEATS--TIsqISEiLCIGCGICVKKCPYDAIKIINLPANL 90
Cdd:COG2878 142 CGD-CIKACPFD-----AIVGAAKGmhTV--DED-KCTGCGLCVEACPVDCIEMVPVSPTV 193
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
371-544 |
1.32e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 47.39 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 371 LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPedenTElPHVSI-SYKPQK--------IS-------------P 428
Cdd:COG4586 43 FTIEPG-----EIVGFIGPNGAGKSTTIKMLTGILVP----TS-GEVRVlGYVPFKrrkefarrIGvvfgqrsqlwwdlP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 429 KSETtvrFMLHDKIqnmYEHP--QFK------TDVMNplmMEQLLDRNVKELSGGelQR----VALALcLGKTASLYLiD 496
Cdd:COG4586 113 AIDS---FRLLKAI---YRIPdaEYKkrldelVELLD---LGELLDTPVRQLSLG--QRmrceLAAAL-LHRPKILFL-D 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17555800 497 EPSAYLDseqrLHAAKVIKRFI--MHAKK--TAFVVEHDfiMA--TYLADRVVV 544
Cdd:COG4586 180 EPTIGLD----VVSKEAIREFLkeYNRERgtTILLTSHD--MDdiEALCDRVIV 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
362-544 |
1.37e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.10 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 362 MSKTLGNFH------LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPeDENTelphVSISYKPQKI-SPK----- 429
Cdd:COG3845 11 ITKRFGGVVanddvsLTVRPG-----EIHALLGENGAGKSTLMKILYGLYQP-DSGE----ILIDGKPVRIrSPRdaial 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 430 ------------------------SETTVRFML-----HDKIQNMYEHPQFKTDvmnplmmeqlLDRNVKELSGGELQRV 480
Cdd:COG3845 81 gigmvhqhfmlvpnltvaenivlgLEPTKGGRLdrkaaRARIRELSERYGLDVD----------PDAKVEDLSVGEQQRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 481 AL--ALCLGktASLyLI-DEPSAYLDSEQRLHAAKVIKRFImHAKKTAFVVEHDF--IMAtyLADRVVV 544
Cdd:COG3845 151 EIlkALYRG--ARI-LIlDEPTAVLTPQEADELFEILRRLA-AEGKSIIFITHKLreVMA--IADRVTV 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
371-543 |
1.53e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 46.89 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 371 LDVEAGDfsdseIIVMLGENGTGKTTMIKMMAGSLKPEDEntelphvSISYKPQKISPKSETTVRFMLHDKIQ------- 443
Cdd:PRK10619 26 LQANAGD-----VISIIGSSGSGKSTFLRCINFLEKPSEG-------SIVVNGQTINLVRDKDGQLKVADKNQlrllrtr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 444 --------NMYEHPQFKTDVMN-PLMMEQLLDRNVKE----------------------LSGGELQRVALALCLGKTASL 492
Cdd:PRK10619 94 ltmvfqhfNLWSHMTVLENVMEaPIQVLGLSKQEAREravkylakvgideraqgkypvhLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17555800 493 YLIDEPSAYLDSEQRLHAAKVIKRfIMHAKKTAFVVEHDFIMATYLADRVV 543
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
366-504 |
1.59e-05 |
|
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: 46.50 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLkPEDENTE----------LPHV---SISYKPQKISPKSET 432
Cdd:cd03234 23 LNDVSLHVESG-----QVMAILGSSGSGKTTLLDAISGRV-EGGGTTSgqilfngqprKPDQfqkCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 433 TVR----FMLHDKIQNMYEHPQFK----TDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDS 504
Cdd:cd03234 97 TVRetltYTAILRLPRKSSDAIRKkrveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
114-288 |
1.64e-05 |
|
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: 46.71 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTII--NHFR---GSELQN--YFTRILEDTLKCVIKPQYVDQ 186
Cdd:cd03252 28 GEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdpAWLRrqvGVVLQEnvLFNRSIRDNIALADPGMSMER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 187 IPRAAKgtveknLTRKHDndnlnsVIDQMEL--RGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRl 264
Cdd:cd03252 108 VIEAAK------LAGAHD------FISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE- 174
|
170 180
....*....|....*....|....*.
gi 17555800 265 kaAAIIR--ERVSDTNYVVVVEHDLA 288
Cdd:cd03252 175 --HAIMRnmHDICAGRTVIIIAHRLS 198
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
368-548 |
1.66e-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: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 368 NFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKP---------ED----------------ENTELPHVSIsyk 422
Cdd:COG3840 17 RFDLTIAAG-----ERVAILGPSGAGKSTLLNLIAGFLPPdsgrilwngQDltalppaerpvsmlfqENNLFPHLTV--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 423 pqkispksETTVRFMLHDKIQnmYEHPQfKTDVMNplMMEQ-----LLDRNVKELSGGELQRVALALCLGKTASLYLIDE 497
Cdd:COG3840 89 --------AQNIGLGLRPGLK--LTAEQ-RAQVEQ--ALERvglagLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17555800 498 PSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVV-VFEGQ 548
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLlVADGR 207
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
1-85 |
1.66e-05 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 46.64 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 1 MSRKGPLIKNNETDVPLRIAIVEKDRCKPKNCGLACKRACPVNRQGKQCIVVEATstisqISEILCIGCGICVKKCPYDA 80
Cdd:COG1145 124 LVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAV-----IDAEKCIGCGLCVKVCPTGA 198
|
....*
gi 17555800 81 IKIIN 85
Cdd:COG1145 199 IRLKD 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
114-301 |
1.75e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 47.04 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQ----------KEQEWTTIINH----FRGSELQNYFTRILEDTlkcVI 179
Cdd:PRK13643 32 GSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvsstsKQKEIKPVRKKvgvvFQFPESQLFEETVLKDV---AF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 180 KPQYVDqiprAAKGTVEKNLTRKhdndnlnsvidqMELRGL----LDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPS 255
Cdd:PRK13643 109 GPQNFG----IPKEKAEKIAAEK------------LEMVGLadefWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17555800 256 SYLDVKQRLKAAAIIRERVSDTNYVVVVEHdlaVLDYLSDFICCLY 301
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSGQTVVLVTH---LMDDVADYADYVY 215
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
19-85 |
1.75e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 47.55 E-value: 1.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 19 IAIVEKDRCKpkNCGLaCKRACPVNrqgkqcIVVEATSTISQISEILCIGCGICVKKCPYDAIKIIN 85
Cdd:COG1148 490 VAEVDPEKCT--GCGR-CVEVCPYG------AISIDEKGVAEVNPALCKGCGTCAAACPSGAISLKG 547
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
356-547 |
1.83e-05 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 46.45 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 356 NIKYPSMSKTLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPED-----ENTELPHVSISYKPQKISPKS 430
Cdd:cd03254 9 NFSYDEKKPVLKDINFSIKPGET-----VAIVGPTGAGKTTLINLLMRFYDPQKgqiliDGIDIRDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 431 ETTvrFMLHDKIQN--MYEHPQFKTDV---------MNPLMM--EQLLDRNVKE----LSGGELQRVALALCLGKTASLY 493
Cdd:cd03254 84 QDT--FLFSGTIMEniRLGRPNATDEEvieaakeagAHDFIMklPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 494 LIDEPSAYLDS--EQRLHAAkvIKRfIMHaKKTAFVVEHDfiMATYL-ADRVVVFEG 547
Cdd:cd03254 162 ILDEATSNIDTetEKLIQEA--LEK-LMK-GRTSIIIAHR--LSTIKnADKILVLDD 212
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
65-85 |
1.88e-05 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 42.79 E-value: 1.88e-05
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
102-260 |
2.05e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLhrlptPRCGEVlGLVGTNGIGKSTALKILAGKQKPNLGNFqkeqewttiinhfrgselqnyftrILEDTlkcvIKP 181
Cdd:PRK11819 344 SFSL-----PPGGIV-GIIGPNGAGKSTLFKMITGQEQPDSGTI------------------------KIGET----VKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVDQipraakgtveknlTRKH--DNDNLNSVI----DQMELrGllDREI--------------DQ------LSGGELQR 235
Cdd:PRK11819 390 AYVDQ-------------SRDAldPNKTVWEEIsgglDIIKV-G--NREIpsrayvgrfnfkggDQqkkvgvLSGGERNR 453
|
170 180
....*....|....*....|....*
gi 17555800 236 FAIAMCCVQKADVYMFDEPSSYLDV 260
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
462-546 |
2.10e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.55 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 462 EQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRfiMHAKK--TAFVVEHDFIMATYLA 539
Cdd:PRK13634 136 EELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYK--LHKEKglTTVLVTHSMEDAARYA 213
|
....*..
