|
Name |
Accession |
Description |
Interval |
E-value |
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-604 |
0e+00 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 871.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 7 RIAIVSADKCKPKKCRQECKRSCPVVKTGKLCIEVTPTSKIAFISEILCIGCGICVKKCPFDAIQIINLPTNLEAHVTHR 86
Cdd:COG1245 3 RIAVVDRDRCQPKKCNYECIKYCPVNRTGKEAIEIDEDDGKPVISEELCIGCGICVKKCPFDAISIVNLPEELEEDPVHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 87 YSANSFKLHRLPTPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDDPPEWQEIIKYFRGSELQNYFTKMLEDDIKA 166
Cdd:COG1245 83 YGENGFRLYGLPVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKRFRGTELQDYFKKLANGEIKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 167 IIKPQYVDNIPRAIKGpvqKVGELLKLRMEKSpeDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFD 246
Cdd:COG1245 163 AHKPQYVDLIPKVFKG---TVRELLEKVDERG--KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 247 EPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIYGVPSVYGVVTLPASVREGINIFLDGHIPAEN 326
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILYGEPGVYGVVSKPKSVRVGINQYLDGYLPEEN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 327 LRFRTEALQFRIADATEDLqndSASRAFSYPSLKKTQGDFVLNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPDE 406
Cdd:COG1245 318 VRIRDEPIEFEVHAPRREK---EEETLVEYPDLTKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 407 GQDIPKLNVSMKPQKIAPKFPGTVRQLFFKKIRGQFLNPQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPA 486
Cdd:COG1245 395 GEVDEDLKISYKPQYISPDYDGTVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 487 DIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFEGIPSKNAHARAPESLLTGCNRFLK 566
Cdd:COG1245 475 DLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGVHGHASGPMDMREGMNRFLK 554
|
570 580 590
....*....|....*....|....*....|....*...
gi 398365537 567 NLNVTFRRDPNSFRPRINKLDSQMDKEQKSSGNYFFLD 604
Cdd:COG1245 555 ELGITFRRDEETGRPRINKPGSYLDREQKERGEYYYYE 592
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-604 |
0e+00 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 859.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 6 SRIAIVSADKCKPKKCRQECKRSCPVVKTGKLCIEVTPTSKIAFISEILCIGCGICVKKCPFDAIQIINLPTNLEAHVTH 85
Cdd:PRK13409 2 MRIAVVDYDRCQPKKCNYECIKYCPVVRTGEETIEIDEDDGKPVISEELCIGCGICVKKCPFDAISIVNLPEELEEEPVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 86 RYSANSFKLHRLPTPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDDPPEWQEIIKYFRGSELQNYFTKMLEDDIK 165
Cdd:PRK13409 82 RYGVNGFKLYGLPIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRFRGTELQNYFKKLYNGEIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 166 AIIKPQYVDNIPRAIKGpvqKVGELLKLRMEKSPEDvkRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMF 245
Cdd:PRK13409 162 VVHKPQYVDLIPKVFKG---KVRELLKKVDERGKLD--EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 246 DEPSSYLDVKQRLNAAQIIRSlLAPTKYVICVEHDLSVLDYLSDFVCIIYGVPSVYGVVTLPASVREGINIFLDGHIPAE 325
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRE-LAEGKYVLVVEHDLAVLDYLADNVHIAYGEPGAYGVVSKPKGVRVGINEYLKGYLPEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 326 NLRFRTEALQFRIADATEDlqnDSASRAFSYPSLKKTQGDFVLNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPD 405
Cdd:PRK13409 316 NMRIRPEPIEFEERPPRDE---SERETLVEYPDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 406 EGQDIPKLNVSMKPQKIAPKFPGTVRQlFFKKIRGQFLNPQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIP 485
Cdd:PRK13409 393 EGEVDPELKISYKPQYIKPDYDGTVED-LLRSITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRD 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 486 ADIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFEGIPSKNAHARAPESLLTGCNRFL 565
Cdd:PRK13409 472 ADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGEPGKHGHASGPMDMREGMNRFL 551
|
570 580 590
....*....|....*....|....*....|....*....
gi 398365537 566 KNLNVTFRRDPNSFRPRINKLDSQMDKEQKSSGNYFFLD 604
Cdd:PRK13409 552 KELGITFRRDEETGRPRVNKPGSYLDREQKERGEYYYAD 590
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
78-337 |
8.95e-155 |
|
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: 444.89 E-value: 8.95e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 78 NLEAHVTHRYSANSFKLHRLPTPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDDPPEWQEIIKYFRGSELQNYFT 157
Cdd:cd03236 1 ELEDEPVHRYGPNSFKLHRLPVPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 158 KMLEDDIKAIIKPQYVDNIPRAIKGpvqKVGELLKLRMEKSPEDvkRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCV 237
Cdd:cd03236 81 KLLEGDVKVIVKPQYVDLIPKAVKG---KVGELLKKKDERGKLD--ELVDQLELRHVLDRNIDQLSGGELQRVAIAAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 238 QEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIYGVPSVYGVVTLPASVREGINIF 317
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPGAYGVVTLPKSVREGINEF 235
|
250 260
....*....|....*....|
gi 398365537 318 LDGHIPAENLRFRTEALQFR 337
Cdd:cd03236 236 LDGYLPTENMRFREESIEFE 255
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
354-598 |
2.32e-141 |
|
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: 410.26 E-value: 2.32e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQGDFVLNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQ-DIPKLNVSMKPQKIAPKFPGTVRQ 432
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDiEIELDTVSYKPQYIKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 LFFKKIRGQFLNPQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRR 512
Cdd:cd03237 81 LLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 513 FILHNKKTAFIVEHDFIMATYLADKVIVFEGIPSKNAHARAPESLLTGCNRFLKNLNVTFRRDPNSFRPRINKLDSQMDK 592
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVANPPQSLRSGMNRFLKNLDITFRRDPETGRPRINKLGSVKDR 240
|
....*.
gi 398365537 593 EQKSSG 598
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 ... |
356-573 |
1.02e-67 |
|
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: 217.82 E-value: 1.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 356 YPSLKKTQGDFVLNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQD-IPKLNVSMKPQKIApkfpgtvrqlf 434
Cdd:cd03222 3 YPDCVKRYGVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDeWDGITPVYKPQYID----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 435 fkkirgqflnpqfqtdvvkplriddiidqevqhLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFI 514
Cdd:cd03222 72 ---------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 515 LHNKKTAFIVEHDFIMATYLADKVIVFEGIPSKNAHARAPESLLTGCNRFLKNLNVTFR 573
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYLITFR 177
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
79-326 |
2.74e-41 |
|
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: 147.72 E-value: 2.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 79 LEAHVTHRYsANSFKLHRLPTPRPGQVLGLVGTNGIGKSTALKILAGKQKPNlgrfDDPPEWqeiikyfrgselqnyftk 158
Cdd:cd03222 2 LYPDCVKRY-GVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPN----GDNDEW------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 159 mleDDIKAIIKPQYVDnipraikgpvqkvgellklrmekspedvkryikilqlenvlkrdiekLSGGELQRFAIGMSCVQ 238
Cdd:cd03222 59 ---DGITPVYKPQYID-----------------------------------------------LSGGELQRVAIAAALLR 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 239 EADVYMFDEPSSYLDVKQRLNAAQIIRSLLAP-TKYVICVEHDLSVLDYLSDFVCIIYGVPSVYGVVTLPASVREGINIF 317
Cdd:cd03222 89 NATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRF 168
|
....*....
gi 398365537 318 LDGHIPAEN 326
Cdd:cd03222 169 LRGYLITFR 177
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
87-318 |
3.61e-41 |
|
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: 149.48 E-value: 3.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 87 YSANSFKLHRLP-TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGrfdDPPEWQEIIKYfrgselqnyftkmleddik 165
Cdd:cd03237 8 KTLGEFTLEVEGgSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG---DIEIELDTVSY------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 166 aiiKPQYVDnipraIKGPVqKVGELL--KLR-MEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADV 242
Cdd:cd03237 66 ---KPQYIK-----ADYEG-TVRDLLssITKdFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 243 YMFDEPSSYLDVKQRLNAAQIIRSL-LAPTKYVICVEHDLSVLDYLSDFVCIIYGVPSVYGVVTLPASVREGINIFL 318
Cdd:cd03237 137 YLLDEPSAYLDVEQRLMASKVIRRFaENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVANPPQSLRSGMNRFL 213
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
377-580 |
4.58e-38 |
|
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: 141.35 E-value: 4.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 377 DSEILVMMGENGTGKTTLIKLLAGALKPDEG--QDIP------------------------KLNVSMKPQ--KIAPK-FP 427
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfDDPPdwdeildefrgselqnyftkllegDVKVIVKPQyvDLIPKaVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 428 GTVRQLFFKKIRGQFLNpqfqtDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICS 507
Cdd:cd03236 105 GKVGELLKKKDERGKLD-----ELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 508 KVIRRFILHnKKTAFIVEHDFIMATYLADKVIVFEGIPSKNAHARAPESLLTGCNRFL----KNLNVTFRRDPNSFR 580
Cdd:cd03236 180 RLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLYGEPGAYGVVTLPKSVREGINEFLdgylPTENMRFREESIEFE 255
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
101-540 |
3.48e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 130.41 E-value: 3.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQkPNLGRFDDppewqEIIkyFRGSELQNYFTKMLEDDIKAIikPQYVDN--IPR 178
Cdd:COG1123 30 APGETVALVGESGSGKSTLALALMGLL-PHGGRISG-----EVL--LDGRDLLELSEALRGRRIGMV--FQDPMTqlNPV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 179 AIKGPVQKVGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRL 258
Cdd:COG1123 100 TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 259 NAAQIIRSLLAPT-KYVICVEHDLSVLDYLSDFVCIIYGvpsvyGVVTLPASVREginIFLDGHIPAENLRFRTEALQFR 337
Cdd:COG1123 180 EILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDD-----GRIVEDGPPEE---ILAAPQALAAVPRLGAARGRAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 338 IADAT-------EDLQndsasraFSYPSLKKtqGDFV------LNVEEGefsdsEILVMMGENGTGKTTLIKLLAGALKP 404
Cdd:COG1123 252 PAAAAaepllevRNLS-------KRYPVRGK--GGVRavddvsLTLRRG-----ETLGLVGESGSGKSTLARLLLGLLRP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 405 DEGQdipklnVSMKPQKIAPKFPGTVRQLfFKKIrgQF--------LNPQF--QTDVVKPLRIDDIIDQEVQH------- 467
Cdd:COG1123 318 TSGS------ILFDGKDLTKLSRRSLREL-RRRV--QMvfqdpyssLNPRMtvGDIIAEPLRLHGLLSRAERRervaell 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 468 ----------------LSGGELQRVAI--VLALGipADIYLIDEP-SAyLD-SEQRIICsKVIRRfiLHNK--KTAFIVE 525
Cdd:COG1123 389 ervglppdladrypheLSGGQRQRVAIarALALE--PKLLILDEPtSA-LDvSVQAQIL-NLLRD--LQRElgLTYLFIS 462
|
490
....*....|....*
gi 398365537 526 HDFIMATYLADKVIV 540
Cdd:COG1123 463 HDLAVVRYIADRVAV 477
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
354-542 |
2.46e-29 |
|
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: 115.26 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQGDFV-LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKPQKIapkf 426
Cdd:cd03225 7 FSYPDGARPALDDIsLTIKKGEF-----VLIVGPNGSGKSTLLRLLNGLLGPTSGevlvdgKDLTKLSLKELRRKV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 427 pGTV-----RQLFFKKIR-------GQFLNPQFQ-----TDVVKPLRIDDIIDQEVQHLSGGELQRVAI--VLALGipAD 487
Cdd:cd03225 78 -GLVfqnpdDQFFGPTVEeevafglENLGLPEEEieervEEALELVGLEGLRDRSPFTLSGGQKQRVAIagVLAMD--PD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365537 488 IYLIDEPSAYLDSEQRIICSKVIRRfiLHNK-KTAFIVEHDFIMATYLADKVIVFE 542
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKK--LKAEgKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
360-542 |
4.64e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 110.03 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 360 KKTQGDFVLNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFPGTVRQLFFkkir 439
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE------ILIDGKDIAKLPLEELRRRIG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 440 gqflnpqfqtdvvkplriddIIDQevqhLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNkK 519
Cdd:cd00267 77 --------------------YVPQ----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEG-R 131
|
170 180
....*....|....*....|...
gi 398365537 520 TAFIVEHDFIMATYLADKVIVFE 542
Cdd:cd00267 132 TVIIVTHDPELAELAADRVIVLK 154
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
364-543 |
5.08e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.05 E-value: 5.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 364 GDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ-----------DIPKL--NVSMKPQKiAPKFPGTV 430
Cdd:COG4619 17 SPVSLTLEAGEC-----VAITGPSGSGKSTLLRALADLDPPTSGEiyldgkplsamPPPEWrrQVAYVPQE-PALWGGTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 431 RQLFFK--KIRGQFLNPQFQTDVVKPLRID-DIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICS 507
Cdd:COG4619 91 RDNLPFpfQLRERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVE 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 398365537 508 KVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFEG 543
Cdd:COG4619 171 ELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
354-543 |
1.27e-24 |
|
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: 102.41 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQGDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPKLNVSMKPQKIapkfp 427
Cdd:COG1122 8 FSYPGGTPALDDVSLSIEKGEF-----VAIIGPNGSGKSTLLRLLNGLLKPTSGEvlvdgkDITKKNLRELRRKV----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 428 GTV-----RQLFF----------------------KKIRgqflnpqfqtDVVKPLRIDDIIDQEVQHLSGGELQRVAI-- 478
Cdd:COG1122 78 GLVfqnpdDQLFAptveedvafgpenlglpreeirERVE----------EALELVGLEHLADRPPHELSGGQKQRVAIag 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 479 VLALGiPaDIYLIDEPSAYLD--SEQRIIcsKVIRRfiLHNKKTAFI-VEHDFIMATYLADKVIVFEG 543
Cdd:COG1122 148 VLAME-P-EVLVLDEPTAGLDprGRRELL--ELLKR--LNKEGKTVIiVTHDLDLVAELADRVIVLDD 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
368-543 |
7.94e-24 |
|
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: 99.92 E-value: 7.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ-DIPKLNVSMKPQKIA---------PKFPGTVRQL---- 433
Cdd:cd03235 20 FEVKPGEF-----LAIVGPNGAGKSTLLKAILGLLKPTSGSiRVFGKPLEKERKRIGyvpqrrsidRDFPISVRDVvlmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 434 FFKKIRGQFLNPQFQTDVV----KPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKV 509
Cdd:cd03235 95 LYGHKGLFRRLSKADKAKVdealERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYEL 174
|
170 180 190
....*....|....*....|....*....|....*
gi 398365537 510 IRRfiLHNK-KTAFIVEHDFIMATYLADKVIVFEG 543
Cdd:cd03235 175 LRE--LRREgMTILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
368-543 |
1.48e-23 |
|
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: 97.89 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPklnvSMKPQKIApkfpgtvrqlffkKIRGq 441
Cdd:cd03214 20 LSIEAGE-----IVGILGPNGAGKSTLLKTLAGLLKPSSGeilldgKDLA----SLSPKELA-------------RKIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 442 FLnPQfqtdVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTA 521
Cdd:cd03214 77 YV-PQ----ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTV 151
|
170 180
....*....|....*....|..