gi 17555800 540 DRVVVFE 546
Cdd:PRK13634 214 DQIVVMH 220
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
32-84 |
2.29e-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: 319872 [Multi-domain] Cd Length: 130 Bit Score: 44.10 E-value: 2.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 32 CGLA-CKRACPVN---RQGKQCIVVeatstisqISEILCIGCGICVKKCPYDAIKII 84
Cdd:cd10550 52 CEDApCVEACPVGaisRDEETGAVV--------VDEDKCIGCGMCVEACPFGAIRVD 100
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
376-517 |
2.32e-05 |
|
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: 45.62 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 376 GDFSDSEIIVMLGENGTGKTTMIKMMAGSLKPedentelPHVS--ISYKPQKISPKSettvrfmLHDKI----QNMYEHP 449
Cdd:cd03213 30 GKAKPGELTAIMGPSGAGKSTLLNALAGRRTG-------LGVSgeVLINGRPLDKRS-------FRKIIgyvpQDDILHP 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 450 QFkTdVMNPLMMEQLLdrnvKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRF 517
Cdd:cd03213 96 TL-T-VRETLMFAAKL----RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL 157
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
60-82 |
2.36e-05 |
|
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: 41.46 E-value: 2.36e-05
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
383-547 |
2.38e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.41 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 383 IIVMLGENGTGKTTMIKMMAG---------SLKPEDENTELPHVSISYKPQkiSPKSETTVRFMLHDKIQ-NMYEH---- 448
Cdd:PRK15056 35 IAALVGVNGSGKSTLFKALMGfvrlasgkiSILGQPTRQALQKNLVAYVPQ--SEEVDWSFPVLVEDVVMmGRYGHmgwl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 449 -------PQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRlhaAKVIK--RFIM 519
Cdd:PRK15056 113 rrakkrdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE---ARIISllRELR 189
|
170 180
....*....|....*....|....*...
gi 17555800 520 HAKKTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:PRK15056 190 DEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
366-551 |
2.40e-05 |
|
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: 45.60 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGslkpeDENTELPHVSISYKPQKISpKSETTVR-----FMLhd 440
Cdd:cd03217 16 LKGVNLTIKKG-----EVHALMGPNGSGKSTLAKTIMG-----HPKYEVTEGEILFKGEDIT-DLPPEERarlgiFLA-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 441 kIQNMYEHPQFKtdvmnplmMEQLLdRNVKE-LSGGELQRVALALCLGKTASLYLIDEPSAYLDseqrLHAAKVIKRFIM 519
Cdd:cd03217 83 -FQYPPEIPGVK--------NADFL-RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD----IDALRLVAEVIN 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17555800 520 H---AKKTAFVVEH-----DFIMATY---LADRVVVFEGQPSV 551
Cdd:cd03217 149 KlreEGKSVLIITHyqrllDYIKPDRvhvLYDGRIVKSGDKEL 191
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
366-572 |
2.61e-05 |
|
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: 45.94 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPED-----ENTELPHVSISYKPQKISPKSETTVRF--ML 438
Cdd:cd03252 18 LDNISLRIKPG-----EVVGIVGRSGSGKSTLTKLIQRFYVPENgrvlvDGHDLALADPAWLRRQVGVVLQENVLFnrSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 439 HDKIQNMYEHPQFKTDVMN-------------PLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSE 505
Cdd:cd03252 93 RDNIALADPGMSMERVIEAaklagahdfiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17555800 506 qrlhAAKVIKRFiMH---AKKTAFVVEHDfIMATYLADRVVVFEGQPSVKCTacKPQSLL--EGMNRFLKML 572
Cdd:cd03252 173 ----SEHAIMRN-MHdicAGRTVIIIAHR-LSTVKNADRIIVMEKGRIVEQG--SHDELLaeNGLYAYLYQL 236
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
371-543 |
2.74e-05 |
|
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: 45.73 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 371 LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPeDENTelphVSISYKPQKISPKS-------------ETTVRFM 437
Cdd:cd03269 21 FSVEKG-----EIFGLLGPNGAGKTTTIRMILGIILP-DSGE----VLFDGKPLDIAARNrigylpeerglypKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 438 LH--DKIQNMYEHPQFK--TDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEqrlhAAKV 513
Cdd:cd03269 91 LVylAQLKGLKKEEARRriDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV----NVEL 166
|
170 180 190
....*....|....*....|....*....|...
gi 17555800 514 IKRFIMHAK---KTAFVVEHDFIMATYLADRVV 543
Cdd:cd03269 167 LKDVIRELAragKTVILSTHQMELVEELCDRVL 199
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
364-550 |
3.02e-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: 46.72 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 364 KTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPE-DENTELPHVSISYKPQKISPKS------------ 430
Cdd:TIGR03269 14 EVLKNISFTIEEG-----EVLGILGRSGAGKSVLMHVLRGMDQYEpTSGRIIYHVALCEKCGYVERPSkvgepcpvcggt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 431 -----------ETTVRFMLHDKIQNM-------YEHPQFKTDVMNPL-----MMEQLLDRNVK----------------E 471
Cdd:TIGR03269 89 lepeevdfwnlSDKLRRRIRKRIAIMlqrtfalYGDDTVLDNVLEALeeigyEGKEAVGRAVDliemvqlshrithiarD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 472 LSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEH------DFI-MATYLADRVVV 544
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevieDLSdKAIWLENGEIK 248
|
....*.
gi 17555800 545 FEGQPS 550
Cdd:TIGR03269 249 EEGTPD 254
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
119-292 |
3.21e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.38 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 119 LVGTNGIGKSTALKILAGKQKPNLGNFQKEQewTTIINHFRGSELQNY-FTRILEDTLKCVIKPQYVDQIPRAA--KGTV 195
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGD--IYIGDKKNNHELITNpYSKKIKNFKELRRRVSMVFQFPEYQlfKDTI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 196 EKNLT------RKHDNDNLNSVIDQMELRGL----LDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLK 265
Cdd:PRK13631 135 EKDIMfgpvalGVKKSEAKKLAKFYLNKMGLddsyLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHE 214
|
170 180 190
....*....|....*....|....*....|.
gi 17555800 266 AAAIIRERVSDTNYVVVV----EHDLAVLDY 292
Cdd:PRK13631 215 MMQLILDAKANNKTVFVIthtmEHVLEVADE 245
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
20-82 |
3.91e-05 |
|
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: 41.50 E-value: 3.91e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 20 AIVEKDRCKpkNCGLaCKRACPVNrqGKQCIVVEATSTISQISEiLCIGCGICVKKCP-YDAIK 82
Cdd:pfam14697 1 ARIDEDTCI--GCGK-CYIACPDT--SHQAIVGDGKRHHTVIED-ECTGCNLCVSVCPvDDCIT 58
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
366-546 |
4.31e-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: 45.30 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMM-------AGSLkpEDENTELPHVSISYKPQKISPKSETTVRF-- 436
Cdd:cd03251 18 LRDISLDIPAG-----ETVALVGPSGSGKSTLVNLIprfydvdSGRI--LIDGHDVRDYTLASLRRQIGLVSQDVFLFnd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 437 -------------------------MLHDKIQNMYEhpQFKTDVMnplmmeqllDRNVKeLSGGELQRVALALCLGKTAS 491
Cdd:cd03251 91 tvaeniaygrpgatreeveeaaraaNAHEFIMELPE--GYDTVIG---------ERGVK-LSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 492 LYLIDEPSAYLDSEqrlhAAKVIKRFIMH--AKKTAFVVEHDF--IMAtylADRVVVFE 546
Cdd:cd03251 159 ILILDEATSALDTE----SERLVQAALERlmKNRTTFVIAHRLstIEN---ADRIVVLE 210
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
227-288 |
4.36e-05 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 45.47 E-value: 4.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17555800 227 QLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLA 288
Cdd:PRK09493 136 ELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
466-545 |
4.43e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 466 DRNV----KELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDfIMATYLADR 541
Cdd:PTZ00265 1349 DTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR-IASIKRSDK 1427
|
....
gi 17555800 542 VVVF 545
Cdd:PTZ00265 1428 IVVF 1431
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
112-290 |
4.94e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 45.36 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 112 RCGEVLGLVGTNGIGKSTALKILAGKQKP----------NLGNFQKEQEWTTIInhfrGSELQNYFTriledtlkcvikp 181
Cdd:PRK13644 26 KKGEYIGIIGKNGSGKSTLALHLNGLLRPqkgkvlvsgiDTGDFSKLQGIRKLV----GIVFQNPET------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVDQipraakgTVEKNLTRKHDNDNLNSVidqmELRGLLDREIDQ-------------LSGGELQRFAIAMCCVQKADV 248
Cdd:PRK13644 89 QFVGR-------TVEEDLAFGPENLCLPPI----EIRKRVDRALAEiglekyrhrspktLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17555800 249 YMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVL 290
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL 199
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
357-505 |
5.14e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 45.39 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 357 IKYPSMSKTLgNFHLDVEAGDF--SDSEIIVMLGENGTGKTTMIKMMAGsLKPEDENTElPHVSISYKPQKISPKSETTV 434
Cdd:PRK09984 5 IRVEKLAKTF-NQHQALHAVDLniHHGEMVALLGPSGSGKSTLLRHLSG-LITGDKSAG-SHIELLGRTVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 435 R------------FMLHDKIQNM-------------------YEHPQFKTDVMNPLM---MEQLLDRNVKELSGGELQRV 480
Cdd:PRK09984 82 RksrantgyifqqFNLVNRLSVLenvligalgstpfwrtcfsWFTREQKQRALQALTrvgMVHFAHQRVSTLSGGQQQRV 161
|
170 180
....*....|....*....|....*
gi 17555800 481 ALALCLGKTASLYLIDEPSAYLDSE 505
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPE 186
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
114-292 |
5.68e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 45.00 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALK----ILAGKQKPN-----LGN-----------FQKEQEWTTIInhFRGSELQNYFTrILED 173
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRhlsgLITGDKSAGshielLGRtvqregrlardIRKSRANTGYI--FQQFNLVNRLS-VLEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 174 TLKCVI--KPQY---VDQIPRAAKGTVEKNLTRkhdndnlnsvidqMELRGLLDREIDQLSGGELQRFAIAMCCVQKADV 248
Cdd:PRK09984 107 VLIGALgsTPFWrtcFSWFTREQKQRALQALTR-------------VGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17555800 249 YMFDEPSSYLDVkqrlKAAAIIRERVSDTNY-----VVVVEHDlavLDY 292
Cdd:PRK09984 174 ILADEPIASLDP----ESARIVMDTLRDINQndgitVVVTLHQ---VDY 215
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
112-295 |
6.59e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.08 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 112 RCGEVLGLVGTNGIGKS----TALKIL-------AGK----QKPNLGNFQKEQEWTTIINHFRGS--ELQNYFTRILEdT 174
Cdd:PRK10418 27 QRGRVLALVGGSGSGKSltcaAALGILpagvrqtAGRvlldGKPVAPCALRGRKIATIMQNPRSAfnPLHTMHTHARE-T 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 175 LKCVIKPQYVDQIPRAAKGTVEKNLTRkhdndnlnsvidqmelrgLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEP 254
Cdd:PRK10418 106 CLALGKPADDATLTAALEAVGLENAAR------------------VLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17555800 255 SSYLDVKQRLKA----AAIIRERVSDtnyVVVVEHDLAVLDYLSD 295
Cdd:PRK10418 168 TTDLDVVAQARIldllESIVQKRALG---MLLVTHDMGVVARLAD 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
114-287 |
6.62e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.08 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIINHFrgsELQNYFTRILEDTLKCVIKPQYVDQIpraAKG 193
Cdd:PRK13642 33 GEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVW---NLRRKIGMVFQNPDNQFVGATVEDDV---AFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TVEKNLTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIREr 273
Cdd:PRK13642 107 MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE- 185
|
170
....*....|....*.
gi 17555800 274 VSDTNYVVV--VEHDL 287
Cdd:PRK13642 186 IKEKYQLTVlsITHDL 201
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
465-546 |
7.33e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 45.72 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 465 LDRNVKE----LSGGELQRVALALCLGKTASLYLIDEPSAYLDS--EQRLHAAkvIKRfIMHAkKTAFVVEHDfiMATYL 538
Cdd:PRK13657 461 YDTVVGErgrqLSGGERQRLAIARALLKDPPILILDEATSALDVetEAKVKAA--LDE-LMKG-RTTFIIAHR--LSTVR 534
|
....*....
gi 17555800 539 -ADRVVVFE 546
Cdd:PRK13657 535 nADRILVFD 543
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
356-550 |
7.94e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 44.84 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 356 NIKYPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQKI--------- 426
Cdd:PRK13636 12 NYNYSDGTHALKGININIKKG-----EVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLmklresvgm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 427 ---SPKSE-------TTVRF------MLHDKIQNMYEHPQFKTDVmnplmmEQLLDRNVKELSGGELQRVALALCLGKTA 490
Cdd:PRK13636 87 vfqDPDNQlfsasvyQDVSFgavnlkLPEDEVRKRVDNALKRTGI------EHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 491 SLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRV-------VVFEGQPS 550
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVfvmkegrVILQGNPK 227
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
228-295 |
8.27e-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: 45.77 E-value: 8.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 228 LSGGELQRFAIAMCCVQKAD---VYMFDEPSSYL---DVKQRLKaaaIIRERVSDTNYVVVVEHDLAVL---DYLSD 295
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfdDIKKLLE---VLQRLVDKGNTVVVIEHNLDVIktaDYIID 903
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
114-302 |
8.65e-05 |
|
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: 44.60 E-value: 8.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIInhFRGSELQNYFTRILEDTLKCVIkpQYVDQIPRAakg 193
Cdd:cd03295 27 GEFLVLIGPSGSGKTTTMKMINRLIEPTSG---------EIF--IDGEDIREQDPVELRRKIGYVI--QQIGLFPHM--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TVEKNLT------------RKHDNDNLNSVIDqMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLD-- 259
Cdd:cd03295 91 TVEENIAlvpkllkwpkekIRERADELLALVG-LDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDpi 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17555800 260 VKQRLKAAAI-IRERVSDTnyVVVVEHDL--AVLdyLSDFICCLYG 302
Cdd:cd03295 170 TRDQLQEEFKrLQQELGKT--IVFVTHDIdeAFR--LADRIAIMKN 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
114-295 |
8.72e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKS-TALKILAGKQKPNLGNFQKEqewttIInhFRGSELQNyftrILEDTLKCVIKPQ--YVDQIPRA 190
Cdd:PRK15134 35 GETLALVGESGSGKSvTALSILRLLPSPPVVYPSGD-----IR--FHGESLLH----ASEQTLRGVRGNKiaMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 191 AKG---TVEKNLT----------RKHDNDNLNSVIDQMELRGLLDREID---QLSGGELQRFAIAMCCVQKADVYMFDEP 254
Cdd:PRK15134 104 SLNplhTLEKQLYevlslhrgmrREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEP 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17555800 255 SSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDLAVLDYLSD 295
Cdd:PRK15134 184 TTALDVSVQAQILQLLRELQQELNMgLLFITHNLSIVRKLAD 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
114-298 |
9.39e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 45.20 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQkeqewttiINhfrGSELQNYftriLEDTLK---CVIkPQYVDQIpra 190
Cdd:PRK11160 366 GEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL--------LN---GQPIADY----SEAALRqaiSVV-SQRVHLF--- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 191 aKGTVEKNLT----RKHDnDNLNSVIDQMELRGLLDRE--ID--------QLSGGELQRFAIAMCCVQKADVYMFDEPSS 256
Cdd:PRK11160 427 -SATLRDNLLlaapNASD-EALIEVLQQVGLEKLLEDDkgLNawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17555800 257 YLDVKQRLKAAAIIRERVSDTNyVVVVEHDLAVLDYLsDFIC 298
Cdd:PRK11160 505 GLDAETERQILELLAEHAQNKT-VLMITHRLTGLEQF-DRIC 544
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
35-83 |
9.73e-05 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 43.40 E-value: 9.73e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 17555800 35 ACKRACPVNrqgkqCIVVEATSTISQISEiLCIGCGICVKKCPYDAIKI 83
Cdd:COG0437 67 PCVKVCPTG-----ATYKREDGIVLVDYD-KCIGCRYCVAACPYGAPRF 109
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
465-531 |
1.05e-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: 44.14 E-value: 1.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 465 LDRNVKELSGGELQRVALALCLGKTAS---LYLIDEPSAYLDSEQRLHAAKVIKRFImHAKKTAFVVEHD 531
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLV-DKGNTVVVIEHN 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
194-260 |
1.39e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.48 E-value: 1.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TVEKNLT---RKHDNDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDV 260
Cdd:PRK11144 92 KVRGNLRygmAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
66-84 |
1.53e-04 |
|
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: 40.11 E-value: 1.53e-04
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
216-302 |
1.57e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 43.75 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 216 ELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNyVVVVEHDLAVLDYLSD 295
Cdd:PRK14247 135 EVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMT-IVLVTHFPQQAARISD 213
|
....*..