gi 398365537 522 FIVEHDFIMATYLADKVIVFEG 543
Cdd:cd03214 152 VMVLHDLNLAARYADRVILLKD 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
101-294 |
1.62e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 98.69 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDPPEWQEIIKYFR---GSELQN----YFTKMLEDDIkaiikpq 171
Cdd:cd03225 25 KKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvlVDGKDLTKLSLKELRrkvGLVFQNpddqFFGPTVEEEV------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 172 yvdniprAIkGPvqkvgELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSY 251
Cdd:cd03225 98 -------AF-GL-----ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 398365537 252 LDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCII 294
Cdd:cd03225 165 LDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
358-541 |
4.93e-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: 98.18 E-value: 4.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 358 SLKKTQGDFVLNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPD------EGQDIPKL-----NVSMKPQKIApKF 426
Cdd:cd03299 5 NLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDsgkillNGKDITNLppekrDISYVPQNYA-LF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 427 P----------GTVRQLFFKK-IRGQFLNpqfqtdVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPS 495
Cdd:cd03299 84 PhmtvykniayGLKKRKVDKKeIERKVLE------IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365537 496 AYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVF 541
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIM 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
368-559 |
6.17e-23 |
|
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: 98.19 E-value: 6.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLN-------VSMKPQKIAPKFPGTVRQL- 433
Cdd:COG1120 22 LSLPPGEV-----TALLGPNGSGKSTLLRALAGLLKPSSGevlldgRDLASLSrrelarrIAYVPQEPPAPFGLTVRELv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 434 ---------FFkkirgQFLNPQFQTDVVKPLR---IDDIIDQEVQHLSGGELQRVAI--VLALGipADIYLIDEPSAYLD 499
Cdd:COG1120 97 algryphlgLF-----GRPSAEDREAVEEALErtgLEHLADRPVDELSGGERQRVLIarALAQE--PPLLLLDEPTSHLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 500 SEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVF-EGipsKNAHARAPESLLT 559
Cdd:COG1120 170 LAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLkDG---RIVAQGPPEEVLT 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
368-540 |
8.86e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 97.47 E-value: 8.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ-DIPKLNVSMKPQKIA---------PKFPGTVRQL---- 433
Cdd:COG1121 27 LTIPPGEF-----VAIVGPNGAGKSTLLKAILGLLPPTSGTvRLFGKPPRRARRRIGyvpqraevdWDFPITVRDVvlmg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 434 FFKKIR-GQFLNPQFQTDVVKPLR---IDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD--SEQRIIcs 507
Cdd:COG1121 102 RYGRRGlFRRPSRADREAVDEALErvgLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDaaTEEALY-- 179
|
170 180 190
....*....|....*....|....*....|....
gi 398365537 508 KVIRRfiLHNK-KTAFIVEHDFIMATYLADKVIV 540
Cdd:COG1121 180 ELLRE--LRREgKTILVVTHDLGAVREYFDRVLL 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
359-540 |
2.53e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.90 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 359 LKKTQGDFV------LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKpQKIA--- 423
Cdd:COG1131 6 LTKRYGDKTaldgvsLTVEPGE-----IFGLLGPNGAGKTTTIRMLLGLLRPTSGevrvlgEDVARDPAEVR-RRIGyvp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 424 --PKFPG--TVRQL--FFKKIRGqfLNPQFQT----DVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDE 493
Cdd:COG1131 80 qePALYPdlTVRENlrFFARLYG--LPRKEAReridELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398365537 494 PSAYLDSEQRiicsKVIRRFILHNK---KTAFIVEHdfIM--ATYLADKVIV 540
Cdd:COG1131 158 PTSGLDPEAR----RELWELLRELAaegKTVLLSTH--YLeeAERLCDRVAI 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
82-294 |
8.86e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 94.36 E-value: 8.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSAN------SFKLhrlptpRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--------FDDPPEWQEIIkyf 147
Cdd:COG1131 5 GLTKRYGDKtaldgvSLTV------EPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvrvlgedvARDPAEVRRRI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 148 rGSELQNYFtkmLEDDIKAIikpQYVDNIpraikgpvqkvGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGEL 227
Cdd:COG1131 76 -GYVPQEPA---LYPDLTVR---ENLRFF-----------ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMK 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 228 QRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCII 294
Cdd:COG1131 138 QRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAII 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
101-294 |
1.11e-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: 94.54 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGrfddppewqEIIKYFRGSELQNYFTK----MLEDDIkaiikpqyvdNI 176
Cdd:COG4555 25 KDGEITGLLGPNGAGKTTLLRMLAGLLKPDSG---------SILIDGEDVRKEPREARrqigVLPDER----------GL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 177 P--RAIKGPVQKVGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDV 254
Cdd:COG4555 86 YdrLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398365537 255 KQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCII 294
Cdd:COG4555 166 MARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVIL 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
82-542 |
2.51e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSAN------SFKLHrlptprPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDDPPEWQeiIKYFRgselQNY 155
Cdd:COG0488 3 NLSKSFGGRpllddvSLSIN------PGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR--IGYLP----QEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 156 FtkmLEDDIKAIikpqyvDNIPRAIKGPVQKVGELLKL--RMEKSPEDVKRYIKIL-------------QLENVLK---- 216
Cdd:COG0488 71 P---LDDDLTVL------DTVLDGDAELRALEAELEELeaKLAEPDEDLERLAELQeefealggweaeaRAEEILSglgf 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 217 ------RDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDvkqrLNAAQIIRSLLAptKY---VICVEHDLSVLDyl 287
Cdd:COG0488 142 peedldRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLK--NYpgtVLVVSHDRYFLD-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 288 sdfvciiygvpsvyGVVTLPASV-REGINIFlDGhipaeN----LRFRTEAL---------------------------- 334
Cdd:COG0488 214 --------------RVATRILELdRGKLTLY-PG-----NysayLEQRAERLeqeaaayakqqkkiakeeefirrfraka 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 335 ------QFRIaDATEDLQNDSASRAFSYPSLKKTQ----GDFVLNVEEGEFS--DSEIL-------------VMMGENGT 389
Cdd:COG0488 274 rkakqaQSRI-KALEKLEREEPPRRDKTVEIRFPPperlGKKVLELEGLSKSygDKTLLddlslridrgdriGLIGPNGA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 390 GKTTLIKLLAGALKPDEG--------------QDIPKLNVSMKP----QKIAPKF-PGTVRQLFfkkirGQFLnpqFQTD 450
Cdd:COG0488 353 GKSTLLKLLAGELEPDSGtvklgetvkigyfdQHQEELDPDKTVldelRDGAPGGtEQEVRGYL-----GRFL---FSGD 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 451 VVkplriddiiDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFilhnKKTAFIVEHD--F 528
Cdd:COG0488 425 DA---------FKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF----PGTVLLVSHDryF 491
|
570
....*....|....
gi 398365537 529 IMAtyLADKVIVFE 542
Cdd:COG0488 492 LDR--VATRILEFE 503
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
374-540 |
2.99e-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: 93.00 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 374 EFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQ----DIPKLNVSMKPQK---IAPKFPG-----TVRQ--LFFKKIR 439
Cdd:COG4555 23 TAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSilidGEDVRKEPREARRqigVLPDERGlydrlTVREniRYFAELY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 440 GQFL--NPQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDseqrIICSKVIRRFILH- 516
Cdd:COG4555 103 GLFDeeLKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD----VMARRLLREILRAl 178
|
170 180
....*....|....*....|....*.
gi 398365537 517 --NKKTAFIVEHDFIMATYLADKVIV 540
Cdd:COG4555 179 kkEGKTVLFSSHIMQEVEALCDRVVI 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
99-281 |
3.72e-21 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 90.96 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 99 TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGrfddppewqEIikYFRGSELQNYFTKMLEDDIkAIIkPQYvdnipr 178
Cdd:cd03214 21 SIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSG---------EI--LLDGKDLASLSPKELARKI-AYV-PQA------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 179 aikgpvqkvgellklrmekspedvkryIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRL 258
Cdd:cd03214 82 ---------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180
....*....|....*....|....
gi 398365537 259 NAAQIIRSLLAPT-KYVICVEHDL 281
Cdd:cd03214 135 ELLELLRRLARERgKTVVMVLHDL 158
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
101-281 |
7.32e-21 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 92.41 E-value: 7.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELQNYftkmledDIKAIIK-----PQyVDN 175
Cdd:COG1120 25 PPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEV-----------LLDGRDLASL-------SRRELARriayvPQ-EPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 176 IPRAIKgpvqkVGEL--------LKLRMEKSPED---VKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYM 244
Cdd:COG1120 86 APFGLT-----VRELvalgryphLGLFGRPSAEDreaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 398365537 245 FDEPSSYLDVKQRLNAAQIIRSLLAPTKY-VICVEHDL 281
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRtVVMVLHDL 198
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
354-543 |
8.90e-21 |
|
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: 89.75 E-value: 8.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPS-LKKTQGDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKPQKIA--- 423
Cdd:cd03228 8 FSYPGrPKPVLKDVSLTIKPGE-----KVAIVGPSGSGKSTLLKLLLRLYDPTSGeilidgVDLRDLDLESLRKNIAyvp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 424 ---PKFPGTVRqlffkkirgqflnpqfqtdvvkplriDDIidqevqhLSGGELQRVAIVLALGIPADIYLIDEPSAYLD- 499
Cdd:cd03228 83 qdpFLFSGTIR--------------------------ENI-------LSGGQRQRIAIARALLRDPPILILDEATSALDp 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398365537 500 -SEQRIIcsKVIRRfiLHNKKTAFIVEHDFIMATyLADKVIVFEG 543
Cdd:cd03228 130 eTEALIL--EALRA--LAKGKTVIVIAHRLSTIR-DADRIIVLDD 169
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
82-294 |
3.80e-20 |
|
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: 87.30 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRY------SANSFKLhrlptpRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELQNY 155
Cdd:cd00267 4 NLSFRYggrtalDNVSLTL------KAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI-----------LIDGKDIAKL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 156 FTKMLEDDIkaIIKPQyvdnipraikgpvqkvgellklrmekspedvkryikilqlenvlkrdiekLSGGELQRFAIGMS 235
Cdd:cd00267 67 PLEELRRRI--GYVPQ--------------------------------------------------LSGGQRQRVALARA 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 236 CVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCII 294
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
365-540 |
4.74e-20 |
|
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: 88.73 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKL-----NVSMKPQKIA--P------- 424
Cdd:cd03259 18 DLSLTVEPGEF-----LALLGPSGCGKTTLLRLIAGLERPDSGeilidgRDVTGVpperrNIGMVFQDYAlfPhltvaen 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 425 -KFPGTVRQLFFKKIRGQFLNpqfqtdVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQR 503
Cdd:cd03259 93 iAFGLKLRGVPKAEIRARVRE------LLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 398365537 504 IICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIV 540
Cdd:cd03259 167 EELREELKELQRELGITTIYVTHDQEEALALADRIAV 203
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
91-296 |
4.93e-20 |
|
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: 89.10 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 91 SFKLHRlptprpGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELQNYFTKMLEDDIKAIikp 170
Cdd:cd03257 25 SFSIKK------GETLGLVGESGSGKSTLARAILGLLKPTSGSI-----------IFDGKDLLKLSRRLRKIRRKEI--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 171 QYVDNIPRAIKGPVQKVGE-----LLKLRMEKSPEDVKRYI-----KILQLENVLKRDIEKLSGGELQRFAIGMSCVQEA 240
Cdd:cd03257 85 QMVFQDPMSSLNPRMTIGEqiaepLRIHGKLSKKEARKEAVllllvGVGLPEEVLNRYPHELSGGQRQRVAIARALALNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 241 DVYMFDEPSSYLDVkqrLNAAQIIRSLL-APTKY---VICVEHDLSVLDYLSDFVCIIYG 296
Cdd:cd03257 165 KLLIADEPTSALDV---SVQAQILDLLKkLQEELgltLLFITHDLGVVAKIADRVAVMYA 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
361-542 |
5.46e-20 |
|
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: 88.89 E-value: 5.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 361 KTQGDFVLNVEegeFS-DSEILVMMGENGTGKTTLIKLLAGALKPDEGQ--------DIPKLNVSMKPQ--KI------A 423
Cdd:cd03297 8 KRLPDFTLKID---FDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivlngtvlFDSRKKINLPPQqrKIglvfqqY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 424 PKFPG-TVRQ--LFFKKIRGQFLNPQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDS 500
Cdd:cd03297 85 ALFPHlNVREnlAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 398365537 501 EQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFE 542
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVME 206
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
365-540 |
5.82e-20 |
|
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: 88.47 E-value: 5.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ---------DIP--KLNVSMKPQKIA--PK------ 425
Cdd:cd03301 18 DLNLDIADGEF-----VVLLGPSGCGKTTTLRMIAGLEEPTSGRiyiggrdvtDLPpkDRDIAMVFQNYAlyPHmtvydn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 426 --FPGTVRQLFFKKIRGQFlnpqfqTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQR 503
Cdd:cd03301 93 iaFGLKLRKVPKDEIDERV------REVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 398365537 504 IICSKVIRRfiLHNK-KTAFI-VEHDFIMATYLADKVIV 540
Cdd:cd03301 167 VQMRAELKR--LQQRlGTTTIyVTHDQVEAMTMADRIAV 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
359-540 |
7.17e-20 |
|
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: 87.07 E-value: 7.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 359 LKKTQGDFV------LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKpQKIA--- 423
Cdd:cd03230 6 LSKRYGKKTalddisLTVEKGE-----IYGLLGPNGAGKTTLIKIILGLLKPDSGeikvlgKDIKKEPEEVK-RRIGylp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 424 --PKFPG--TVRQLFfkkirgqflnpqfqtdvvkplriddiidqevqHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:cd03230 80 eePSLYEnlTVRENL--------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 398365537 500 SEQRIICSKVIRRFILHNkKTAFIVEHDFIMATYLADKVIV 540
Cdd:cd03230 128 PESRREFWELLRELKKEG-KTILLSSHILEEAERLCDRVAI 167
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
101-289 |
9.72e-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: 88.71 E-value: 9.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELQNYFTKMLEDDIkaiikpQYV--DniPR 178
Cdd:COG1124 29 APGESFGLVGESGSGKSTLLRALAGLERPWSGEV-----------TFDGRPVTRRRRKAFRRRV------QMVfqD--PY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 179 AIKGPVQKVGELLK--LRMEKSPEDVKRYIKILQL----ENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYL 252
Cdd:COG1124 90 ASLHPRHTVDRILAepLRIHGLPDREERIAELLEQvglpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 398365537 253 DVkqrLNAAQIIRsLLAPTK------YVIcVEHDLSVLDYLSD 289
Cdd:COG1124 170 DV---SVQAEILN-LLKDLReergltYLF-VSHDLAVVAHLCD 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
368-496 |
2.10e-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: 85.01 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ-------------DIPKLNVSMKPQKIAPkFPG-TVRQL 433
Cdd:pfam00005 6 LTLNPGE-----ILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltdderKSLRKEIGYVFQDPQL-FPRlTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 434 FFKKIRGQFLNPQFQTDVVKPLR--------IDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSA 496
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALeklglgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
368-542 |
6.25e-19 |
|
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: 85.62 E-value: 6.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKP----QKIA---------PKFpg 428
Cdd:cd03255 25 LSIEKGEF-----VAIVGPSGSGKSTLLNILGGLDRPTSGevrvdgTDISKLSEKELAafrrRHIGfvfqsfnllPDL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 429 TVRQ-----LFFKKIRGQFLNPQFqTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQR 503
Cdd:cd03255 98 TALEnvelpLLLAGVPKKERRERA-EELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETG 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 398365537 504 IICSKVIRRFILHNKKTAFIVEHDFIMATYlADKVIVFE 542
Cdd:cd03255 177 KEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELR 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
365-542 |
6.84e-19 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 84.55 E-value: 6.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKPQKiapKFPGTVRQlffkki 438
Cdd:cd03229 18 DVSLNIEAGE-----IVALLGPSGSGKSTLLRCIAGLEEPDSGsilidgEDLTDLEDELPPLR---RRIGMVFQ------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 439 rgQF-LNPQFqtdvvkplridDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHN 517
Cdd:cd03229 84 --DFaLFPHL-----------TVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQL 150
|
170 180
....*....|....*....|....*
gi 398365537 518 KKTAFIVEHDFIMATYLADKVIVFE 542
Cdd:cd03229 151 GITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
102-293 |
6.92e-19 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 85.66 E-value: 6.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDdppewqeiikyfrgselqnYFTKMLEDDIKAI-IKPQY--VD-NIP 177
Cdd:cd03235 24 PGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR-------------------VFGKPLEKERKRIgYVPQRrsIDrDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 178 RAIK-----GPVQKVGELLKLRMEKSpEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYL 252
Cdd:cd03235 85 ISVRdvvlmGLYGHKGLFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 398365537 253 DVKQRLNAAQIIRSLLAPTKYVICVEHDL-SVLDYLSDFVCI 293
Cdd:cd03235 164 DPKTQEDIYELLRELRREGMTILVVTHDLgLVLEYFDRVLLL 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
365-547 |
2.76e-18 |
|
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: 84.06 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQdipklnvsmkpqkiapkfpgtVRqLFFKKIRGQflN 444
Cdd:cd03293 22 DISLSVEEGEF-----VALVGPSGCGKSTLLRIIAGLERPTSGE---------------------VL-VDGEPVTGP--G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 445 PQ----FQTD-----------VVKPLRIDDIIDQEVQH---------------------LSGGELQRVAIVLALGIPADI 488
Cdd:cd03293 73 PDrgyvFQQDallpwltvldnVALGLELQGVPKAEAREraeellelvglsgfenayphqLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 489 YLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFEGIPSK 547
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGR 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
354-543 |
6.53e-18 |
|
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: 87.12 E-value: 6.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQGDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKL-------NVSMKPQ 420
Cdd:COG4988 344 FSYPGGRPALDGLSLTIPPGER-----VALVGPSGAGKSTLLNLLLGFLPPYSGsilingVDLSDLdpaswrrQIAWVPQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 421 KiaPK-FPGTVRQlffkKIRgqFLNPQF-QTDVVKPLR---IDDIIDQ-------EV----QHLSGGELQRVAIVLALGI 484
Cdd:COG4988 419 N--PYlFAGTIRE----NLR--LGRPDAsDEELEAALEaagLDEFVAAlpdgldtPLgeggRGLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 485 PADIYLIDEPSAYLD--SEQRIIcsKVIRRfiLHNKKTAFIVEHDfIMATYLADKVIVFEG 543
Cdd:COG4988 491 DAPLLLLDEPTAHLDaeTEAEIL--QALRR--LAKGRTVILITHR-LALLAQADRILVLDD 546
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
368-541 |
8.67e-18 |
|
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: 82.87 E-value: 8.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIpklnVSMKPQKIA----------PK-FPG-T 429
Cdd:cd03219 21 FSVRPGE-----IHGLIGPNGAGKTTLFNLISGFLRPTSGsvlfdgEDI----TGLPPHEIArlgigrtfqiPRlFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 430 VRQ-----LFFKKIRGQFLNPQFQT---------DVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPS 495
Cdd:cd03219 92 VLEnvmvaAQARTGSGLLLARARREereareraeELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365537 496 AYLDSEQRIICSKVIRRfILHNKKTAFIVEHD--FIMAtyLADKVIVF 541
Cdd:cd03219 172 AGLNPEETEELAELIRE-LRERGITVLLVEHDmdVVMS--LADRVTVL 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
368-541 |
8.75e-18 |
|
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: 80.94 E-value: 8.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFPGTVRQLffkKIRgqflnpqf 447
Cdd:cd03216 21 LSVRRGE-----VHALLGENGAGKSTLMKILSGLYKPDSGE------ILVDGKEVSFASPRDARRA---GIA-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 448 qtdvvkplriddIIDQevqhLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRfiLHNKKTAFI-VEH 526
Cdd:cd03216 79 ------------MVYQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRR--LRAQGVAVIfISH 140
|
170
....*....|....*..