gi 17555800 296 FICCLYG 302
Cdd:PRK14247 214 YVAFLYK 220
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
66-85 |
1.59e-04 |
|
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: 43.69 E-value: 1.59e-04
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
114-302 |
1.60e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.96 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTAL-----------KILAGKQKPNLGNFQK--EQEWTTIInhfrGSELqnyfTRILEDTLKCvIK 180
Cdd:PRK11022 33 GEVVGIVGESGSGKSVSSlaimglidypgRVMAEKLEFNGQDLQRisEKERRNLV----GAEV----AMIFQDPMTS-LN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 181 PQYVD--QIPRAAKgtVEKNLTRKHDNDNlnsVIDQMELRGL------LDREIDQLSGGELQRFAIAMCCVQKADVYMFD 252
Cdd:PRK11022 104 PCYTVgfQIMEAIK--VHQGGNKKTRRQR---AIDLLNQVGIpdpasrLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17555800 253 EPSSYLDVKQRLKAAAIIRERVSDTNY-VVVVEHDLAVLDYLSDFICCLYG 302
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMaLVLITHDLALVAEAAHKIIVMYA 229
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
228-295 |
1.60e-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: 43.76 E-value: 1.60e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 228 LSGGELQRFAIAmCCVQKAD----VYMFDEPSSYL---DVKQRLkaaAIIRERVSDTNYVVVVEHDLAVL---DYLSD 295
Cdd:cd03271 170 LSGGEAQRIKLA-KELSKRStgktLYILDEPTTGLhfhDVKKLL---EVLQRLVDKGNTVVVIEHNLDVIkcaDWIID 243
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
371-547 |
1.71e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 43.53 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 371 LDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPedenTElPHVSISykpQKISP--------KSETTVRfmlhdki 442
Cdd:COG1134 47 FEVERG-----ESVGIIGRNGAGKSTLLKLIAGILEP----TS-GRVEVN---GRVSAllelgagfHPELTGR------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 443 QNMYehpqfktdvMNPLMM--------------------EQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYL 502
Cdd:COG1134 107 ENIY---------LNGRLLglsrkeidekfdeivefaelGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17555800 503 DSEQRLHAAKVIKRFIMHAkKTAFVVEHDFIMATYLADRVVVFEG 547
Cdd:COG1134 178 DAAFQKKCLARIRELRESG-RTVIFVSHSMGAVRRLCDRAIWLEK 221
|
|
| PRK14993 |
PRK14993 |
tetrathionate reductase subunit TtrB; |
36-115 |
1.77e-04 |
|
tetrathionate reductase subunit TtrB;
Pssm-ID: 184955 [Multi-domain] Cd Length: 244 Bit Score: 43.32 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 36 CKRACPVNR--QGKQCIVVeatstisqISEILCIGCGICVKKCPYDAIKIinlpanlaNETTHRYSQNSFKLHRLPT--- 110
Cdd:PRK14993 108 CVPVCPVQAtfQREDGIVV--------VDNKRCVGCAYCVQACPYDARFI--------NHETQTADKCTFCVHRLEAgll 171
|
....*
gi 17555800 111 PRCGE 115
Cdd:PRK14993 172 PACVE 176
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
31-87 |
1.80e-04 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 43.77 E-value: 1.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 31 NCGLaCKRACPVnrqgkQCIVVEatSTISQISEILCIGCGICVKKCPYDAIKIINLP 87
Cdd:PRK07118 217 GCGK-CVKACPA-----GAITME--NNLAVIDQEKCTSCGKCVEKCPTKAIRILNKP 265
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
102-259 |
1.81e-04 |
|
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: 43.79 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIINHFRGSEL---------QNY----FT 168
Cdd:cd03294 44 SLDVRE------GEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkismvfQSFallpHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 169 RILEDT---LKCvikpQYVDQIPRAAKGTveknltrkhdndnlnSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQK 245
Cdd:cd03294 118 TVLENVafgLEV----QGVPRAEREERAA---------------EALELVGLEGWEHKYPDELSGGMQQRVGLARALAVD 178
|
170
....*....|....
gi 17555800 246 ADVYMFDEPSSYLD 259
Cdd:cd03294 179 PDILLMDEAFSALD 192
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
464-548 |
1.82e-04 |
|
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: 42.80 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 464 LLDRNVKE-------LSGGELQRVALALCLGKTASLYLIDEPSAYLDseqrLHAAKVIKRFIMHAKK--TAFVV---EHD 531
Cdd:cd03215 90 VLDLSVAEnialsslLSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VGAKAEIYRLIRELADagKAVLLissELD 165
|
90
....*....|....*...
gi 17555800 532 FIMAtyLADRVVVF-EGQ 548
Cdd:cd03215 166 ELLG--LCDRILVMyEGR 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
114-274 |
1.90e-04 |
|
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: 41.98 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGkqkpnlgnfqkeqewttiinhfrgselqnyftriledtlkcvikpqyvdQIPRAAKG 193
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAR-------------------------------------------------ELGPPGGG 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TVEKNLtrkhdnDNLNSVIDQMELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRER 273
Cdd:smart00382 33 VIYIDG------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELR 106
|
.
gi 17555800 274 V 274
Cdd:smart00382 107 L 107
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
351-506 |
2.10e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.00 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 351 IKRTGNIKYPSMSKTLGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPED-----ENTELPH--------- 416
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPG-----EIHALLGENGAGKSTLMKVLSGIHEPTKgtitiNNINYNKldhklaaql 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 417 -VSISYkpQKISPKSETTVrfmlhdkIQNMY--EHPQFK---TDVMNPLMMEQL-------------LDRNVKELSGGEL 477
Cdd:PRK09700 81 gIGIIY--QELSVIDELTV-------LENLYigRHLTKKvcgVNIIDWREMRVRaammllrvglkvdLDEKVANLSISHK 151
|
170 180
....*....|....*....|....*....
gi 17555800 478 QRVALALCLGKTASLYLIDEPSAYLDSEQ 506
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSLTNKE 180
|
|
| flavo_MJ0208 |
TIGR02700 |
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ... |
22-82 |
2.34e-04 |
|
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of archaealflavoprotein. The other, described by TIGR02699 and typified by the partially characterized AF1518 of Archaeoglobus fulgidus, is a homodimeric FMN-containing flavoprotein that accepts electrons from ferredoxin and can transfer them to various oxidoreductases. The function of this protein family is unknown. [Unknown function, General]
Pssm-ID: 131747 [Multi-domain] Cd Length: 234 Bit Score: 42.94 E-value: 2.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 22 VEKDRCKpkNCGLaCKRACPVnrqgkqcivvEATSTISQISEIL---CIGCGICVKKCPYDAIK 82
Cdd:TIGR02700 145 IDRKRCK--GCGI-CVDACPR----------SAIDMVDGKAFIRllkCVGCGKCKEACPYNAIH 195
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
6-92 |
2.38e-04 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 42.62 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 6 PLIKNNETDVPLR-IAIVEKDRCKpkNCGLaCKRACPVNrqgkqcIVVEATSTISQISEILCIGCGICVKKCPYDAIKII 84
Cdd:PRK05113 94 PLDGEAQEATPARkVAFIDEDNCI--GCTK-CIQACPVD------AIVGATKAMHTVISDLCTGCDLCVAPCPTDCIEMI 164
|
....*...
gi 17555800 85 NLPANLAN 92
Cdd:PRK05113 165 PVAETPDN 172
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
221-295 |
2.51e-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: 44.23 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 221 LDREIDQLSGGELQRFAIA------MCCVqkadVYMFDEPSSYLDVKQRLKAAAIIReRVSDT-NYVVVVEHD---LAVL 290
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLAtqigsgLTGV----LYVLDEPSIGLHQRDNRRLINTLK-RLRDLgNTLIVVEHDedtIRAA 556
|
....*
gi 17555800 291 DYLSD 295
Cdd:TIGR00630 557 DYVID 561
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
216-301 |
2.54e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.91 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 216 ELRGLLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNyVVVVEHDLAVLDYLSD 295
Cdd:PRK14267 138 EVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYT-IVLVTHSPAQAARVSD 216
|
....*.
gi 17555800 296 FICCLY 301
Cdd:PRK14267 217 YVAFLY 222
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
21-77 |
2.54e-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: 39.16 E-value: 2.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17555800 21 IVEKDRCKpkNCGlACKRACPVNRQGkqcivVEATSTISQISEIL-----CIGCGICVKKCP 77
Cdd:pfam13237 3 VIDPDKCI--GCG-RCTAACPAGLTR-----VGAIVERLEGEAVRigvwkCIGCGACVEACP 56
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
379-576 |
2.74e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 43.16 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 379 SDSEIIVMLGENGTGKTTMIKMM-------AGSLKPEDENTELPHV--------SISYKP--QKISPKSETTVRFMLHDk 441
Cdd:PRK13642 31 TKGEWVSIIGQNGSGKSTTARLIdglfeefEGKVKIDGELLTAENVwnlrrkigMVFQNPdnQFVGATVEDDVAFGMEN- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 442 iQNMYEHPQFKTdVMNPLMMEQLLDRNVKE---LSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFI 518
Cdd:PRK13642 110 -QGIPREEMIKR-VDEALLAVNMLDFKTREparLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIK 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 519 MHAKKTAFVVEHDFIMATYlADRVVVFEGQPSVKCTAckPQSLLEGMNRFLKM-LDITF 576
Cdd:PRK13642 188 EKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAA--PSELFATSEDMVEIgLDVPF 243
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
369-531 |
3.03e-04 |
|
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: 42.21 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 369 FHlDVEAGDFsDSEIIVMLGENGTGKTTMIKMMAGSLKPE-----DENTELPHVSisykpQKISPKSETTVRFMLHDKIQ 443
Cdd:cd03240 12 FH-ERSEIEF-FSPLTLIVGQNGAGKTTIIEALKYALTGElppnsKGGAHDPKLI-----REGEVRAQVKLAFENANGKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 444 -------NMYEHPQF-KTDVMNPLMMeqlldRNVKELSGGE------LQRVALALCLGKTASLYLIDEPSAYLDSEQRLH 509
Cdd:cd03240 85 ytitrslAILENVIFcHQGESNWPLL-----DMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
170 180
....*....|....*....|....*.
gi 17555800 510 A-AKVIKrfiMHAKKTAF---VVEHD 531
Cdd:cd03240 160 SlAEIIE---ERKSQKNFqliVITHD 182
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
52-83 |
3.14e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 43.70 E-value: 3.14e-04
10 20 30
....*....|....*....|....*....|..
gi 17555800 52 VEATSTISQISEILCIGCGICVKKCPYDAIKI 83
Cdd:COG1148 484 LGVEPSVAEVDPEKCTGCGRCVEVCPYGAISI 515
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
102-295 |
3.29e-04 |
|
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: 43.52 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKST-ALKIL-----------AGKQkpnlgnfqkeqewttiINHFRGSELQNYFTR 169
Cdd:COG4172 306 SLTLRR------GETLGLVGESGSGKSTlGLALLrlipsegeirfDGQD----------------LDGLSRRALRPLRRR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 170 IledtlkcvikpQYVDQIPRAA---KGTVE-----------KNLTRKhdnDNLNSVIDQMELRGL----LDREIDQLSGG 231
Cdd:COG4172 364 M-----------QVVFQDPFGSlspRMTVGqiiaeglrvhgPGLSAA---ERRARVAEALEEVGLdpaaRHRYPHEFSGG 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17555800 232 ELQRFAIAMCCVQKADVYMFDEPSSYLDV---KQ------RLKAaaiiRERVSdtnYvVVVEHDLAVLDYLSD 295
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVsvqAQildllrDLQR----EHGLA---Y-LFISHDLAVVRALAH 494
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
365-505 |
3.34e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 42.26 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 365 TLGNFH--LDVEAGDFSD---SEIIVMLGENGTGKTTMIKMMAGSL---KPEDENTELPHVSISYKPQKIspksETTVRF 436
Cdd:cd03279 7 ELKNFGpfREEQVIDFTGldnNGLFLICGPTGAGKSTILDAITYALygkTPRYGRQENLRSVFAPGEDTA----EVSFTF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 437 MLHDKIqnmY--------EHPQFKTDVMNPL-MMEQLLDRNVKELSGGELQRVALALCLGKTASLYL----------IDE 497
Cdd:cd03279 83 QLGGKK---YrversrglDYDQFTRIVLLPQgEFDRFLARPVSTLSGGETFLASLSLALALSEVLQNrggarlealfIDE 159
|
....*...
gi 17555800 498 PSAYLDSE 505
Cdd:cd03279 160 GFGTLDPE 167
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
114-268 |
3.43e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 43.68 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQkPNLGNFQkeqewttiINhfrGSELQNYftrILEDTLKCVikpQYVDQIPRAAKG 193
Cdd:PRK11174 376 GQRIALVGPSGAGKTSLLNALLGFL-PYQGSLK--------IN---GIELREL---DPESWRKHL---SWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TVEKNLT--RKHDND----------NLNSVIDQMELrGLlDREI-DQ---LSGGELQRFAIAMCCVQKADVYMFDEPSSY 257
Cdd:PRK11174 438 TLRDNVLlgNPDASDeqlqqalenaWVSEFLPLLPQ-GL-DTPIgDQaagLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170
....*....|....*..
gi 17555800 258 LD------VKQRLKAAA 268
Cdd:PRK11174 516 LDahseqlVMQALNAAS 532
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
63-85 |
3.50e-04 |
|
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: 42.67 E-value: 3.50e-04
10 20
....*....|....*....|...
gi 17555800 63 EILCIGCGICVKKCPYDAIKIIN 85
Cdd:COG2878 136 EYGCIGCGDCIKACPFDAIVGAA 158
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
472-549 |
3.53e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 472 LSGGELQRVALALCLGKTAS---LYLIDEPSAyldseqRLHAA------KVIKRFImHAKKTAFVVEH--DFIMAtylAD 540
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTT------GLHFHdirkllEVLHRLV-DKGNTVVVIEHnlDVIKT---AD 896
|
90 100
....*....|....*....|..
gi 17555800 541 RV-------------VVFEGQP 549
Cdd:COG0178 897 WIidlgpeggdgggeIVAEGTP 918
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
102-258 |
3.64e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.48 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIinHFRGSELQnyFTRiledtlkcvikp 181
Cdd:COG3845 25 SLTVRP------GEIHALLGENGAGKSTLMKILYGLYQPDSG---------EI--LIDGKPVR--IRS------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 qyvdqiPRAA--KG--------------TVEKN------------LTRKHDNDNLNSVIDQMELRGLLDREIDQLSGGEL 233
Cdd:COG3845 74 ------PRDAiaLGigmvhqhfmlvpnlTVAENivlgleptkggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQ 147
|
170 180
....*....|....*....|....*
gi 17555800 234 QRFAIAMCCVQKADVYMFDEPSSYL 258
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVL 172
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
65-85 |
3.64e-04 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 39.26 E-value: 3.64e-04
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
366-544 |
3.99e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.51 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKpedeNTELPH-------VSISYKP-QKISPKSETTVRFM 437
Cdd:PRK13547 17 LRDLSLRIEPG-----RVTALLGRNGAGKSTLLKALAGDLT----GGGAPRgarvtgdVTLNGEPlAAIDAPRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 438 LHDKIQnmyehPQFKTDVMNPLMM-----------------------------EQLLDRNVKELSGGELQRVALALCLGK 488
Cdd:PRK13547 88 LPQAAQ-----PAFAFSAREIVLLgrypharragalthrdgeiawqalalagaTALVGRDVTTLSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17555800 489 ---------TASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRVVV 544
Cdd:PRK13547 163 lwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAM 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
114-287 |
4.05e-04 |
|
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: 42.22 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFqkeqewtTIINH-FRGSELQNYFTRIledtlkcvikpQYVDQIPRAAK 192
Cdd:cd03251 28 GETVALVGPSGSGKSTLVNLIPRFYDVDSGRI-------LIDGHdVRDYTLASLRRQI-----------GLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 193 GTVEKNLTR-KHDND-----------NLNSVIDQMEL--------RGLldreidQLSGGELQRFAIAMCCVQKADVYMFD 252
Cdd:cd03251 90 DTVAENIAYgRPGATreeveeaaraaNAHEFIMELPEgydtvigeRGV------KLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 17555800 253 EPSSYLDVK-QRLKAAAIirERVSDTNYVVVVEHDL 287
Cdd:cd03251 164 EATSALDTEsERLVQAAL--ERLMKNRTTFVIAHRL 197
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
359-547 |
4.10e-04 |
|
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: 42.07 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 359 YPSMSKT--LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSIS-----YKPQKISPKSE 431
Cdd:cd03248 21 YPTRPDTlvLQDVSFTLHPG-----EVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyehkYLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 432 TTVRF--MLHDKIQnmYEHPQFKTDVMNPL-----------MMEQLLDRNVKE----LSGGELQRVALALCLGKTASLYL 494
Cdd:cd03248 96 EPVLFarSLQDNIA--YGLQSCSFECVKEAaqkahahsfisELASGYDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17555800 495 IDEPSAYLDSEQRLHAAKVIKRFimHAKKTAFVVEHDfIMATYLADRVVVFEG 547
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDW--PERRTVLVIAHR-LSTVERADQILVLDG 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
361-527 |
4.16e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 361 SMSKTLGNFHLDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPE--DENTELPHVS-ISY-KPQKI---------- 426
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDS-----WAFVGANGSGKSALARALAGELPLLsgERQSQFSHITrLSFeQLQKLvsdewqrnnt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 427 ---SPKSETTVRFMlHDKIQNMYEHPQFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLD 503
Cdd:PRK10938 89 dmlSPGEDDTGRTT-AEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180
....*....|....*....|....
gi 17555800 504 SEQRLHAAKVIKRfiMHAKKTAFV 527
Cdd:PRK10938 168 VASRQQLAELLAS--LHQSGITLV 189
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
371-541 |
4.20e-04 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 42.04 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 371 LDVEAGDFsdseiIVMLGENGTGKTTMIKMMAGSLKPeDENTelphVSISykPQKISPKSE---TTVR----------FM 437
Cdd:COG4181 33 LEVEAGES-----VAIVGASGSGKSTLLGLLAGLDRP-TSGT----VRLA--GQDLFALDEdarARLRarhvgfvfqsFQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 438 LhdkIQNMyehpqfkT---DVMNPLMM----------EQLLDRnV----------KELSGGELQRVALALCLGKTASLYL 494
Cdd:COG4181 101 L---LPTL-------TaleNVMLPLELagrrdararaRALLER-VglghrldhypAQLSGGEQQRVALARAFATEPAILF 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17555800 495 IDEPSAYLDSEQrlhAAKVIK-RFIMHAKK--TAFVVEHDfimaTYLADR 541
Cdd:COG4181 170 ADEPTGNLDAAT---GEQIIDlLFELNRERgtTLVLVTHD----PALAAR 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
381-548 |
4.68e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.07 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 381 SEIIVMLGENGTGKTTMIKMMAG----------------SLKPEDENTEL--PHVSISYKPQKISPKSETTVRFMLHDKI 442
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGlddgssgevslvgqplHQMDEEARAKLraKHVGFVFQSFMLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 443 QNMYEHP--QFKTDVMNPLMMEQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMH 520
Cdd:PRK10584 116 RGESSRQsrNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNRE 195
|
170 180
....*....|....*....|....*...