gi 398365537 527 DF--IMAtyLADKVIVF 541
Cdd:cd03216 141 RLdeVFE--IADRVTVL 155
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
353-539 |
1.11e-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: 81.92 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 353 AFSYPSLKKTQGDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQdiPKLNVSMKPQKIAPKFPGTV-- 430
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGE-----IIALTGKNGAGKTTLAKILAGLIKESSGS--ILLNGKPIKAKERRKSIGYVmq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 431 ---RQLFFKKIRGQFL--------NPQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:cd03226 79 dvdYQLFTDSVREELLlglkeldaGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398365537 500 SEQRIICSKVIRRfILHNKKTAFIVEHDFIMATYLADKVI 539
Cdd:cd03226 159 YKNMERVGELIRE-LAAQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
103-280 |
1.64e-17 |
|
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: 81.53 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLGRF--------DDPPEWQEIIKYFrgselQNYftkmleddikaIIKPQYV- 173
Cdd:cd03301 26 GEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtDLPPKDRDIAMVF-----QNY-----------ALYPHMTv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 174 -DNIPraikgpvqkvgelLKLRMEKSPED-----VKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDE 247
Cdd:cd03301 90 yDNIA-------------FGLKLRKVPKDeiderVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190
....*....|....*....|....*....|....
gi 398365537 248 PSSYLDVKQRLNAAQIIRSLLAPTKY-VICVEHD 280
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTtTIYVTHD 190
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
365-540 |
1.78e-17 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 81.78 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPD------EGQDIPKLNVSMkpqkiapkfpgtvRQLFFKKI 438
Cdd:cd03257 23 DVSFSIKKGE-----TLGLVGESGSGKSTLARAILGLLKPTsgsiifDGKDLLKLSRRL-------------RKIRRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 439 rgQF--------LNPQF--QTDVVKPLRI------------------------DDIIDQEVQHLSGGELQRVAIVLALGI 484
Cdd:cd03257 85 --QMvfqdpmssLNPRMtiGEQIAEPLRIhgklskkearkeavllllvgvglpEEVLNRYPHELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 485 PADIYLIDEPSAYLDSeqriicskVIRRFILH-------NKKTAFI-VEHDFIMATYLADKVIV 540
Cdd:cd03257 163 NPKLLIADEPTSALDV--------SVQAQILDllkklqeELGLTLLfITHDLGVVAKIADRVAV 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
82-293 |
2.11e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 82.06 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSAN------SFKLHrlptprPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR---FDDPPEWQ-EIIKYFrgse 151
Cdd:COG1121 11 NLTVSYGGRpvledvSLTIP------PGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTvrlFGKPPRRArRRIGYV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 152 lqnyftkmleddikaiikPQYVdNIPRAIkgPVqKVGELL------KLRMEKSP-----EDVKRYIKILQLENVLKRDIE 220
Cdd:COG1121 81 ------------------PQRA-EVDWDF--PI-TVRDVVlmgrygRRGLFRRPsradrEAVDEALERVGLEDLADRPIG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 221 KLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLS-VLDYLSDFVCI 293
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGaVREYFDRVLLL 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
368-540 |
2.74e-17 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 84.95 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPD---------EGQDIPKLNVSMKPQKIAPKF--------PGTV 430
Cdd:COG1123 27 LTIAPGET-----VALVGESGSGKSTLALALMGLLPHGgrisgevllDGRDLLELSEALRGRRIGMVFqdpmtqlnPVTV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 431 -RQLFFKKIRGQFLNPQFQTDVVKPLR---IDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIIC 506
Cdd:COG1123 102 gDQIAEALENLGLSRAEARARVLELLEavgLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEI 181
|
170 180 190
....*....|....*....|....*....|....
gi 398365537 507 SKVIRRFILHNKKTAFIVEHDFIMATYLADKVIV 540
Cdd:COG1123 182 LDLLRELQRERGTTVLLITHDLGVVAEIADRVVV 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
99-282 |
4.54e-17 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 80.26 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 99 TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDD------PPEWQEIIKYFrgselQNY--FTKM-LEDDIkai 167
Cdd:cd03259 22 TVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEilIDGrdvtgvPPERRNIGMVF-----QDYalFPHLtVAENI--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 168 ikpqyvdnipraikgpvqkvgeLLKLRMEKSPED-----VKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADV 242
Cdd:cd03259 94 ----------------------AFGLKLRGVPKAeirarVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 398365537 243 YMFDEPSSYLDVKQRLNAAQIIRSLLAPTKY-VICVEHDLS 282
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGItTIYVTHDQE 192
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
79-295 |
4.54e-17 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 84.57 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 79 LEA-HVTHRYSAN-----------SFKLHRlptprpGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikY 146
Cdd:COG1123 261 LEVrNLSKRYPVRgkggvravddvSLTLRR------GETLGLVGESGSGKSTLARLLLGLLRPTSGSI-----------L 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 147 FRGSELqnyfTKMLEDDIKAIIKP-QYVDNIPRAIKGPVQKVGEL----LKLRMEKSPEDVKRYIK-ILQL----ENVLK 216
Cdd:COG1123 324 FDGKDL----TKLSRRSLRELRRRvQMVFQDPYSSLNPRMTVGDIiaepLRLHGLLSRAERRERVAeLLERvglpPDLAD 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 217 RDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRlnaAQIIRSL--------LAptkyVICVEHDLSVLDYLS 288
Cdd:COG1123 400 RYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQ---AQILNLLrdlqrelgLT----YLFISHDLAVVRYIA 472
|
....*..
gi 398365537 289 DFVCIIY 295
Cdd:COG1123 473 DRVAVMY 479
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
99-281 |
5.49e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 99 TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDPPEWQeiikyFRGSELQNYFTKMleddikaiikPQyVDNI 176
Cdd:PRK11231 24 SLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTvfLGDKPISM-----LSSRQLARRLALL----------PQ-HHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 177 PRAIKgpvqkVGEL--------LKLRMEKSPED---VKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMF 245
Cdd:PRK11231 88 PEGIT-----VRELvaygrspwLSLWGRLSAEDnarVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 398365537 246 DEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDL 281
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDL 198
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
353-543 |
8.70e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 80.81 E-value: 8.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 353 AFSYPSLKKTQGDFV-LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPKLNVSMKPQKIA-- 423
Cdd:PRK13632 14 SFSYPNSENNALKNVsFEINEGEY-----VAILGHNGSGKSTISKILTGLLKPQSGEikidgiTISKENLKEIRKKIGii 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 424 ---P--KFPG-TV----------RQLFFKKIRgqflnpQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPAD 487
Cdd:PRK13632 89 fqnPdnQFIGaTVeddiafglenKKVPPKKMK------DIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365537 488 IYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATyLADKVIVFEG 543
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSE 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
368-543 |
1.16e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 79.85 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFPGTvrqlFFKKIRGQF----- 442
Cdd:COG1124 26 LEVAPGE-----SFGLVGESGSGKSTLLRALAGLERPWSGE------VTFDGRPVTRRRRKA----FRRRVQMVFqdpya 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 443 -LNPQFQTDVV--KPLRIDDIIDQEVQ-------------------H-LSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:COG1124 91 sLHPRHTVDRIlaEPLRIHGLPDREERiaelleqvglppsfldrypHqLSGGQRQRVAIARALILEPELLLLDEPTSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398365537 500 -SEQRIICSkVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFEG 543
Cdd:COG1124 171 vSVQAEILN-LLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
102-294 |
1.22e-16 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 78.88 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDD------------PPEWQEIikyfrGSELQNY--FTKMleddik 165
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivLNGtvlfdsrkkinlPPQQRKI-----GLVFQQYalFPHL------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 166 aiikpQYVDNIPRAIKGPVQKVgellklrMEKSPEDVkryIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMF 245
Cdd:cd03297 91 -----NVRENLAFGLKRKRNRE-------DRISVDEL---LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 398365537 246 DEPSSYLDVKQRLNAAQIIRSLLAPTKY-VICVEHDLSVLDYLSDFVCII 294
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIpVIFVTHDLSEAEYLADRIVVM 205
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
99-303 |
1.60e-16 |
|
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: 79.86 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 99 TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDdppewqeiikyFRGSELQNyFTKMLEDDIKAIIKPQYVDNIPR 178
Cdd:TIGR03873 23 TAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVD-----------LAGVDLHG-LSRRARARRVALVEQDSDTAVPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 179 AIKGPVQkVGEL--LKLRMEKSPED---VKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLD 253
Cdd:TIGR03873 91 TVRDVVA-LGRIphRSLWAGDSPHDaavVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 254 VKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIYG-----------------VPSVYGV 303
Cdd:TIGR03873 170 VRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGgrvvaagpprevltpalIRAVYGV 236
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
374-527 |
1.67e-16 |
|
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: 78.29 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 374 EFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPKLNVSMKPQ------KIAPKfPG-TVRQL--FFKKI 438
Cdd:COG4133 24 TLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvlwngePIRDAREDYRRRlaylghADGLK-PElTVRENlrFWAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 439 RGQFLNPQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFiLHNK 518
Cdd:COG4133 103 YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAH-LARG 181
|
....*....
gi 398365537 519 KTAFIVEHD 527
Cdd:COG4133 182 GAVLLTTHQ 190
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
358-542 |
2.80e-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: 80.54 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 358 SLKKTQGDFVLNVEEgEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQ---DIPKLNVSMKPQKIAPK--------- 425
Cdd:TIGR02142 4 RFSKRLGDFSLDADF-TLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEivlNGRTLFDSRKGIFLPPEkrrigyvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 426 ----FPG-TVRQLF---FKKIRGQFLNPQFQTdVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAY 497
Cdd:TIGR02142 83 earlFPHlSVRGNLrygMKRARPSERRISFER-VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398365537 498 LDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFE 542
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLE 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
377-540 |
2.95e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 78.18 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 377 DSEILVMMGENGTGKTTLIKLLAGALKPDEGQ-DIPKLNVSMKPQKIAPK---FPG--------TVRQ--LFFKKIRGqf 442
Cdd:cd03266 30 PGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFaTVDGFDVVKEPAEARRRlgfVSDstglydrlTAREnlEYFAGLYG-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 443 LNPQFQT----DVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDseqrIICSKVIRRFILHNK 518
Cdd:cd03266 108 LKGDELTarleELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD----VMATRALREFIRQLR 183
|
170 180
....*....|....*....|....*
gi 398365537 519 ---KTAFIVEHDFIMATYLADKVIV 540
Cdd:cd03266 184 algKCILFSTHIMQEVERLCDRVVV 208
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
365-543 |
3.48e-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: 75.56 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQdipklnvsmkpqkiaPKFPGTVRQLFFkkirgqfln 444
Cdd:cd03221 18 DISLTINPGD-----RIGLVGRNGAGKSTLLKLIAGELEPDEGI---------------VTWGSTVKIGYF--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 445 pqfqtdvvkplriddiidqevQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRiicsKVIRRFILHNKKTAFIV 524
Cdd:cd03221 69 ---------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI----EALEEALKEYPGTVILV 123
|
170
....*....|....*....