gi 17555800 521 AKKTAFVVEHDFIMATYLADRVVVFEGQ 548
Cdd:PRK10584 196 HGTTLILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
428-528 |
4.79e-04 |
|
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: 42.25 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 428 PKSETTVR---------FMLHDKIQNmyehpqfKTDVMNPL-----------------------MMEQLLDRNVKELSGG 475
Cdd:cd03272 90 DKEEVRLRrtiglkkdeYFLDKKNVT-------KNDVMNLLesagfsrsnpyyivpqgkinsltNMKQDEQQEMQQLSGG 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 476 ELQRVALAL--CLGKT--ASLYLIDEPSAYLDSEQRLHAAKVIKRFimhAKKTAFVV 528
Cdd:cd03272 163 QKSLVALALifAIQKCdpAPFYLFDEIDAALDAQYRTAVANMIKEL---SDGAQFIT 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
462-546 |
4.79e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.38 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 462 EQLLDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADR 541
Cdd:PRK10418 131 ARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADD 210
|
....*
gi 17555800 542 VVVFE 546
Cdd:PRK10418 211 VAVMS 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
102-136 |
5.18e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 42.38 E-value: 5.18e-04
10 20 30
....*....|....*....|....*....|....*
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAG 136
Cdd:COG4586 42 SFTIEP------GEIVGFIGPNGAGKSTTIKMLTG 70
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
114-261 |
5.21e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 42.84 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTI------INHFRGSELQNYF------TRILEDTLKCVI-- 179
Cdd:COG1132 366 GETVALVGPSGSGKSTLVNLLLRFYDPTSG---------RIlidgvdIRDLTLESLRRQIgvvpqdTFLFSGTIRENIry 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 180 -KPQYVD-QIPRAAKgtveknLTRKHDndnlnsVIDQMElRGLlDREIDQ----LSGGELQRFAIA--MccVQKADVYMF 251
Cdd:COG1132 437 gRPDATDeEVEEAAK------AAQAHE------FIEALP-DGY-DTVVGErgvnLSGGQRQRIAIAraL--LKDPPILIL 500
|
170
....*....|
gi 17555800 252 DEPSSYLDVK 261
Cdd:COG1132 501 DEATSALDTE 510
|
|
| DMSOR_beta_like |
cd16367 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
36-84 |
5.39e-04 |
|
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: 40.37 E-value: 5.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 17555800 36 CKRACPVNrqgkqcIVVEATSTISQISEIlCIGCGICVKKCPYDAIKII 84
Cdd:cd16367 65 CMIGCPTG------AIHRDDGGEVVISDA-CCGCGNCASACPYGAIQMV 106
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
65-92 |
6.13e-04 |
|
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: 40.70 E-value: 6.13e-04
10 20
....*....|....*....|....*...
gi 17555800 65 LCIGCGICVKKCPYDAIKIINLPANLAN 92
Cdd:cd16373 15 LCIRCGLCVEACPTGVIQPAGLEDGLEG 42
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
471-548 |
6.23e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 6.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 471 ELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEHDFIMATYLADRV-VVFEGQ 548
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKInVLYCGQ 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
112-288 |
7.16e-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: 41.37 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 112 RCGEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewTTIINHFRGSELQNYFTRILedtlkcvIKpqYVDQIPRAA 191
Cdd:cd03249 27 PPGKTVALVGSSGCGKSTVVSLLERFYDPTSG--------EILLDGVDIRDLNLRWLRSQ-------IG--LVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 192 KGTVEKNLtRKHDND-------------NLNSVIdqMELRGLLDREI----DQLSGGELQRFAIAMCCVQKADVYMFDEP 254
Cdd:cd03249 90 DGTIAENI-RYGKPDatdeeveeaakkaNIHDFI--MSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190
....*....|....*....|....*....|....*
gi 17555800 255 SSYLDVK-QRLKAAAIIRERVSDTnyVVVVEHDLA 288
Cdd:cd03249 167 TSALDAEsEKLVQEALDRAMKGRT--TIVIAHRLS 199
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
5-84 |
7.17e-04 |
|
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: 39.87 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 5 GPLIKNNETDVPlriaIVEKDRCKpkNCGlACKRACPVNRqgkqcIVVEATSTISQISeILCIGCGICVKKCPYDAIKII 84
Cdd:cd10550 64 GAISRDEETGAV----VVDEDKCI--GCG-MCVEACPFGA-----IRVDPETGKAIKC-DLCGGDPACVKVCPTGALEFV 130
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
410-530 |
7.25e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 410 ENTELPHVSISYKPQKISPKSETTVRFMLHDKIQNMyehpqfktdvmnPLMMEQLLDRNVKELSGGELQRVALALCLGKT 489
Cdd:PTZ00265 530 DSNELIEMRKNYQTIKDSEVVDVSKKVLIHDFVSAL------------PDKYETLVGSNASKLSGGQKQRISIARAIIRN 597
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 17555800 490 ASLYLIDEPSAYLDSEQRLHAAKVIKRFIMHAKKTAFVVEH 530
Cdd:PTZ00265 598 PKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
114-287 |
7.60e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.00 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGnfqkeqewtTIINHFRGSELQNYFTRILEDTLKCVIKPQYVDQIPRAA-- 191
Cdd:PRK13651 33 GEFIAIIGQTGSGKTTFIEHLNALLLPDTG---------TIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIKKIKei 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 192 ----------------KGTVEKNL--------TRKhdNDNLNSVIDQMELRGL----LDREIDQLSGGELQRFAIAMCCV 243
Cdd:PRK13651 104 rrrvgvvfqfaeyqlfEQTIEKDIifgpvsmgVSK--EEAKKRAAKYIELVGLdesyLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17555800 244 QKADVYMFDEPSSYLD---VKQRLKaaaIIRERVSDTNYVVVVEHDL 287
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDpqgVKEILE---IFDNLNKQGKTIILVTHDL 225
|
|
| PRK05888 |
PRK05888 |
NADH-quinone oxidoreductase subunit NuoI; |
32-81 |
7.75e-04 |
|
NADH-quinone oxidoreductase subunit NuoI;
Pssm-ID: 235637 [Multi-domain] Cd Length: 164 Bit Score: 40.64 E-value: 7.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 32 CGLaCKRACPVNrqgkqCIVVEATS--------TISQISEILCIGCGICVKKCPYDAI 81
Cdd:PRK05888 63 CKL-CAAICPAD-----AITIEAAEredgrrrtTRYDINFGRCIFCGFCEEACPTDAI 114
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
472-540 |
7.90e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 7.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17555800 472 LSGGELQRVALALCLGKTA---SLYLIDEPSAYLDSE--QRLhaAKVIKRFIMHAkKTAFVVEH--DFI-MATYLAD 540
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEdiRKL--LEVLHRLVDKG-NTVVVIEHnlDVIkTADWIID 904
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
114-301 |
7.97e-04 |
|
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: 40.97 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAG--KQKPNLGNfqkeqewttIInhFRGSELQNYFTrilEDTLKCVI--KPQYVDQIPr 189
Cdd:cd03217 26 GEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGE---------IL--FKGEDITDLPP---EERARLGIflAFQYPPEIP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 190 aakGTVEKNLTRkhdndNLNsvidqmelrglldreiDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAI 269
Cdd:cd03217 91 ---GVKNADFLR-----YVN----------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV 146
|
170 180 190
....*....|....*....|....*....|...
gi 17555800 270 IRERVSDTNYVVVVEHDLAVLDYL-SDFICCLY 301
Cdd:cd03217 147 INKLREEGKSVLIITHYQRLLDYIkPDRVHVLY 179
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
211-331 |
8.25e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 41.69 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 211 VIDQMELRGLldreidQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNyVVVVEHDLAVL 290
Cdd:PRK14243 141 VKDKLKQSGL------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT-IIIVTHNMQQA 213
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 17555800 291 DYLSDFIcclygvpGVYGVVTLPSGVREGinmFLEGFIRTE 331
Cdd:PRK14243 214 ARVSDMT-------AFFNVELTEGGGRYG---YLVEFDRTE 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
110-143 |
9.15e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.96 E-value: 9.15e-04
10 20 30
....*....|....*....|....*....|....