gi 398365537 525 EHDFIMATYLADKVIVFEG 543
Cdd:cd03221 124 SHDRYFLDQVATKIIELED 142
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
373-527 |
3.58e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.89 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 373 GEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEG--QDIPKLNVSMKPQKIA--PKFPGTVRQL----FFKKiRGQFLN 444
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGtvRRAGGARVAYVPQRSEvpDSLPLTVRDLvamgRWAR-RGLWRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 445 PQFQ-----TDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRfILHNKK 519
Cdd:NF040873 92 LTRDdraavDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAE-EHARGA 170
|
....*...
gi 398365537 520 TAFIVEHD 527
Cdd:NF040873 171 TVVVVTHD 178
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
354-542 |
4.12e-16 |
|
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: 78.63 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQGDFV-LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ----DIPKLNVSMKPQkiapkfpg 428
Cdd:TIGR04520 8 FSYPESEKPALKNVsLSIEKGEF-----VAIIGHNGSGKSTLAKLLNGLLLPTSGKvtvdGLDTLDEENLWE-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 429 tVRQlffkKIRGQFLNP--QF-----QTDV--------VKP----LRID---------DIIDQEVQHLSGGELQRVAI-- 478
Cdd:TIGR04520 75 -IRK----KVGMVFQNPdnQFvgatvEDDVafglenlgVPReemrKRVDealklvgmeDFRDREPHLLSGGQKQRVAIag 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 479 VLALGiPaDIYLIDEPSAYLDSEQR--IIcsKVIRRfiLH--NKKTAFIVEHDFIMATyLADKVIVFE 542
Cdd:TIGR04520 150 VLAMR-P-DIIILDEATSMLDPKGRkeVL--ETIRK--LNkeEGITVISITHDMEEAV-LADRVIVMN 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
82-291 |
4.74e-16 |
|
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: 76.91 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSAN-------SFKLHRlptprpGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF----DDPPEWQEIIKYFRGS 150
Cdd:cd03226 4 NISFSYKKGteilddlSLDLYA------GEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngKPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 151 ELQNY--FTKMLEDDIKAIIKPQYVDNipraikgpvQKVGELLKLrmekspedvkryIKILQLENVLKRDiekLSGGELQ 228
Cdd:cd03226 78 QDVDYqlFTDSVREELLLGLKELDAGN---------EQAETVLKD------------LDLYALKERHPLS---LSGGQKQ 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365537 229 RFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFV 291
Cdd:cd03226 134 RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
358-540 |
9.54e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.96 E-value: 9.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 358 SLKKTQGDFV------LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ---------DIP--KLNVSMKPQ 420
Cdd:COG3839 8 NVSKSYGGVEalkdidLDIEDGEF-----LVLLGPSGCGKSTLLRMIAGLEDPTSGEiliggrdvtDLPpkDRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 421 ------------------KIApKFPGTVRQlffKKIRgqflnpqfqtDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLAL 482
Cdd:COG3839 83 syalyphmtvyeniafplKLR-KVPKAEID---RRVR----------EAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365537 483 GIPADIYLIDEPSAYLDSEQRIicskVIRRFI--LHNK-KTAFI-VEHDFIMATYLADKVIV 540
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRV----EMRAEIkrLHRRlGTTTIyVTHDQVEAMTLADRIAV 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
368-542 |
1.42e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 76.24 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKL---------------------------- 413
Cdd:COG1136 29 LSIEAGEF-----VAIVGPSGSGKSTLLNILGGLDRPTSGevlidgQDISSLserelarlrrrhigfvfqffnllpelta 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 414 --NVSMkPQKIApKFPGTVRQlffKKIRgqflnpqfqtDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLI 491
Cdd:COG1136 104 leNVAL-PLLLA-GVSRKERR---ERAR----------ELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365537 492 DEPSAYLDSE--QRIIcsKVIRRFILHNKKTAFIVEHDFIMATYlADKVIVFE 542
Cdd:COG1136 169 DEPTGNLDSKtgEEVL--ELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLR 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
368-545 |
1.43e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 77.05 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFP--GTVRQ---LF-FKKIRGq 441
Cdd:COG1116 32 LTVAAGEF-----VALVGPSGCGKSTLLRLIAGLEKPTSGE------VLVDGKPVTGPGPdrGVVFQepaLLpWLTVLD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 442 flNpqfqtdVVKPLRIDDI----IDQEVQH-----------------LSGGELQRVAIVLALGIPADIYLIDEP-SAyLD 499
Cdd:COG1116 100 --N------VALGLELRGVpkaeRRERAREllelvglagfedayphqLSGGMRQRVAIARALANDPEVLLMDEPfGA-LD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365537 500 SEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFEGIP 545
Cdd:COG1116 171 ALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARP 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
355-547 |
1.48e-15 |
|
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: 76.57 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 355 SYPSLKKTQGDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPD------EGQDIPKLN---VSMKPQKIAPK 425
Cdd:TIGR02315 10 VYPNGKQALKNINLNINPGEF-----VAIIGPSGAGKSTLLRCINRLVEPSsgsillEGTDITKLRgkkLRKLRRRIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 426 F-------PGTV----------RQLFFKKIRGQFLNPQFQT--DVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPA 486
Cdd:TIGR02315 85 FqhynlieRLTVlenvlhgrlgYKPTWRSLLGRFSEEDKERalSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 487 DIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKV-------IVFEGIPSK 547
Cdd:TIGR02315 165 DLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIvglkageIVFDGAPSE 232
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
82-294 |
1.49e-15 |
|
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: 76.22 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSAN-------SFKLHrlptprPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDPPEWQEIIKYFR---G 149
Cdd:COG1122 5 NLSFSYPGGtpalddvSLSIE------KGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvlVDGKDITKKNLRELRrkvG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 150 SELQNY----FTKMLEDDIkaiikpqyvdniprAIkGPVQkvgelLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGG 225
Cdd:COG1122 79 LVFQNPddqlFAPTVEEDV--------------AF-GPEN-----LGLPREEIRERVEEALELVGLEHLADRPPHELSGG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 226 ELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCII 294
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVL 207
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
379-542 |
1.63e-15 |
|
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: 76.07 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 379 EILVMMGENGTGKTTLIKLLAGALK-----PDEG------QDIPKLN---------VSMKPQKIAPkFPGTVRQ--LFFK 436
Cdd:cd03260 27 EITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGevlldgKDIYDLDvdvlelrrrVGMVFQKPNP-FPGSIYDnvAYGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 437 KIRGQFLNPQFQTDVVKPLRIDDIIDqEVQ------HLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSeqriICSKVI 510
Cdd:cd03260 106 RLHGIKLKEELDERVEEALRKAALWD-EVKdrlhalGLSGGQQQRLCLARALANEPEVLLLDEPTSALDP----ISTAKI 180
|
170 180 190
....*....|....*....|....*....|....
gi 398365537 511 RRFI--LHNKKTAFIVEHDFIMATYLADKVIVFE 542
Cdd:cd03260 181 EELIaeLKKEYTIVIVTHNMQQAARVADRTAFLL 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
354-543 |
2.62e-15 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 79.49 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQ-GDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPKLN-------VSMKP 419
Cdd:COG2274 481 FRYPGDSPPVlDNISLTIKPGER-----VAIVGRSGSGKSTLLKLLLGLYEPTSGRilidgiDLRQIDpaslrrqIGVVL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 420 QKIAPkFPGTVRQ--LFFkkirgqflNPQF-QTDVVKPLR---IDDIIDQ-----------EVQHLSGGELQRVAIVLAL 482
Cdd:COG2274 556 QDVFL-FSGTIREniTLG--------DPDAtDEEIIEAARlagLHDFIEAlpmgydtvvgeGGSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365537 483 GIPADIYLIDEPSAYLD--SEQRIIcsKVIRRFIlhNKKTAFIVEHDFIMATyLADKVIVFEG 543
Cdd:COG2274 627 LRNPRILILDEATSALDaeTEAIIL--ENLRRLL--KGRTVIIIAHRLSTIR-LADRIIVLDK 684
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
380-581 |
3.00e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.82 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 380 ILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLN-------VSMKPQK-IAPKfpG-TVRQL----------F 434
Cdd:PRK11231 30 ITALIGPNGCGKSTLLKCFARLLTPQSGtvflgdKPISMLSsrqlarrLALLPQHhLTPE--GiTVRELvaygrspwlsL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 435 FKKIRGQflNPQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRfi 514
Cdd:PRK11231 108 WGRLSAE--DNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRE-- 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 515 LHNK-KTAFIVEHDFIMATYLADKVIVFEGipSKNAHARAPESLLTgcNRFLK---NLNVTFRRDPNSFRP 581
Cdd:PRK11231 184 LNTQgKTVVTVLHDLNQASRYCDHLVVLAN--GHVMAQGTPEEVMT--PGLLRtvfDVEAEIHPEPVSGTP 250
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
101-280 |
3.02e-15 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 74.85 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLG--RFD-------DPPEWQEIIKYFRgselQNYFtkMLEDDIKaiikpq 171
Cdd:COG4619 24 EAGECVAITGPSGSGKSTLLRALADLDPPTSGeiYLDgkplsamPPPEWRRQVAYVP----QEPA--LWGGTVR------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 172 yvDNIPRAikgpvqkvgelLKLRMEK-SPEDVKRYIKILQL-ENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPS 249
Cdd:COG4619 92 --DNLPFP-----------FQLRERKfDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190
....*....|....*....|....*....|..
gi 398365537 250 SYLDVKQRLNAAQIIRSLLA-PTKYVICVEHD 280
Cdd:COG4619 159 SALDPENTRRVEELLREYLAeEGRAVLWVSHD 190
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
91-250 |
3.83e-15 |
|
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: 73.07 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 91 SFKLHrlptprPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDPPEWQEIIKYFRGSelqnyftkmleddIKAIi 168
Cdd:pfam00005 5 SLTLN------PGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilLDGQDLTDDERKSLRKE-------------IGYV- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 169 kPQYVDNIPRA-IKGPVQKVGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEK----LSGGELQRFAIGMSCVQEADVY 243
Cdd:pfam00005 65 -FQDPQLFPRLtVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLL 143
|
....*..
gi 398365537 244 MFDEPSS 250
Cdd:pfam00005 144 LLDEPTA 150
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
368-559 |
3.96e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.57 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ----DIPKLNVSMK---------PQKIAPKFPGTVRQLF 434
Cdd:PRK09536 24 LSVREGSL-----VGLVGPNGAGKTTLLRAINGTLTPTAGTvlvaGDDVEALSARaasrrvasvPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 435 ---FKKIRGQFlNPQFQTD------VVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRII 505
Cdd:PRK09536 99 emgRTPHRSRF-DTWTETDraaverAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398365537 506 CSKVIRRFIlHNKKTAFIVEHDFIMATYLADKVIVFEGipSKNAHARAPESLLT 559
Cdd:PRK09536 178 TLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLAD--GRVRAAGPPADVLT 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
358-543 |
3.96e-15 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 77.06 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 358 SLKKTQGDFVLNVEEgEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEG---------QDIpKLNVSMKPQK--I---- 422
Cdd:COG4148 6 DFRLRRGGFTLDVDF-TLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGrirlggevlQDS-ARGIFLPPHRrrIgyvf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 423 --APKFPG-TVRQ-LFF--KKIRGQFLNPQFQtDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSA 496
Cdd:COG4148 84 qeARLFPHlSVRGnLLYgrKRAPRAERRISFD-EVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398365537 497 YLDSE--QRII--CSKVIRRF---ILhnkktafIVEHDFIMATYLADKVIVFEG 543
Cdd:COG4148 163 ALDLArkAEILpyLERLRDELdipIL-------YVSHSLDEVARLADHVVLLEQ 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
354-547 |
5.70e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 75.44 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKK-TQGDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGqdipklNVSMKPQKIAPKFPGTVRq 432
Cdd:PRK13635 13 FRYPDAATyALKDVSFSVYEGEW-----VAIVGHNGSGKSTLAKLLNGLLLPEAG------TITVGGMVLSEETVWDVR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 lffKKIRGQFLNP--QF-----QTDV---------------------VKPLRIDDIIDQEVQHLSGGELQRVAIVLALGI 484
Cdd:PRK13635 81 ---RQVGMVFQNPdnQFvgatvQDDVafglenigvpreemvervdqaLRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 485 PADIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYlADKVIVF-------EGIPSK 547
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMnkgeileEGTPEE 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
82-294 |
6.19e-15 |
|
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: 74.08 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSANSFK-LHRLP-TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELQNyftkm 159
Cdd:cd03263 5 NLTKTYKKGTKPaVDDLSlNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-----------YINGYSIRT----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 160 ledDIKAI-----IKPQYvDNIPRAIKgpvqkVGELLKL-------RMEKSPEDVKRYIKILQLENVLKRDIEKLSGGEL 227
Cdd:cd03263 69 ---DRKAArqslgYCPQF-DALFDELT-----VREHLRFyarlkglPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMK 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 228 QRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSlLAPTKYVICVEHDLSVLDYLSDFVCII 294
Cdd:cd03263 140 RKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIM 205
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
353-542 |
1.47e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.45 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 353 AFSYPSLKKTQ-GDFVLNVEEGEFSdseilVMMGENGTGKTTLIKLLAGALKPDegqDIPKLNVSMKPQKIAPKFPGTVR 431
Cdd:PRK13640 12 SFTYPDSKKPAlNDISFSIPRGSWT-----ALIGHNGSGKSTISKLINGLLLPD---DNPNSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 432 Q---LFFKKIRGQFLN------------------PQFQT---DVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPAD 487
Cdd:PRK13640 84 EkvgIVFQNPDNQFVGatvgddvafglenravprPEMIKivrDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 488 IYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDfIMATYLADKVIVFE 542
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHD-IDEANMADQVLVLD 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
359-543 |
2.40e-14 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 73.09 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 359 LKKTQGDFV------LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKpQKIAPKF 426
Cdd:COG1127 11 LTKSFGDRVvldgvsLDVPRGE-----ILAIIGGSGSGKSVLLKLIIGLLRPDSGeilvdgQDITGLSEKEL-YELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 427 pG------------TVRQlffkkirgqflNPQFqtdvvkPLR---------IDDIIDQ--------EVQH-----LSGGE 472
Cdd:COG1127 85 -GmlfqggalfdslTVFE-----------NVAF------PLRehtdlseaeIRELVLEklelvglpGAADkmpseLSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 473 LQRVAIVLALGIPADIYLIDEPSAYLDseqrIICSKVIRRFILH-NKK---TAFIVEHD----FIMATY---LADKVIVF 541
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLD----PITSAVIDELIRElRDElglTSVVVTHDldsaFAIADRvavLADGKIIA 222
|
..