gi 17555800 110 TPRCGEVLGLVGTNGIGKSTALKILAGKQKPNLG 143
Cdd:PRK15439 33 TLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSG 66
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
102-302 |
9.39e-04 |
|
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: 40.49 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQkeqewttiinhFRGSELQNYFTR---------ILE 172
Cdd:cd03215 20 SFEVRA------GEIVGIAGLVGNGQTELAEALFGLRPPASGEIT-----------LDGKPVTRRSPRdairagiayVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 173 DtlkcvikpqyvdqipRAAKGTVeknLTRkhdndnlnSVIDQMELRglldreiDQLSGGELQRFAIAMCCVQKADVYMFD 252
Cdd:cd03215 83 D---------------RKREGLV---LDL--------SVAENIALS-------SLLSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17555800 253 EPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDLAVLDYLSDFICCLYG 302
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYE 179
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
102-295 |
9.56e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.87 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 102 SFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTIINHfrgSELQNYFTRIledtlkcvikp 181
Cdd:PRK11308 35 SFTLER------GKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP---EAQKLLRQKI----------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 182 QYVDQIPRAA---KGTVEKNLTRKHD-NDNLNS------VIDQMELRGL----LDREIDQLSGGELQRFAIAMCCVQKAD 247
Cdd:PRK11308 95 QIVFQNPYGSlnpRKKVGQILEEPLLiNTSLSAaerrekALAMMAKVGLrpehYDRYPHMFSGGQRQRIAIARALMLDPD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17555800 248 VYMFDEPSSYLDVK---QRLKAAAIIRERVSdTNYvVVVEHDLAVLDYLSD 295
Cdd:PRK11308 175 VVVADEPVSALDVSvqaQVLNLMMDLQQELG-LSY-VFISHDLSVVEHIAD 223
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
366-540 |
1.04e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.24 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 366 LGNFHLDVEAGdfsdsEIIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHVSISYKPQKISPKSETTVRF--------- 436
Cdd:PRK11147 19 LDNAELHIEDN-----ERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGTVYdfvaegiee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 437 ----------MLHD--------------KIQNMYEHP---QFKTDVMNPLmmEQL-LDRNVK--ELSGGELQRVALALCL 486
Cdd:PRK11147 94 qaeylkryhdISHLvetdpseknlnelaKLQEQLDHHnlwQLENRINEVL--AQLgLDPDAAlsSLSGGWLRKAALGRAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 487 GKTASLYLIDEPSAYLDSEqrlhAAKVIKRFIMHAKKTAFVVEHD--FI--MATYLAD 540
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHDrsFIrnMATRIVD 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
183-259 |
1.06e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.42 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 183 YVDQIPRAAKGTVEKNLT--RKHDNDNLNSVIDQMELRGLLD-------REIDQ----LSGGELQRFAIAMCCVQKADVY 249
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILfgSPFDPERYERAIDVTALQHDLDllpggdlTEIGErgvnISGGQKQRVSMARAVYSNSDVY 762
|
90
....*....|
gi 17555800 250 MFDEPSSYLD 259
Cdd:PLN03130 763 IFDDPLSALD 772
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
222-286 |
1.14e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17555800 222 DREIDQLSGGELQ------RFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHD 286
Cdd:PRK03918 783 ERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHD 853
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
36-137 |
1.22e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 41.94 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 36 CKRACPVNrqgkqCIVVEATSTisQISEILCIGCGICVKKCPYDAIKIINLPANLANETTHRYSQNSFKLHRLPTpRCGE 115
Cdd:PRK12809 64 CVTACPVN-----ALTFQSDSV--QLDEQKCIGCKRCAIACPFGVVEMVDTIAQKCDLCNQRSSGTQACIEVCPT-QALR 135
|
90 100
....*....|....*....|..
gi 17555800 116 VLGLVGTNGIGKSTALKILAGK 137
Cdd:PRK12809 136 LMDDKGLQQIKVARQRKTAAGK 157
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
114-260 |
1.34e-03 |
|
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: 40.53 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQkeqewttiinhfrgselqnYFTRILedtlkcvikpqYVDQIPRAAKG 193
Cdd:cd03250 31 GELVAIVGPVGSGKSSLLSALLGELEKLSGSVS-------------------VPGSIA-----------YVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 194 TVEKNLT--RKHDNDNLNSVIDQMELRglLDREI----DQ---------LSGGELQRFAIAMCCVQKADVYMFDEPSSYL 258
Cdd:cd03250 81 TIRENILfgKPFDEERYEKVIKACALE--PDLEIlpdgDLteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
..
gi 17555800 259 DV 260
Cdd:cd03250 159 DA 160
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
65-85 |
1.35e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 41.52 E-value: 1.35e-03
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
467-530 |
1.38e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 1.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 467 RNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDseqrLHAAKVIKRFIMHAKKTAFVVEH 530
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD----LHAVLWLETYLLKWPKTFIVVSH 399
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
377-547 |
1.41e-03 |
|
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: 41.85 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 377 DFSDSE--IIVMLGENGTGKTTMIKMMAGSLKPEDENTELPHvSISYKPQKISPKSETTVRFML--HDKIQNMYEHPQFK 452
Cdd:TIGR00957 658 TFSIPEgaLVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQAWIQNDSLRENILfgKALNEKYYQQVLEA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 453 TDVMNPLMMEQLLDRN-VKE----LSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHA-AKVIKRFIMHAKKTAF 526
Cdd:TIGR00957 737 CALLPDLEILPSGDRTeIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfEHVIGPEGVLKNKTRI 816
|
170 180
....*....|....*....|...
gi 17555800 527 VVEHDFimaTYL--ADRVVVFEG 547
Cdd:TIGR00957 817 LVTHGI---SYLpqVDVIIVMSG 836
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
414-531 |
1.63e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 414 LPHV-SISYKPQKISPKSETTVR-----FMLHDKIQNmyehpqfKTDVMNPLMMEQL-LDRNVKELSGGELQRVALA--- 483
Cdd:PRK00635 752 LPQVlEVRYKGKNIADILEMTAYeaekfFLDEPSIHE-------KIHALCSLGLDYLpLGRPLSSLSGGEIQRLKLAyel 824
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 17555800 484 LCLGKTASLYLIDEPSAYLDSEQrLHAAKVIKRFIMHAKKTAFVVEHD 531
Cdd:PRK00635 825 LAPSKKPTLYVLDEPTTGLHTHD-IKALIYVLQSLTHQGHTVVIIEHN 871
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
114-259 |
1.68e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPnlgnfqkeQEWTTIInhFRGSelqnyftriledtlkcvikPQYVDQIPRAAKG 193
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGELSH--------AETSSVV--IRGS-------------------VAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 194 TVEKNLT--RKHDNDNLNSVIDQMELRGLLD-------REIDQ----LSGGELQRFAIAMCCVQKADVYMFDEPSSYLD 259
Cdd:PLN03232 694 TVRENILfgSDFESERYWRAIDVTALQHDLDllpgrdlTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
465-543 |
1.73e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 465 LDRNVKELSGGELQRVALALCLGK--TASLYLIDEPSAYL---DSEqrlhaakvikRFIMHAKK------TAFVVEHDF- 532
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSglTGVLYVLDEPSIGLhqrDND----------RLIETLKHlrdlgnTLIVVEHDEd 552
|
90
....*....|..
gi 17555800 533 -IMAtylADRVV 543
Cdd:PRK00349 553 tIRA---ADYIV 561
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
223-281 |
1.76e-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: 40.32 E-value: 1.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17555800 223 REIDQLSGGELQRFAIAMC-CVQKAD---VYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVV 281
Cdd:cd03272 154 QEMQQLSGGQKSLVALALIfAIQKCDpapFYLFDEIDAALDAQYRTAVANMIKELSDGAQFIT 216
|
|
| FDH_b_like |
cd10562 |
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ... |
35-83 |
1.89e-03 |
|
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: 39.21 E-value: 1.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 17555800 35 ACKRACPVNrqgkqCIVVEATSTISqISEILCIGCGICVKKCPYDAIKI 83
Cdd:cd10562 77 ACVKVCPTG-----ALYKTENGAVV-VDEDKCIGCGYCVAACPFDVPRY 119
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
5-83 |
2.09e-03 |
|
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: 40.06 E-value: 2.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 5 GPLIKNNETDVPLRIAIVEKDRCKpkNCGLaCKRACPVNrqgkqciVVEATSTISQISEILCIGCGICVKKCPYDAIKI 83
Cdd:cd03110 44 GPEPEEEEDFVGGKKAFIDQEKCI--RCGN-CERVCKFG-------AILEFFQKLIVDESLCEGCGACVIICPRGAIYL 112
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
66-84 |
2.30e-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: 38.47 E-value: 2.30e-03
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
114-285 |
2.38e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 40.11 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLG----------NFQKEQEWTTIINH----FRGSELQNYFTRILEDTlkcVI 179
Cdd:PRK13649 33 GSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvrvddtlitSTSKNKDIKQIRKKvglvFQFPESQLFEETVLKDV---AF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 180 KPQYVDQIPRAAKGTVEKNLTRKHDNDNLnsvidqmelrglLDREIDQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLD 259
Cdd:PRK13649 110 GPQNFGVSQEEAEALAREKLALVGISESL------------FEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180
....*....|....*....|....*.
gi 17555800 260 VKQRLKAAAIIRERVSDTNYVVVVEH 285
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
228-295 |
2.43e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 228 LSGGELQRfaiamccV------QKAD----VYMFDEPSSYL---DVKQRLKAaaiIRERVSDTNYVVVVEHDLAVL---D 291
Cdd:COG0178 827 LSGGEAQR-------VklaselSKRStgktLYILDEPTTGLhfhDIRKLLEV---LHRLVDKGNTVVVIEHNLDVIktaD 896
|
....
gi 17555800 292 YLSD 295
Cdd:COG0178 897 WIID 900
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
465-544 |
2.76e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 465 LDRNVKELSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQRLHAAKVIKRfiMHAKKTAFV-VEHDFIMATYLADRVV 543
Cdd:PRK15439 397 AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRS--IAAQNVAVLfISSDLEEIEQMADRVL 474
|
.
gi 17555800 544 V 544
Cdd:PRK15439 475 V 475
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
227-295 |
2.77e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 40.20 E-value: 2.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 227 QLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHDL-AVLDYLSD 295
Cdd:PRK13641 145 ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADD 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
112-136 |
2.92e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.68 E-value: 2.92e-03
10 20
....*....|....*....|....*
gi 17555800 112 RCGEVLGLVGTNGIGKSTALKILAG 136
Cdd:PRK13549 29 RAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
11-86 |
3.05e-03 |
|
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: 38.38 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 11 NETDVPLRIAIveKDRCKPKN---CgLACKRACPVnrqgkQCIVVEATSTISQISEI---LCIGCGICVKKCPYDAIKII 84
Cdd:cd10564 66 REAPWPLRAEI--GDSCLALQgveC-RSCQDACPT-----QAIRFRPRLGGIALPELdadACTGCGACVSVCPVGAITLT 137
|
..
gi 17555800 85 NL 86
Cdd:cd10564 138 PL 139
|
|
| FDH-O_like |
cd10560 |
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ... |
25-83 |
3.40e-03 |
|
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: 39.29 E-value: 3.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 25 DRCKpkNCGLA-CKRACPVNrqgkqCIVVEATSTISqISEILCIGCGICVKKCPYDAIKI 83
Cdd:cd10560 76 DVCK--HCTDAgCLEACPTG-----AIFRTEFGTVY-IQPDICNGCGYCVAACPFGVIDR 127
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
466-531 |
3.61e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 466 DRNVKELSGGElqRVALALCLGKTASLYLI--------DEPSAYLDSEQRLHAAKVIKRfimHAKK--TAFVVEHD 531
Cdd:PRK03918 783 ERPLTFLSGGE--RIALGLAFRLALSLYLAgnipllilDEPTPFLDEERRRKLVDIMER---YLRKipQVIIVSHD 853
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
227-295 |
3.70e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 39.69 E-value: 3.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 227 QLSGGELQRFAIAMCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRErVSDTNYVVVVEHDLAVLDYLSD 295
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS-LADRLTVIIVTHNLAQAARISD 230
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
32-85 |
3.88e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 40.36 E-value: 3.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 17555800 32 CGLaCKRACPVNrqgkqCIVVEATSTISQISEILCIGCGICVKKCPydAIKIIN 85
Cdd:PRK13795 586 CGV-CVGACPTG-----AIRIEEGKRKISVDEEKCIHCGKCTEVCP--VVKYKD 631
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
472-545 |
4.30e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 39.31 E-value: 4.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 472 LSGGELQRVALALCLGKTASLYLIDEPSAYLDSEqrlhAAKVIKRFI--MHAKKTAFVVEHDFIMATYLADRVVVF 545
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPT----TTEKIEEFIrsLADRLTVIIVTHNLAQAARISDRAALF 235
|
|
| porD |
PRK09625 |
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
31-94 |
4.36e-03 |
|
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 37.80 E-value: 4.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17555800 31 NCGLACKRACPVNRQGKqcivveatstISQISEILCIGCGICVKKCPYDAIKIINLPANLANET 94
Cdd:PRK09625 66 NCWVYCPDAAILSRDKK----------LKGVDYSHCKGCGVCVEVCPTNPKSLLMFEEQIENET 119
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
467-511 |
4.78e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 39.80 E-value: 4.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 17555800 467 RNVKeLSGGELQRVALALCLGKTASLYLIDEPSAYLDS--EQRLHAA 511
Cdd:COG5265 491 RGLK-LSGGEKQRVAIARTLLKNPPILIFDEATSALDSrtERAIQAA 536
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
66-87 |
5.49e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 39.75 E-value: 5.49e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
221-297 |
5.63e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 221 LDREIDQLSGGELQRFAIA---MCCVQKADVYMFDEPSSYL---DVKQRLKaaaIIRERVSDTNYVVVVEHDLAVLDyLS 294
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLhthDIKALIY---VLQSLTHQGHTVVIIEHNMHVVK-VA 878
|
...
gi 17555800 295 DFI 297
Cdd:PRK00635 879 DYV 881
|
|
| PsrB |
cd10551 |
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ... |
35-113 |
5.86e-03 |
|
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.
Pssm-ID: 319873 [Multi-domain] Cd Length: 185 Bit Score: 38.28 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 35 ACKRACPVNrqgkqcivveATST----ISQISEILCIGCGICVKKCPYDAIKIINLPANLANETTHRYSQN----SFKLH 106
Cdd:cd10551 60 PCVKVCPTG----------ATYKredgIVLVDYDKCIGCRYCMAACPYGARYFNPEEPHEFGEVPVRPKGVvekcTFCYH 129
|
90
....*....|
gi 17555800 107 RL---PTPRC 113
Cdd:cd10551 130 RLdegLLPAC 139
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
472-547 |
5.95e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 39.42 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 472 LSGGELQRVALALCLGKTASLYLIDEPSAYLDSEQrlhaakviKRFIM-----HAK-KTAFVVEHDfimATYLA--DRVV 543
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET--------ERQILellaeHAQnKTVLMITHR---LTGLEqfDRIC 544
|
....
gi 17555800 544 VFEG 547
Cdd:PRK11160 545 VMDN 548
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
221-286 |
5.98e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 5.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 221 LDREIDQLSGGELQRFAIA--MCCVQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVVVEHD 286
Cdd:PRK00635 470 PERALATLSGGEQERTALAkhLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
24-81 |
6.02e-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: 37.25 E-value: 6.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 17555800 24 KDRCKpkNCGlACKRACPVNrqgkqCIVVEATSTISqiseILCIGCGICVKKCPYDAI 81
Cdd:cd16370 82 KEKCI--GCG-NCVKACIVG-----AIFWDEETNKP----IICIHCGYCARYCPHDVL 127
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
218-259 |
6.08e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 39.42 E-value: 6.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 17555800 218 RGLldreidQLSGGELQRFAIAMCCVQKADVYMFDEPSSYLD 259
Cdd:COG5265 491 RGL------KLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
66-81 |
6.18e-03 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 35.22 E-value: 6.18e-03
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
79-154 |
6.34e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 6.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 79 DAIKIINLPANlANETTHRYSQNSFKLHRlptprcGEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQKEQEWTTI 154
Cdd:PRK13546 22 ERMKDALIPKH-KNKTFFALDDISLKAYE------GDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVI 90
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
114-259 |
6.57e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 114 GEVLGLVGTNGIGKSTALKILAGKQKPNLGNFQkeqeWttiinhfrgSELQN--YFtriledtlkcvikPQyvDQiprAA 191
Cdd:PRK15064 345 GERLAIIGENGVGKTTLLRTLVGELEPDSGTVK----W---------SENANigYY-------------AQ--DH---AY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555800 192 KGTVEKNLT------RKHDNDnlnsviDQMeLRGLLDR------EIDQ----LSGGELQRFAIAMCCVQKADVYMFDEPS 255
Cdd:PRK15064 394 DFENDLTLFdwmsqwRQEGDD------EQA-VRGTLGRllfsqdDIKKsvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
....
gi 17555800 256 SYLD 259
Cdd:PRK15064 467 NHMD 470
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
66-83 |
7.20e-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: 7.20e-03
|
| Fer4_6 |
pfam12837 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
65-81 |
7.71e-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: 432822 [Multi-domain] Cd Length: 24 Bit Score: 34.13 E-value: 7.71e-03
|
| Fer4_16 |
pfam13484 |
4Fe-4S double cluster binding domain; |
66-82 |
7.75e-03 |
|
4Fe-4S double cluster binding domain;
Pssm-ID: 463893 [Multi-domain] Cd Length: 65 Bit Score: 35.16 E-value: 7.75e-03
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
223-282 |
8.03e-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: 39.57 E-value: 8.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17555800 223 REIDQLSGGELQ------RFAIAMCcvQKADVYMFDEPSSYLDVKQRLKAAAIIRERVSDTNYVVV 282
Cdd:pfam02463 1073 KNLDLLSGGEKTlvalalIFAIQKY--KPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVI 1136
|
|
| napG |
PRK09476 |
quinol dehydrogenase periplasmic component; Provisional |
66-94 |
8.74e-03 |
|
quinol dehydrogenase periplasmic component; Provisional
Pssm-ID: 236534 [Multi-domain] Cd Length: 254 Bit Score: 38.45 E-value: 8.74e-03
10 20
....*....|....*....|....*....
gi 17555800 66 CIGCGICVKKCPYDAIKIINLPANLANET 94
Cdd:PRK09476 61 CIRCGLCVQACPYDTLKLATLASGLSAGT 89
|
|
| PRK09898 |
PRK09898 |
ferredoxin-like protein; |
21-84 |
8.84e-03 |
|
ferredoxin-like protein;
Pssm-ID: 182135 [Multi-domain] Cd Length: 208 Bit Score: 37.89 E-value: 8.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17555800 21 IVEKDRCKpkNCGlACKRACP-----VNRQGKQcivveatSTisqiseiLCIGCGICVKKCPYDAIKII 84
Cdd:PRK09898 150 TVDHKRCI--GCS-ACTTACPwmmatVNTESKK-------SS-------KCVLCGECANACPTGALKII 201
|
|
| |