gi 398365537 542 EG 543
Cdd:COG1127 223 EG 224
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
365-539 |
2.65e-14 |
|
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: 71.88 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPD------EGQDIPKLNvSMKPQKIAPKFPG---------- 428
Cdd:TIGR03608 16 DLNLTIEKGKM-----YAIIGESGSGKSTLLNIIGLLEKFDsgqvylNGQETPPLN-SKKASKFRREKLGylfqnfalie 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 429 --TVRQ-----LFFKKIRGQfLNPQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSE 501
Cdd:TIGR03608 90 neTVEEnldlgLKYKKLSKK-EKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398365537 502 QRiicSKVIRRFILHNK--KTAFIVEHDFIMATyLADKVI 539
Cdd:TIGR03608 169 NR---DEVLDLLLELNDegKTIIIVTHDPEVAK-QADRVI 204
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
379-545 |
2.70e-14 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 72.53 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 379 EILVMMGENGTGKTTLIKLLAGALKPD------EGQDIPKLNVSMKpQKIAPKFpGTVRQ---LFFKKIRGQflNPQFqt 449
Cdd:cd03261 27 EILAIIGPSGSGKSTLLRLIVGLLRPDsgevliDGEDISGLSEAEL-YRLRRRM-GMLFQsgaLFDSLTVFE--NVAF-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 450 dvvkPLR---------IDDII-------------DQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSeqriICS 507
Cdd:cd03261 101 ----PLRehtrlseeeIREIVlekleavglrgaeDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP----IAS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365537 508 KVIRRFILHNKK----TAFIVEHDFIMATYLADKV-------IVFEGIP 545
Cdd:cd03261 173 GVIDDLIRSLKKelglTSIMVTHDLDTAFAIADRIavlydgkIVAEGTP 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
354-540 |
2.85e-14 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 75.79 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQGDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKPQKIA--PK 425
Cdd:TIGR02857 329 VAYPGRRPALRPVSFTVPPGE-----RVALVGPSGAGKSTLLNLLLGFVDPTEGsiavngVPLADADADSWRDQIAwvPQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 426 ----FPGTVRQ--LFFKK----------IRGQFLNPQFQTdvvKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIY 489
Cdd:TIGR02857 404 hpflFAGTIAEniRLARPdasdaeireaLERAGLDEFVAA---LPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365537 490 LIDEPSAYLD--SEQRIIcsKVIRRfiLHNKKTAFIVEHDfIMATYLADKVIV 540
Cdd:TIGR02857 481 LLDEPTAHLDaeTEAEVL--EALRA--LAQGRTVLLVTHR-LALAALADRIVV 528
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
359-542 |
2.93e-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: 72.76 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 359 LKKTQGDFV-LNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQ-----------DIPKLNVSMKPQKIAPKF 426
Cdd:cd03296 8 VSKRFGDFVaLDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTilfggedatdvPVQERNVGFVFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 427 PGTVRQ--LFFKKIRGQFLNPQFQT------DVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYL 498
Cdd:cd03296 88 HMTVFDnvAFGLRVKPRSERPPEAEirakvhELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365537 499 DSEQRiicsKVIRRFI--LHNKK--TAFIVEHDFIMATYLADKVIVFE 542
Cdd:cd03296 168 DAKVR----KELRRWLrrLHDELhvTTVFVTHDQEEALEVADRVVVMN 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
354-543 |
2.98e-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: 72.24 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYP-SLKKTQGDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPKLNVSMKPQKIapkf 426
Cdd:cd03245 10 FSYPnQEIPALDNVSLTIRAGEK-----VAIIGRVGSGKSTLLKLLAGLYKPTSGSvlldgtDIRQLDPADLRRNI---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 427 pGTVRQ---LFFKKIRGQF-LNPQFQTD-----VVKPLRIDDII-------DQEV----QHLSGGELQRVAIVLALGIPA 486
Cdd:cd03245 81 -GYVPQdvtLFYGTLRDNItLGAPLADDerilrAAELAGVTDFVnkhpnglDLQIgergRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 487 DIYLIDEPSAYLD--SEQRIIcsKVIRRFILHnkKTAFIVEHDFIMATyLADKVIVFEG 543
Cdd:cd03245 160 PILLLDEPTSAMDmnSEERLK--ERLRQLLGD--KTLIIITHRPSLLD-LVDRIIVMDS 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
82-294 |
4.17e-14 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 71.46 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRY----SANSFKLhRLPtprPGqVLGLVGTNGIGKSTALKILAGKQKPNLGRF--------DDPPEWQEIIKY--- 146
Cdd:cd03264 5 NLTKRYgkkrALDGVSL-TLG---PG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIridgqdvlKQPQKLRRRIGYlpq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 147 -------FRGSELQNYFTkmleddikaiikpqyvdniprAIKGPVQKvgellklrmeKSPEDVKRYIKILQLENVLKRDI 219
Cdd:cd03264 80 efgvypnFTVREFLDYIA---------------------WLKGIPSK----------EVKARVDEVLELVNLGDRAKKKI 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 220 EKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSlLAPTKYVICVEHDLSVLDYLSDFVCII 294
Cdd:cd03264 129 GSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSE-LGEDRIVILSTHIVEDVESLCNQVAVL 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
101-257 |
4.35e-14 |
|
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: 71.88 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDppewQEIIK---YFRGSEL--QNY--FTKMleddikaiikpq 171
Cdd:cd03300 24 KEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEilLDG----KDITNlppHKRPVNTvfQNYalFPHL------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 172 yvdNIPRAIKGPvqkvgellkLRMEKSPED-----VKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFD 246
Cdd:cd03300 88 ---TVFENIAFG---------LRLKKLPKAeikerVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170
....*....|.
gi 398365537 247 EPSSYLDVKQR 257
Cdd:cd03300 156 EPLGALDLKLR 166
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
82-295 |
4.66e-14 |
|
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: 70.50 E-value: 4.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSAN------SFKLhrlptpRPGQVLGLVGTNGIGKSTALKILAGkqkpnlgrfddppewqeIIKYFRGSelqny 155
Cdd:cd03230 5 NLSKRYGKKtalddiSLTV------EKGEIYGLLGPNGAGKTTLIKIILG-----------------LLKPDSGE----- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 156 ftkmleddikAIIKPQYVDNIPRAIKgpvQKVGELlklrmeksPEDVKRYIKILQLENVlkrdieKLSGGELQRFAIGMS 235
Cdd:cd03230 57 ----------IKVLGKDIKKEPEEVK---RRIGYL--------PEEPSLYENLTVRENL------KLSGGMKQRLALAQA 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 236 CVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIY 295
Cdd:cd03230 110 LLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILN 169
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
368-543 |
7.44e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.65 E-value: 7.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQdipkLNVSMkpqKIA----------PKFpgTVRQ-LFFk 436
Cdd:COG1134 47 FEVERGE-----SVGIIGRNGAGKSTLLKLIAGILEPTSGR----VEVNG---RVSallelgagfhPEL--TGREnIYL- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 437 kiRGQFLNpqFQTDVVKPlRIDDI---------IDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICS 507
Cdd:COG1134 112 --NGRLLG--LSRKEIDE-KFDEIvefaelgdfIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCL 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 398365537 508 KVIRRFIlHNKKTAFIVEHDFIMATYLADKVIVFEG 543
Cdd:COG1134 187 ARIRELR-ESGRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
365-511 |
1.16e-13 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 70.61 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ------------DIPKLNVSMKPQK--IAPKFpgTV 430
Cdd:cd03263 20 DLSLNVYKGE-----IFGLLGHNGAGKTTTLKMLTGELRPTSGTayingysirtdrKAARQSLGYCPQFdaLFDEL--TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 431 RQL--FFKKIRGQFLNPQFQ--TDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSE-QRII 505
Cdd:cd03263 93 REHlrFYARLKGLPKSEIKEevELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAsRRAI 172
|
....*.
gi 398365537 506 CSKVIR 511
Cdd:cd03263 173 WDLILE 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
368-546 |
1.17e-13 |
|
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: 70.54 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPD------EGQDIPKLnvsmKPQKIA-------PK----FPG-T 429
Cdd:cd03224 21 LTVPEGE-----IVALLGRNGAGKTTLLKTIMGLLPPRsgsirfDGRDITGL----PPHERAragigyvPEgrriFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 430 VRQ-----LFFKKIRGqflnPQFQTDVVKPL--RIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLdseQ 502
Cdd:cd03224 92 VEEnlllgAYARRRAK----RKARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL---A 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365537 503 RIICSKVIRRFILHNKK--TAFIVEHDFIMATYLADKV-------IVFEGIPS 546
Cdd:cd03224 165 PKIVEEIFEAIRELRDEgvTILLVEQNARFALEIADRAyvlergrVVLEGTAA 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
82-294 |
1.19e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 70.47 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSANSFKLHRLP----TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR-----FD---DPPEWQEIIKYFRG 149
Cdd:cd03266 6 ALTKRFRDVKKTVQAVDgvsfTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgFDvvkEPAEARRRLGFVSD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 150 SElqnyftkMLEDDIKAIIKPQYVDNI----PRAIKGPVQKVgellklrmekspedvkryIKILQLENVLKRDIEKLSGG 225
Cdd:cd03266 86 ST-------GLYDRLTARENLEYFAGLyglkGDELTARLEEL------------------ADRLGMEELLDRRVGGFSTG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 226 ELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCII 294
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
359-543 |
1.33e-13 |
|
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: 70.25 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 359 LKKTQGDFV------LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ--------DIPKLNVSMKPQKIap 424
Cdd:cd03262 6 LHKSFGDFHvlkgidLTVKKGE-----VVVIIGPSGSGKSTLLRCINLLEEPDSGTiiidglklTDDKKNINELRQKV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 425 kfpGTVRQLF--F-------------KKIRGQflnPQFQ-----TDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGI 484
Cdd:cd03262 79 ---GMVFQQFnlFphltvlenitlapIKVKGM---SKAEaeeraLELLEKVGLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 485 PADIYLIDEPSAYLDSEQRIICSKVIRRfILHNKKTAFIVEHDFIMATYLADKVIVFEG 543
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKD-LAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
354-543 |
1.47e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 73.66 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPS----LKktqgDFVLNVEEGEFsdseI-LVmmGENGTGKTTLIKLLAGALKPDEG------QDIPKL-------NV 415
Cdd:COG1132 347 FSYPGdrpvLK----DISLTIPPGET----VaLV--GPSGSGKSTLVNLLLRFYDPTSGrilidgVDIRDLtleslrrQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 416 SMKPQKiAPKFPGTVRQlffkKIRgqFLNPQF-QTDVVKPLR---IDDII-------DQEV----QHLSGGELQRVAIVL 480
Cdd:COG1132 417 GVVPQD-TFLFSGTIRE----NIR--YGRPDAtDEEVEEAAKaaqAHEFIealpdgyDTVVgergVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 481 ALGIPADIYLIDEPSAYLD--SEQRIIcsKVIRRfiLHNKKTAFIVEHDF--IMAtylADKVIVFEG 543
Cdd:COG1132 490 ALLKDPPILILDEATSALDteTEALIQ--EALER--LMKGRTTIVIAHRLstIRN---ADRILVLDD 549
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
103-294 |
1.83e-13 |
|
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: 70.06 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLGRF--------DDPPEWQEIIKYFrgselQNY--FTKMledDIKaiikpqy 172
Cdd:cd03299 25 GDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngkditNLPPEKRDISYVP-----QNYalFPHM---TVY------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 173 vDNIPRAikgpvqkvgelLKLRMEKSPEDVKRYIKI---LQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPS 249
Cdd:cd03299 90 -KNIAYG-----------LKKRKVDKKEIERKVLEIaemLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365537 250 SYLDVKQRLNA----AQIIRSLLAPtkyVICVEHDLSVLDYLSDFVCII 294
Cdd:cd03299 158 SALDVRTKEKLreelKKIRKEFGVT---VLHVTHDFEEAWALADKVAIM 203
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
81-294 |
2.17e-13 |
|
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: 69.62 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 81 AHVTHRYSAN------SFKLHRlptprpGQVLGLVGTNGIGKSTALKILAGKQKPNLG--RFDDPPEwqeiikyfrGSEL 152
Cdd:cd03269 4 ENVTKRFGRVtalddiSFSVEK------GEIFGLLGPNGAGKTTTIRMILGIILPDSGevLFDGKPL---------DIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 153 QNYFTKMLEDdikaiikpqyvdnipraiKG--PVQKVGELLK-------LRMEKSPEDVKRYIKILQLENVLKRDIEKLS 223
Cdd:cd03269 69 RNRIGYLPEE------------------RGlyPKMKVIDQLVylaqlkgLKKEEARRRIDEWLERLELSEYANKRVEELS 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 224 GGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCII 294
Cdd:cd03269 131 KGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
366-539 |
2.45e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 69.74 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 366 FVLNveEGEFSdseilVMMGENGTGKTTLIKLLAGALKPD------EGQDIPKLNVSMKPQKIA-----PK-FPGTVRQ- 432
Cdd:PRK10247 28 FSLR--AGEFK-----LITGPSGCGKSTLLKIVASLISPTsgtllfEGEDISTLKPEIYRQQVSycaqtPTlFGDTVYDn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 -LFFKKIRGQFLNPQ-FQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVI 510
Cdd:PRK10247 101 lIFPWQIRNQQPDPAiFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEII 180
|
170 180
....*....|....*....|....*....
gi 398365537 511 RRFILHNKKTAFIVEHDFIMATYlADKVI 539
Cdd:PRK10247 181 HRYVREQNIAVLWVTHDKDEINH-ADKVI 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
355-546 |
2.60e-13 |
|
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: 69.90 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 355 SYPSLKKTQGDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKPQ---KIAPK 425
Cdd:cd03256 9 TYPNGKKALKDVSLSINPGEF-----VALIGPSGAGKSTLLRCLNGLVEPTSGsvlidgTDINKLKGKALRQlrrQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 426 FPG-------TV----------RQLFFKKIRGQFlNPQfqtDVVKPLR------IDDIIDQEVQHLSGGELQRVAIVLAL 482
Cdd:cd03256 84 FQQfnlierlSVlenvlsgrlgRRSTWRSLFGLF-PKE---EKQRALAalervgLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365537 483 GIPADIYLIDEPSAYLD--SEQRIIcsKVIRRFILHNKKTAFIVEHDFIMATYLADKV-------IVFEGIPS 546
Cdd:cd03256 160 MQQPKLILADEPVASLDpaSSRQVM--DLLKRINREEGITVIVSLHQVDLAREYADRIvglkdgrIVFDGPPA 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
374-541 |
3.16e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 374 EFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQ--------DIPKLNVSMKPQKIAPKFPGTVRQLFFKKIRGQFLNP 445
Cdd:PRK13638 23 DFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAvlwqgkplDYSKRGLLALRQQVATVFQDPEQQIFYTDIDSDIAFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 446 QFQTDVVK---PLRIDD---IID------QEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRf 513
Cdd:PRK13638 103 LRNLGVPEaeiTRRVDEaltLVDaqhfrhQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRR- 181
|
170 180
....*....|....*....|....*...
gi 398365537 514 ILHNKKTAFIVEHDFIMATYLADKVIVF 541
Cdd:PRK13638 182 IVAQGNHVIISSHDIDLIYEISDAVYVL 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
101-289 |
3.17e-13 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 69.39 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELqnyfTKMLEDDIKA--------IIKP-- 170
Cdd:cd03219 24 RPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-----------LFDGEDI----TGLPPHEIARlgigrtfqIPRLfp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 171 -QYV-DN--IPRAIKGPVQKVGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFD 246
Cdd:cd03219 89 eLTVlENvmVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 398365537 247 EPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSD 289
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLAD 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
368-548 |
3.73e-13 |
|
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: 69.42 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGqdipklNVSMKPQKIAPkfPGTVRQLFFKKI-----RGQF 442
Cdd:TIGR01184 6 LTIQQGEF-----ISLIGHSGCGKSTLLNLISGLAQPTSG------GVILEGKQITE--PGPDRMVVFQNYsllpwLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 443 LNPQFQTDVVKPLR--------IDDIID----QEVQH-----LSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRII 505
Cdd:TIGR01184 73 ENIALAVDRVLPDLskserraiVEEHIAlvglTEAADkrpgqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 398365537 506 CSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFEGIPSKN 548
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAAN 195
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
101-284 |
5.37e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.03 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDDppewqeiikyfRGSELQNYFTKMLEDDikaiikpqyvDNIPRAI 180
Cdd:NF040873 16 PAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR-----------AGGARVAYVPQRSEVP----------DSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 181 KGPV-----QKVGELLKLRMEKSpEDVKRYIKILQLENVLKRDIEKLSGGELQR--FAIGMscVQEADVYMFDEPSSYLD 253
Cdd:NF040873 75 RDLVamgrwARRGLWRRLTRDDR-AAVDDALERVGLADLAGRQLGELSGGQRQRalLAQGL--AQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|.
gi 398365537 254 VKQRLNAAQIIRSLLAPTKYVICVEHDLSVL 284
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
379-543 |
5.48e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.42 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 379 EILVMMGENGTGKTTLIKLLAGALKPDEGQ----DIPKlnVSMKPQKIA------PK-----FPGTVRQLffkkIR---- 439
Cdd:PRK13548 29 EVVAILGPNGAGKSTLLRALSGELSPDSGEvrlnGRPL--ADWSPAELArrravlPQhsslsFPFTVEEV----VAmgra 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 440 -GQFLNPQFQTDVVKPLRIDDII---DQEVQHLSGGELQRV--AIVLA-LGIPAD---IYLIDEPSAYLDSEQRIICSKV 509
Cdd:PRK13548 103 pHGLSRAEDDALVAAALAQVDLAhlaGRDYPQLSGGEQQRVqlARVLAqLWEPDGpprWLLLDEPTSALDLAHQHHVLRL 182
|
170 180 190
....*....|....*....|....*....|....
gi 398365537 510 IRRFILHNKKTAFIVEHDFIMATYLADKVIVFEG 543
Cdd:PRK13548 183 ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
365-542 |
6.25e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.89 E-value: 6.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLL-------AGAL-----------KPDEGQdIPKL--NVSMKPQK--I 422
Cdd:PRK11124 20 DITLDCPQGE-----TLVLLGPSGAGKSSLLRVLnllemprSGTLniagnhfdfskTPSDKA-IRELrrNVGMVFQQynL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 423 APKFpgTVRQLFFK---KIRGqFLNPQFQTD---VVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSA 496
Cdd:PRK11124 94 WPHL--TVQQNLIEapcRVLG-LSKDQALARaekLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365537 497 YLDSEqriICSKV--IRRFILHNKKTAFIVEHDFIMATYLADKVIVFE 542
Cdd:PRK11124 171 ALDPE---ITAQIvsIIRELAETGITQVIVTHEVEVARKTASRVVYME 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
358-543 |
7.55e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 70.13 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 358 SLKKTQGDFV------LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKL-----NVSMKPQ 420
Cdd:COG3842 10 NVSKRYGDVTalddvsLSIEPGEF-----VALLGPSGCGKTTLLRMIAGFETPDSGrilldgRDVTGLppekrNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 421 KIApKFPG-TVRQ--LFFKKIRGqfLNPQFQTDVVKPL----RIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDE 493
Cdd:COG3842 85 DYA-LFPHlTVAEnvAFGLRMRG--VPKAEIRARVAELlelvGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398365537 494 P-SAyLDSEQRIICSKVIRRfILHNKKTAFI-VEHDFIMATYLADKVIVFEG 543
Cdd:COG3842 162 PlSA-LDAKLREEMREELRR-LQRELGITFIyVTHDQEEALALADRIAVMND 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
358-541 |
8.09e-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: 68.42 E-value: 8.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 358 SLKKTQGDFV------LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ---------DIP--KLNVSMKPQ 420
Cdd:cd03300 5 NVSKFYGGFValdgvsLDIKEGEF-----FTLLGPSGCGKTTLLRLIAGFETPTSGEilldgkditNLPphKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 421 KIApKFPG-TVRQ-----LFFKKIRGQFLNPQFqTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEP 494
Cdd:cd03300 80 NYA-LFPHlTVFEniafgLRLKKLPKAEIKERV-AEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365537 495 SAYLDSEQRIICSKVIRRfiLHNK-KTAFI-VEHDFIMATYLADKVIVF 541
Cdd:cd03300 158 LGALDLKLRKDMQLELKR--LQKElGITFVfVTHDQEEALTMSDRIAVM 204
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
354-542 |
8.88e-13 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 66.95 E-value: 8.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYP-SLKKTQGDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIApKFPGTVRQ 432
Cdd:cd03247 8 FSYPeQEQQVLKNLSLELKQGEK-----IALLGRSGSGKSTLLQLLTGDLKPQQGE------ITLDGVPVS-DLEKALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 LFfkkirgQFLNPqfqtdvvKPLRIDDIIDQEV-QHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDseqRIICSKVIR 511
Cdd:cd03247 76 LI------SVLNQ-------RPYLFDTTLRNNLgRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD---PITERQLLS 139
|
170 180 190
....*....|....*....|....*....|..
gi 398365537 512 RFILHNK-KTAFIVEHDFIMATYlADKVIVFE 542
Cdd:cd03247 140 LIFEVLKdKTLIWITHHLTGIEH-MDKILFLE 170
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
380-504 |
9.46e-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: 67.60 E-value: 9.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 380 ILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMK------PQKIA--PKFpgTVRQL-----FFKKIRG 440
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPSSGtiridgQDVLKQPQKLRrrigylPQEFGvyPNF--TVREFldyiaWLKGIPS 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 441 QFLNPQFQtDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLAL-GIPaDIYLIDEPSAYLDSEQRI 504
Cdd:cd03264 105 KEVKARVD-EVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALvGDP-SILIVDEPTAGLDPEERI 167
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
374-542 |
1.02e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.12 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 374 EFSDSEILVMMGENGTGKTTLIKLL-------AGAL-----------KPDEGQdIPKL--NVSMKPQK--IAPKFpgTVR 431
Cdd:COG4161 24 ECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLniaghqfdfsqKPSEKA-IRLLrqKVGMVFQQynLWPHL--TVM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 432 Q-LFFKKIRGQFLNPQFQTD----VVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEqriIC 506
Cdd:COG4161 101 EnLIEAPCKVLGLSKEQAREkamkLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE---IT 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 398365537 507 SKV--IRRFILHNKKTAFIVEHDFIMATYLADKVIVFE 542
Cdd:COG4161 178 AQVveIIRELSQTGITQVIVTHEVEFARKVASQVVYME 215
|
|
| urea_trans_UrtD |
TIGR03411 |
urea ABC transporter, ATP-binding protein UrtD; Members of this protein family are ABC ... |
101-291 |
1.09e-12 |
|
urea ABC transporter, ATP-binding protein UrtD; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274568 [Multi-domain] Cd Length: 242 Bit Score: 67.97 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELqnyfTKMLEDDI----------KAIIKP 170
Cdd:TIGR03411 26 DPGELRVIIGPNGAGKTTMMDVITGKTRPDEGSV-----------LFGGTDL----TGLPEHQIaragigrkfqKPTVFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 171 QYV--DNIPRAIKGPvQKVGELLKLRMEKSPED-VKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDE 247
Cdd:TIGR03411 91 NLTvfENLELALPRD-KSVFASLFFRLSAEEKDrIEEVLETIGLADEADRLAGLLSHGQKQWLEIGMLLMQDPKLLLLDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 398365537 248 PSSYLDVKQRLNAAQIIRSlLAPTKYVICVEHDLSVLDYLSDFV 291
Cdd:TIGR03411 170 PVAGMTDEETEKTAELLKS-LAGKHSVVVVEHDMEFVRSIADKV 212
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
102-291 |
1.35e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 67.83 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELqnyfTKMLEDDI-------K----AIIKP 170
Cdd:COG4674 35 PGELRVIIGPNGAGKTTLMDVITGKTRPDSGSV-----------LFGGTDL----TGLDEHEIarlgigrKfqkpTVFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 171 QYV-DNIPRAIKGPVqKVGELLKLRMekSPEDVKRYIKIL---QLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFD 246
Cdd:COG4674 100 LTVfENLELALKGDR-GVFASLFARL--TAEERDRIEEVLetiGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398365537 247 EPSSYLDVKQRLNAAQIIRSlLAPTKYVICVEHDLsvldylsDFV 291
Cdd:COG4674 177 EPVAGMTDAETERTAELLKS-LAGKHSVVVVEHDM-------EFV 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
368-542 |
2.15e-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: 66.79 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGqdipKLNVSMkpqKIAPKF-------PG-TVRQ-LFFkki 438
Cdd:cd03220 43 FEVPRGE-----RIGLIGRNGAGKSTLLRLLAGIYPPDSG----TVTVRG---RVSSLLglgggfnPElTGREnIYL--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 439 RGQFLNpqfQTDVVKPLRIDDI---------IDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKV 509
Cdd:cd03220 108 NGRLLG---LSRKEIDEKIDEIiefselgdfIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRR 184
|
170 180 190
....*....|....*....|....*....|...
gi 398365537 510 IRRFILHNkKTAFIVEHDFIMATYLADKVIVFE 542
Cdd:cd03220 185 LRELLKQG-KTVILVSHDPSSIKRLCDRALVLE 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
82-296 |
2.28e-12 |
|
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: 67.52 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSANSF--KLHRLP-------TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRG--- 149
Cdd:TIGR02769 7 DVTHTYRTGGLfgAKQRAPvltnvslSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTV-----------SFRGqdl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 150 SELQNYFTKMLEDDIKAIIKPQYVDNIPRAIKGpvQKVGELLK--LRMEKSpEDVKRYIKILQL----ENVLKRDIEKLS 223
Cdd:TIGR02769 76 YQLDRKQRRAFRRDVQLVFQDSPSAVNPRMTVR--QIIGEPLRhlTSLDES-EQKARIAELLDMvglrSEDADKLPRQLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 224 GGELQRFAIGMSCVQEADVYMFDEPSSYLDvkqRLNAAQIIRSLLA-----PTKYVIcVEHDLSVLDYLSDFVCIIYG 296
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLD---MVLQAVILELLRKlqqafGTAYLF-ITHDLRLVQSFCQRVAVMDK 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
354-543 |
2.36e-12 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 66.94 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQGDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKPQKI----- 422
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEF-----LVLIGPSGSGKTTTMKMINRLIEPTSGeifidgEDIREQDPVELRRKIgyviq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 423 -APKFP--------GTVRQLFfkkirgQFLNPQFQTDVVKPLRIDDIIDQEVQH-----LSGGELQRVAIVLALGIPADI 488
Cdd:cd03295 83 qIGLFPhmtveeniALVPKLL------KWPKEKIRERADELLALVGLDPAEFADrypheLSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 489 YLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFEG 543
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
365-542 |
2.53e-12 |
|
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: 66.36 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPKLNVSMKPQKIAPK----FPG-TVRQ- 432
Cdd:cd03298 16 HFDLTFAQGE-----ITAIVGPSGSGKSTLLNLIAGFETPQSGRvlingvDVTAAPPADRPVSMLFQennlFAHlTVEQn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 LFFKKIRGQFLNPQFQTDVVKPLR---IDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKV 509
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALArvgLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|...
gi 398365537 510 IRRFILHNKKTAFIVEHDFIMATYLADKVIVFE 542
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLD 203
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
359-499 |
3.11e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 68.36 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 359 LKKTQGDFVLNVEEgEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQ---------DIPKlNVSMKPQK--Iapkfp 427
Cdd:PRK11144 6 FKQQLGDLCLTVNL-TLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRivlngrvlfDAEK-GICLPPEKrrI----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 428 GTVRQ---LF-FKKIRG-------QFLNPQFQtDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSA 496
Cdd:PRK11144 79 GYVFQdarLFpHYKVRGnlrygmaKSMVAQFD-KIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
...
gi 398365537 497 YLD 499
Cdd:PRK11144 158 SLD 160
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
354-543 |
4.52e-12 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 66.09 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQGDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPKLNVSMKPQKIA--PK 425
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGET-----VAIVGPTGAGKTTLINLLMRFYDPQKGQilidgiDIRDISRKSLRSMIGvvLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 426 ----FPGTVRQlffkKIRgqFLNPQFQTDVV----KPLRIDDII-------DQEVQH----LSGGELQRVAIVLALGIPA 486
Cdd:cd03254 85 dtflFSGTIME----NIR--LGRPNATDEEVieaaKEAGAHDFImklpngyDTVLGEnggnLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 487 DIYLIDEPSAYLDSEQRIICSKVIRRfiLHNKKTAFIVEHDfiMATYL-ADKVIVFEG 543
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEK--LMKGRTSIIIAHR--LSTIKnADKILVLDD 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
82-286 |
5.77e-12 |
|
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: 65.59 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSANSFKLHRLPTP----RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELQNYFT 157
Cdd:cd03255 5 NLSKTYGGGGEKVQALKGVslsiEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEV-----------RVDGTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 158 KMLeDDIKA----IIKPQY--------VDNIpraikgpvqkvgEL-LKLRMEKSPEDVKRYIKILQ---LENVLKRDIEK 221
Cdd:cd03255 74 KEL-AAFRRrhigFVFQSFnllpdltaLENV------------ELpLLLAGVPKKERRERAEELLErvgLGDRLNHYPSE 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365537 222 LSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPT-KYVICVEHDLSVLDY 286
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHDPELAEY 206
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
368-540 |
6.67e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 66.34 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ-DIPKLNVSMKP---------QKIAPKFPGTVRQLFFKK 437
Cdd:PRK13646 28 TEFEQGKY-----YAIVGQTGSGKSTLIQNINALLKPTTGTvTVDDITITHKTkdkyirpvrKRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 438 IRGQFL----NPQFQTDVVKP----LRID-----DIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRI 504
Cdd:PRK13646 103 VEREIIfgpkNFKMNLDEVKNyahrLLMDlgfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKR 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 398365537 505 ICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIV 540
Cdd:PRK13646 183 QVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIV 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
353-564 |
7.38e-12 |
|
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: 68.25 E-value: 7.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 353 AFSYPSLKKTQ-GDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPKLN-------VSMK 418
Cdd:COG4987 340 SFRYPGAGRPVlDGLSLTLPPGE-----RVAIVGPSGSGKSTLLALLLRFLDPQSGSitlggvDLRDLDeddlrrrIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 419 PQKiAPKFPGTVRQ-LffkkirgQFLNPQfQTD-----VVKPLRIDDIIDQEVQ-----------HLSGGELQRVAIVLA 481
Cdd:COG4987 415 PQR-PHLFDTTLREnL-------RLARPD-ATDeelwaALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 482 LGIPADIYLIDEPSAYLD--SEQRIIcsKVIRRfILHNkKTAFIVEHDFIMATyLADKVIVFEGipSKNAHARAPESLLT 559
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDaaTEQALL--ADLLE-ALAG-RTVLLITHRLAGLE-RMDRILVLED--GRIVEQGTHEELLA 558
|
....*
gi 398365537 560 GCNRF 564
Cdd:COG4987 559 QNGRY 563
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
365-555 |
7.52e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 66.04 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPkfPGTVRQLFFKKirgQFLN 444
Cdd:COG4525 25 DVSLTIESGEF-----VVALGASGCGKTTLLNLIAGFLAPSSGE------ITLDGVPVTG--PGADRGVVFQK---DALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 445 P--QFQTDVVKPLRI---------------------DDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDS- 500
Cdd:COG4525 89 PwlNVLDNVAFGLRLrgvpkaerraraeellalvglADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAl 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 501 --EQriicskvIRRFIL----HNKKTAFIVEHDFIMATYLADKVIVFEGIPSKNAHARAPE 555
Cdd:COG4525 169 trEQ-------MQELLLdvwqRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELD 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
368-540 |
7.54e-12 |
|
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: 65.43 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQdipklnvsmkpQKIAPKFPGTVRQLFFKKI------RGQ 441
Cdd:cd03267 42 FTIEKGE-----IVGFIGPNGAGKTTTLKILSGLLQPTSGE-----------VRVAGLVPWKRRKKFLRRIgvvfgqKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 442 F------------------LNP-QFQTDV---VKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:cd03267 106 LwwdlpvidsfyllaaiydLPPaRFKKRLdelSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398365537 500 seqrIICSKVIRRFIL-HNKK---TAFIVEHDFIMATYLADKVIV 540
Cdd:cd03267 186 ----VVAQENIRNFLKeYNRErgtTVLLTSHYMKDIEALARRVLV 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
365-543 |
7.96e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.98 E-value: 7.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ---------DIP--KLNVSMKPQKIA--P------- 424
Cdd:PRK11000 21 DINLDIHEGEF-----VVFVGPSGCGKSTLLRMIAGLEDITSGDlfigekrmnDVPpaERGVGMVFQSYAlyPhlsvaen 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 425 -----KFPGTvrqlffKKIRGQflnpQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:PRK11000 96 msfglKLAGA------KKEEIN----QRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365537 500 S----EQRIICSKVIRRFilhnKKTAFIVEHDFIMATYLADKVIVFEG 543
Cdd:PRK11000 166 AalrvQMRIEISRLHKRL----GRTMIYVTHDQVEAMTLADKIVVLDA 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
82-284 |
9.73e-12 |
|
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: 67.94 E-value: 9.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSAN--------SFKLhrlptpRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FD-------DPPEWQEII 144
Cdd:COG2274 478 NVSFRYPGDsppvldniSLTI------KPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRilIDgidlrqiDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 145 KYFrgseLQNYFtkMLEDDIKaiikpqyvDNI----PRAikgpvqkvgellklrmekSPEDVKRYIKILQLEnvlkRDIE 220
Cdd:COG2274 552 GVV----LQDVF--LFSGTIR--------ENItlgdPDA------------------TDEEIIEAARLAGLH----DFIE 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 221 K---------------LSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKqrlNAAQIIRSLLAPTKY--VICVEHDLSV 283
Cdd:COG2274 596 AlpmgydtvvgeggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAE---TEAIILENLRRLLKGrtVIIIAHRLST 672
|
.
gi 398365537 284 L 284
Cdd:COG2274 673 I 673
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
94-308 |
1.10e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 94 LHRLPTPRP-GQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDPPewqeiikyfrgseLQNYFTKMLEDDIKAIikP 170
Cdd:PRK10575 27 LHPLSLTFPaGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEilLDAQP-------------LESWSSKAFARKVAYL--P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 171 QyvdNIPRAIKGPVQKV---------GELLKLRMEKSpEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEAD 241
Cdd:PRK10575 92 Q---QLPAAEGMTVRELvaigrypwhGALGRFGAADR-EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 242 VYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKY-VICVEHDLSV----LDYL-------------------SDFVCIIYGV 297
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLtVIAVLHDINMaaryCDYLvalrggemiaqgtpaelmrGETLEQIYGI 247
|
250
....*....|.
gi 398365537 298 PsvYGVVTLPA 308
Cdd:PRK10575 248 P--MGILPHPA 256
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
101-274 |
1.36e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 66.25 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDD------PPEwQEIIKY-FrgselQNYftkmleddikAIikpq 171
Cdd:COG3839 27 EDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEilIGGrdvtdlPPK-DRNIAMvF-----QSY----------AL---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 172 Y----V-DNI--PraikgpvqkvgellkLRMEKSPED-----VKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQE 239
Cdd:COG3839 87 YphmtVyENIafP---------------LKLRKVPKAeidrrVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 398365537 240 ADVYMFDEPSSYLDVKQRLNA----AQIIRSLLAPTKYV 274
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMraeiKRLHRRLGTTTIYV 190
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
82-289 |
1.39e-11 |
|
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: 63.36 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSAN------SFKLHRlptprpGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELQ-- 153
Cdd:cd03229 5 NVSKRYGQKtvlndvSLNIEA------GEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI-----------LIDGEDLTdl 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 154 NYFTKMLEDDIKAIIKpQYVdnipraikgpvqkvgelLKLRMEKspedvkryikilqLENVlkrdIEKLSGGELQRFAIG 233
Cdd:cd03229 68 EDELPPLRRRIGMVFQ-DFA-----------------LFPHLTV-------------LENI----ALGLSGGQQQRVALA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 234 MSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKY-VICVEHDLSVLDYLSD 289
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGItVVLVTHDLDEAARLAD 169
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
365-540 |
1.46e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 66.26 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKlnVSMKPQKIapkfpGTVRQLF--FK 436
Cdd:PRK10851 20 DISLDIPSGQ-----MVALLGPSGSGKTTLLRIIAGLEHQTSGhirfhgTDVSR--LHARDRKV-----GFVFQHYalFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 437 KIRgQFLNPQFQTDVV----KPLRidDIIDQEV-----------------QHLSGGELQRVAIVLALGIPADIYLIDEPS 495
Cdd:PRK10851 88 HMT-VFDNIAFGLTVLprreRPNA--AAIKAKVtqllemvqlahladrypAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365537 496 AYLDSEQRiicsKVIRRFI--LHN--KKTAFIVEHDFIMATYLADKVIV 540
Cdd:PRK10851 165 GALDAQVR----KELRRWLrqLHEelKFTSVFVTHDQEEAMEVADRVVV 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
360-540 |
2.10e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.75 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 360 KKTQGDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ---DIPKL---NVSMKPQKIapkfpGTVrql 433
Cdd:PRK13650 20 KYTLNDVSFHVKQGEW-----LSIIGHNGSGKSTTVRLIDGLLEAESGQiiiDGDLLteeNVWDIRHKI-----GMV--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 434 fFKKIRGQFLNPQFQTDVVKPL------------RID---------DIIDQEVQHLSGGELQRVAIVLALGIPADIYLID 492
Cdd:PRK13650 87 -FQNPDNQFVGATVEDDVAFGLenkgipheemkeRVNealelvgmqDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365537 493 EPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATyLADKVIV 540
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLV 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
82-285 |
2.26e-11 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 61.70 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSAN------SFKLHrlptprPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDDPPEwqeiikyfrgselqny 155
Cdd:cd03221 5 NLSKTYGGKlllkdiSLTIN------PGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 156 ftkmleddikaiIKPQYVdnipraikgpvqkvgellklrmekspedvkryikilqlenvlkrdiEKLSGGELQRFAIGMS 235
Cdd:cd03221 63 ------------VKIGYF----------------------------------------------EQLSGGEKMRLALAKL 84
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 398365537 236 CVQEADVYMFDEPSSYLDVKQRlnaAQIIRSLLAPTKYVICVEHDLSVLD 285
Cdd:cd03221 85 LLENPNLLLLDEPTNHLDLESI---EALEEALKEYPGTVILVSHDRYFLD 131
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
368-543 |
2.69e-11 |
|
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: 64.59 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPD------EGQDIPKLN-----------VSMKPQKIApKFPG-T 429
Cdd:cd03294 45 LDVREGE-----IFVIMGLSGSGKSTLLRCINRLIEPTsgkvliDGQDIAAMSrkelrelrrkkISMVFQSFA-LLPHrT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 430 VRQ--LFFKKIRGQFLNPQFQ--TDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRII 505
Cdd:cd03294 119 VLEnvAFGLEVQGVPRAEREEraAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190
....*....|....*....|....*....|....*...
gi 398365537 506 CSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFEG 543
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKD 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
368-533 |
3.24e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 63.15 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ--------------DIPKL-------------------- 413
Cdd:COG2884 23 LEIEKGEF-----VFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngqdlsrlkrrEIPYLrrrigvvfqdfrllpdrtvy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 414 -NVSMkPQKIAPKFPGTVRqlffKKIRgqflnpqfqtDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALgI--PaDIYL 490
Cdd:COG2884 98 eNVAL-PLRVTGKSRKEIR----RRVR----------EVLDLVGLSDKAKALPHELSGGEQQRVAIARAL-VnrP-ELLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398365537 491 IDEPSAYLDSE--QRIIcsKVIRRFilHNKKTAfivehdFIMATY 533
Cdd:COG2884 161 ADEPTGNLDPEtsWEIM--ELLEEI--NRRGTT------VLIATH 195
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
360-499 |
3.27e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.98 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 360 KKTQGDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG--QDIPKLNVSMKPQKIA--PKFPGTVRqlff 435
Cdd:PRK09544 17 RRVLSDVSLELKPGK-----ILTLLGPNGAGKSTLVRVVLGLVAPDEGviKRNGKLRIGYVPQKLYldTTLPLTVN---- 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 436 kkiRGQFLNPQFQTD----VVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:PRK09544 88 ---RFLRLRPGTKKEdilpALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
360-543 |
4.08e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.62 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 360 KKTQGDFVLNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQ----DIP-KLNVSMKPQKiapkfpGTVRQLf 434
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTirvgDITiDTARSLSQQK------GLIRQL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 435 fkkirGQFLNPQFQTDVVKPLR--IDDIIDQEV-------------------------------QHLSGGELQRVAIVLA 481
Cdd:PRK11264 84 -----RQHVGFVFQNFNLFPHRtvLENIIEGPVivkgepkeeatararellakvglagketsypRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 482 LGIPADIYLIDEPSAYLDSEqriICSKVIR--RFILHNKKTAFIVEHDFIMATYLADKVIVFEG 543
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPE---LVGEVLNtiRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQ 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
102-407 |
4.87e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeIIKyfrgselQNYFTKMLEDDikaiikPqyvdniPRAIK 181
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI--------IYE-------QDLIVARLQQD------P------PRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 182 GPV--------QKVGELLK------LRMEKSPED-----VKRYIKIL------QLENVLKRDIEK-----------LSGG 225
Cdd:PRK11147 81 GTVydfvaegiEEQAEYLKryhdisHLVETDPSEknlneLAKLQEQLdhhnlwQLENRINEVLAQlgldpdaalssLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 226 ELQRFAIGMSCVQEADVYMFDEPSSYLDVkqrlNAAQIIRSLLAPTK-YVICVEHDLSVLDYLSD-FVCIIYGVpsvygV 303
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQgSIIFISHDRSFIRNMATrIVDLDRGK-----L 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 304 VTLPASVregiNIFLDGHipAENLRfrTEALQFRIAD---ATEDL-----------QNDSASRAfsypsLKK-------- 361
Cdd:PRK11147 232 VSYPGNY----DQYLLEK--EEALR--VEELQNAEFDrklAQEEVwirqgikarrtRNEGRVRA-----LKAlrrerser 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365537 362 --TQGDFVLNVEEGEFS--------------DSEILV--------------MMGENGTGKTTLIKLLAGALKPDEG 407
Cdd:PRK11147 299 reVMGTAKMQVEEASRSgkivfemenvnyqiDGKQLVkdfsaqvqrgdkiaLIGPNGCGKTTLLKLMLGQLQADSG 374
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
361-498 |
6.71e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.05 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 361 KTQGDFV------LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ--------DIP------KLNVSMKPQ 420
Cdd:COG3845 13 KRFGGVVanddvsLTVRPGE-----IHALLGENGAGKSTLMKILYGLYQPDSGEilidgkpvRIRsprdaiALGIGMVHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 421 --KIAPKFpgTVRQ---LFFKKIRGQFLNPQFQTDVVK------PLRIDdiIDQEVQHLSGGELQRVAIV--LALGipAD 487
Cdd:COG3845 88 hfMLVPNL--TVAEnivLGLEPTKGGRLDRKAARARIRelseryGLDVD--PDAKVEDLSVGEQQRVEILkaLYRG--AR 161
|
170
....*....|..
gi 398365537 488 IyLI-DEPSAYL 498
Cdd:COG3845 162 I-LIlDEPTAVL 172
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
354-543 |
6.98e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 62.10 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSlKKTQGDFVLNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMkPQKIA--PKFP---- 427
Cdd:cd03250 8 FTWDS-GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGS------VSV-PGSIAyvSQEPwiqn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 428 GTVRQ--LFfkkirGQFLNPQFQTDVVKP--LRID-DII---DQ-EVQH----LSGGELQRVAIVLALGIPADIYLIDEP 494
Cdd:cd03250 80 GTIREniLF-----GKPFDEERYEKVIKAcaLEPDlEILpdgDLtEIGEkginLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398365537 495 SAYLDSE-QRIICSKVIRRFiLHNKKTAFIVEH--DFIMAtylADKVIVFEG 543
Cdd:cd03250 155 LSAVDAHvGRHIFENCILGL-LLNNKTRILVTHqlQLLPH---ADQIVVLDN 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
99-540 |
7.13e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 99 TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqEIikyfrGSELQNYFTKMLEDDIKAIIKPQyvdnipR 178
Cdd:PRK15439 33 TLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-------EI-----GGNPCARLTPAKAHQLGIYLVPQ------E 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 179 AIKGPVQKVGELLKLRMEKSPEDVKRYIKILQLENV-LKRDIEK--LSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVK 255
Cdd:PRK15439 95 PLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCqLDLDSSAgsLEVADRQIVEILRGLMRDSRILILDEPTASLTPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 256 QRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVciiygvpSVygvvtlpasVREGInIFLDGHIPaenlRFRTEALq 335
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRI-------SV---------MRDGT-IALSGKTA----DLSTDDI- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 336 frIADATEDLQNDSASRA----FSYPSLKKTQ--GDFVLNVEE--GE-FSD-------SEILVMMGENGTGKTTLIKLLA 399
Cdd:PRK15439 233 --IQAITPAAREKSLSASqklwLELPGNRRQQaaGAPVLTVEDltGEgFRNislevraGEILGLAGVVGAGRTELAETLY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 400 GALKPD------EGQDIPKLNVSMKPQKiapkfpGTV-----RQ---LFFK------------KIRGQFLNPQFQTDVVK 453
Cdd:PRK15439 311 GLRPARggrimlNGKEINALSTAQRLAR------GLVylpedRQssgLYLDaplawnvcalthNRRGFWIKPARENAVLE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 454 PL-RIDDI----IDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIvEHDF 528
Cdd:PRK15439 385 RYrRALNIkfnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFI-SSDL 463
|
490
....*....|..
gi 398365537 529 IMATYLADKVIV 540
Cdd:PRK15439 464 EEIEQMADRVLV 475
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
101-294 |
8.38e-11 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 62.00 E-value: 8.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR-----FD---DPPEWQEIIKY-FRGSELQNYFTKMLEDDIKAIIKpq 171
Cdd:cd03265 24 RRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvagHDvvrEPREVRRRIGIvFQDLSVDDELTGWENLYIHARLY-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 172 yvdNIPRAIKGpvQKVGELLKL--RMEKSPEDVKRYikilqlenvlkrdieklSGGELQRFAIGMSCVQEADVYMFDEPS 249
Cdd:cd03265 102 ---GVPGAERR--ERIDELLDFvgLLEAADRLVKTY-----------------SGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365537 250 SYLDVKQRLNAAQIIRSLLAPTKY-VICVEHDLSVLDYLSDFVCII 294
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMtILLTTHYMEEAEQLCDRVAII 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
103-295 |
8.78e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.57 E-value: 8.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELqnyfTKMLEDDIKAIIKP-QYVDNIPRAIK 181
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGLVKATDGEV-----------AWLGKDL----LGMKDDEWRAVRSDiQMIFQDPLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 182 GPVQKVGELLK--LRM---EKSPEDVKRYIKILQ-----LENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSY 251
Cdd:PRK15079 112 NPRMTIGEIIAepLRTyhpKLSRQEVKDRVKAMMlkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365537 252 LDVKQRlnaAQIIRSLLAPTK----YVICVEHDLSVLDYLSDFVCIIY 295
Cdd:PRK15079 192 LDVSIQ---AQVVNLLQQLQRemglSLIFIAHDLAVVKHISDRVLVMY 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
101-257 |
9.18e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 62.36 E-value: 9.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDD------PPEWQEIikyfrGSELQNYftkmleddikAIIKPQY 172
Cdd:cd03296 26 PSGELVALLGPSGSGKTTLLRLIAGLERPDSGTilFGGedatdvPVQERNV-----GFVFQHY----------ALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 173 V-DNIPRAIKgpvqkvgelLKLRMEKSPED-----VKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFD 246
Cdd:cd03296 91 VfDNVAFGLR---------VKPRSERPPEAeirakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170
....*....|.
gi 398365537 247 EPSSYLDVKQR 257
Cdd:cd03296 162 EPFGALDAKVR 172
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
359-545 |
9.93e-11 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 62.00 E-value: 9.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 359 LKKTQGDFV------LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPK------LNVSMKPQ 420
Cdd:cd03265 6 LVKKYGDFEavrgvsFRVRRGE-----IFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghDVVReprevrRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 421 KIA--PKFPGTVRQLFFKKIRGqflnpqFQTDVVKPlRIDDII---------DQEVQHLSGGELQRVAIVLALGIPADIY 489
Cdd:cd03265 81 DLSvdDELTGWENLYIHARLYG------VPGAERRE-RIDELLdfvglleaaDRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365537 490 LIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKV-------IVFEGIP 545
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVaiidhgrIIAEGTP 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
91-269 |
1.04e-10 |
|
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: 61.34 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 91 SFKLHrlptprPGQVLGLVGTNGIGKSTALKILAGKQKPNLGrfddppewqEIikYFRGSELQ----NYFTKML----ED 162
Cdd:COG4133 22 SFTLA------AGEALALTGPNGSGKTTLLRILAGLLPPSAG---------EV--LWNGEPIRdareDYRRRLAylghAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 163 DIKaiikpqyvdnipraikgPVQKVGELLKL-----RMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCV 237
Cdd:COG4133 85 GLK-----------------PELTVRENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190
....*....|....*....|....*....|..
gi 398365537 238 QEADVYMFDEPSSYLDVKQRLNAAQIIRSLLA 269
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLA 179
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
379-500 |
1.06e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 379 EILVMMGENGTGKTTLIKLLAGALKPDEGqdipklNVSMKPQKI-APKFPG---------------TVRQ--LFFKKIRG 440
Cdd:PRK13539 29 EALVLTGPNGSGKTTLLRLIAGLLPPAAG------TIKLDGGDIdDPDVAEachylghrnamkpalTVAEnlEFWAAFLG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 441 QflNPQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDS 500
Cdd:PRK13539 103 G--EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
381-542 |
1.10e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.51 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 381 LVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFPGTVRQ---LFFKKIRGQFLNPQFQTDV------ 451
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGS------VLIRGEPITKENIREVRKfvgLVFQNPDDQIFSPTVEQDIafgpin 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 452 ---------------VKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILH 516
Cdd:PRK13652 107 lgldeetvahrvssaLHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPET 186
|
170 180
....*....|....*....|....*.
gi 398365537 517 NKKTAFIVEHDFIMATYLADKVIVFE 542
Cdd:PRK13652 187 YGMTVIFSTHQLDLVPEMADYIYVMD 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
82-307 |
1.11e-10 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 61.72 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSANSFKLHRLP----TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELQNyft 157
Cdd:cd03293 5 NVSKTYGGGGGAVTALEdislSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-----------LVDGEPVTG--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 158 kmLEDDIkAIIKPQYV--------DNIpraikgpvqkvgeLLKLRMEKSP-----EDVKRYIKILQLENVLKRDIEKLSG 224
Cdd:cd03293 71 --PGPDR-GYVFQQDAllpwltvlDNV-------------ALGLELQGVPkaearERAEELLELVGLSGFENAYPHQLSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 225 GELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKY-VICVEHDLSVLDYLSDFVCIIYGVPS-VYG 302
Cdd:cd03293 135 GMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKtVLLVTHDIDEAVFLADRVVVLSARPGrIVA 214
|
....*
gi 398365537 303 VVTLP 307
Cdd:cd03293 215 EVEVD 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
103-281 |
1.56e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 62.32 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLG--RFDDPPEWQEIIKYFR---GSELQN----YFTKMLEDDIKAIIKPQyv 173
Cdd:PRK13632 35 GEYVAILGHNGSGKSTISKILTGLLKPQSGeiKIDGITISKENLKEIRkkiGIIFQNpdnqFIGATVEDDIAFGLENK-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 174 dNIPRaikgpvqkvgellklrmEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLD 253
Cdd:PRK13632 113 -KVPP-----------------KKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
170 180
....*....|....*....|....*....
gi 398365537 254 VKQRLNAAQIIRSLLAP-TKYVICVEHDL 281
Cdd:PRK13632 175 PKGKREIKKIMVDLRKTrKKTLISITHDM 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
368-541 |
1.77e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.50 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ--------------DIPKLNVSMKPQKIAPkFPG-TVRQ 432
Cdd:COG1129 25 LELRPGE-----VHALLGENGAGKSTLMKILSGVYQPDSGEilldgepvrfrsprDAQAAGIAIIHQELNL-VPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 -LFF--KKIRGQFLNPQFQ----TDVVKPLRIDdiID--QEVQHLSGGELQRVAIVLALGIPADIyLI-DEPSAYLDSEQ 502
Cdd:COG1129 99 nIFLgrEPRRGGLIDWRAMrrraRELLARLGLD--IDpdTPVGDLSVAQQQLVEIARALSRDARV-LIlDEPTASLTERE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 398365537 503 RIICSKVIRRfiLHNKKTAFI-VEHDF--IMAtyLADKVIVF 541
Cdd:COG1129 176 VERLFRIIRR--LKAQGVAIIyISHRLdeVFE--IADRVTVL 213
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
9-72 |
1.77e-10 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 57.36 E-value: 1.77e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 9 AIVSADKCKpkKCRqECKRSCPVvktgklcIEVTPTSKIAFISEILCIGCGICVKKCPFDAIQI 72
Cdd:COG4231 17 YVIDEDKCT--GCG-ACVKVCPA-------DAIEEGDGKAVIDPDLCIGCGSCVQVCPVDAIKL 70
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
82-285 |
1.89e-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: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSAN--------SFKLhrlptpRPGQVLGLVGTNGIGKSTALKILAGKQKPNLG--RFDDPPewqeiIKYFRGSE 151
Cdd:COG4987 338 DVSFRYPGAgrpvldglSLTL------PPGERVAIVGPSGSGKSTLLALLLRFLDPQSGsiTLGGVD-----LRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 152 LQNYFTkMLEDDIkaiikpqYV------DNipraikgpvqkvgelLKL-RMEKSPEDVKRYIKILQLENVLKRDIE---- 220
Cdd:COG4987 407 LRRRIA-VVPQRP-------HLfdttlrEN---------------LRLaRPDATDEELWAALERVGLGDWLAALPDgldt 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 221 -------KLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDvkqRLNAAQIIRSLLAPT--KYVICVEHDLSVLD 285
Cdd:COG4987 464 wlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLD---AATEQALLADLLEALagRTVLLITHRLAGLE 534
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
364-541 |
1.93e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.04 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 364 GDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKP-----QKIApKFPG-TVR 431
Cdd:PRK09452 31 SNLDLTINNGEF-----LTLLGPSGCGKTTVLRLIAGFETPDSGrimldgQDITHVPAENRHvntvfQSYA-LFPHmTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 432 Q-----LFFKKIRGQFLNPQFqTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIIC 506
Cdd:PRK09452 105 EnvafgLRMQKTPAAEITPRV-MEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQM 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 398365537 507 SKVIRRfiLHNK-KTAFI-VEHDFIMATYLADKVIVF 541
Cdd:PRK09452 184 QNELKA--LQRKlGITFVfVTHDQEEALTMSDRIVVM 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
102-294 |
2.11e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF---DDPPEW---------QEIIKYFRGSELQNYFTKmLEDDIKAIIK 169
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqGKPLDYskrgllalrQQVATVFQDPEQQIFYTD-IDSDIAFSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 170 pqyvdNIPRAIKGPVQKVGELLKLrmekspEDVKRYikilqlenvLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPS 249
Cdd:PRK13638 105 -----NLGVPEAEITRRVDEALTL------VDAQHF---------RHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398365537 250 SYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCII 294
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVL 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
101-284 |
2.14e-10 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 61.43 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDppewQEIIKYfRGSELQNYFTK--MLEDDIkAIIKPQYV-DN 175
Cdd:cd03256 25 NPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSvlIDG----TDINKL-KGKALRQLRRQigMIFQQF-NLIERLSVlEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 176 IPRAIKGPVQKVGELLKLRmekSPEDVKRYIKILQ----LENVLKRdIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSY 251
Cdd:cd03256 99 VLSGRLGRRSTWRSLFGLF---PKEEKQRALAALErvglLDKAYQR-ADQLSGGQQQRVAIARALMQQPKLILADEPVAS 174
|
170 180 190
....*....|....*....|....*....|...
gi 398365537 252 LDVKqrlNAAQIIRSLLAptkyvICVEHDLSVL 284
Cdd:cd03256 175 LDPA---SSRQVMDLLKR-----INREEGITVI 199
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
347-564 |
2.31e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 61.80 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 347 NDSASRAFSYPSLKKTQ--GDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQDIPKLNVSMKPQkIAP 424
Cdd:cd03291 35 SDDNNLFFSNLCLVGAPvlKNINLKIEKGE-----MLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQ-FSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 425 KFPGTVRQ-LFFK------KIRGQFLNPQFQTDVVKPLRIDDIIDQEVQ-HLSGGELQRVAIVLALGIPADIYLIDEPSA 496
Cdd:cd03291 109 IMPGTIKEnIIFGvsydeyRYKSVVKACQLEEDITKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 497 YLD--SEQRIICSKVIRrfiLHNKKTAFIV----EHdfimaTYLADKVIV-------FEGIPSKNAHARaPE--SLLTGC 561
Cdd:cd03291 189 YLDvfTEKEIFESCVCK---LMANKTRILVtskmEH-----LKKADKILIlhegssyFYGTFSELQSLR-PDfsSKLMGY 259
|
...
gi 398365537 562 NRF 564
Cdd:cd03291 260 DTF 262
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
379-532 |
2.89e-10 |
|
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: 58.92 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 379 EILVMMGENGTGKTTLIKLLAGALKPDEGQDIpklnvsmkpqkiapkfpgtvrqlffkkirgqFLNPQFQTDVVKPLRID 458
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVI-------------------------------YIDGEDILEEVLDQLLL 51
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 459 DIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVehDFIMAT 532
Cdd:smart00382 52 IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNL--TVILTT 123
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
101-294 |
2.91e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.74 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF---DDP-PEWQEIIKYFRGselqnyftkmleddikaiIKPQYvDNI 176
Cdd:PRK13537 31 QRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcGEPvPSRARHARQRVG------------------VVPQF-DNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 177 -PR-AIKGPVQKVGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDV 254
Cdd:PRK13537 92 dPDfTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398365537 255 KQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCII 294
Cdd:PRK13537 172 QARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVI 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
354-554 |
3.39e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.25 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQGDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGqdipKLNVSMKPQKIAPKFPGTVRQ- 432
Cdd:PRK13639 9 YSYPDGTEALKGINFKAEKGE-----MVALLGPNGAGKSTLFLHFNGILKPTSG----EVLIKGEPIKYDKKSLLEVRKt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 --LFFKKIRGQFLNPQFQTDVV-KPLRI---DDIIDQEVQ-----------------HLSGGELQRVAIVLALGIPADIY 489
Cdd:PRK13639 80 vgIVFQNPDDQLFAPTVEEDVAfGPLNLglsKEEVEKRVKealkavgmegfenkpphHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 490 LIDEPSAYLDSeqrIICSKVIRRFILHNKK--TAFIVEHDFIMATYLADKV-------IVFEGIPS---------KNAHA 551
Cdd:PRK13639 160 VLDEPTSGLDP---MGASQIMKLLYDLNKEgiTIIISTHDVDLVPVYADKVyvmsdgkIIKEGTPKevfsdietiRKANL 236
|
...
gi 398365537 552 RAP 554
Cdd:PRK13639 237 RLP 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
82-285 |
3.48e-10 |
|
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: 59.32 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSAN--------SFKLhrlptpRPGQVLGLVGTNGIGKSTALKILAgkqkpnlgRFDDPPEwQEIikYFRGSELQ 153
Cdd:cd03228 5 NVSFSYPGRpkpvlkdvSLTI------KPGEKVAIVGPSGSGKSTLLKLLL--------RLYDPTS-GEI--LIDGVDLR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 154 NYftkmleddikaiikpqyvdnipraikgpvqkvgellklrmekSPEDVKRYIKILQLENVL-KRDIEK--LSGGELQRF 230
Cdd:cd03228 68 DL------------------------------------------DLESLRKNIAYVPQDPFLfSGTIREniLSGGQRQRI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 231 AIGMSCVQEADVYMFDEPSSYLDVKqrlNAAQIIRSL--LAPTKYVICVEHDLSVLD 285
Cdd:cd03228 106 AIARALLRDPPILILDEATSALDPE---TEALILEALraLAKGKTVIVIAHRLSTIR 159
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
357-540 |
3.61e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.22 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 357 PSLKKTQGDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPKLNVSMKP--QKIAPKFPG 428
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEF-----VGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgvDITDKKVKLSDirKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 429 TVRQLF----FKKIRGQFLN-----PQFQTDVVKPLRI-----DDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEP 494
Cdd:PRK13637 92 PEYQLFeetiEKDIAFGPINlglseEEIENRVKRAMNIvgldyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365537 495 SAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIV 540
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIV 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
383-545 |
4.84e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.54 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 383 MMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFPGTVRQ---LFFKKIRGQFLNPQFQTDV-------- 451
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIEKVKSGE------IFYNNQAITDDNFEKLRKhigIVFQNPDNQFVGSIVKYDVafglenha 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 452 -------------VKPLRIDDIIDQEVQHLSGGELQRVAI--VLALGipADIYLIDEPSAYLDSEQRIICSKVIRRFILH 516
Cdd:PRK13648 114 vpydemhrrvseaLKQVDMLERADYEPNALSGGQKQRVAIagVLALN--PSVIILDEATSMLDPDARQNLLDLVRKVKSE 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 398365537 517 NKKTAFIVEHDFIMATYlADKVIVF-------EGIP 545
Cdd:PRK13648 192 HNITIISITHDLSEAME-ADHVIVMnkgtvykEGTP 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
103-257 |
5.01e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.50 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLGRF--------DDPPEWQEIIKYFrgselQNY--FTKMleddikaiikpQY 172
Cdd:PRK09452 40 GEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqditHVPAENRHVNTVF-----QSYalFPHM-----------TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 173 VDNIPRAikgpvqkvgellkLRMEKSPED-----VKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDE 247
Cdd:PRK09452 104 FENVAFG-------------LRMQKTPAAeitprVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170
....*....|
gi 398365537 248 PSSYLDVKQR 257
Cdd:PRK09452 171 SLSALDYKLR 180
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
368-543 |
5.42e-10 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 60.59 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNvsmkpQKIAPKFPGTVrQLFFKKIRGQ 441
Cdd:TIGR02769 32 LSIEEGE-----TVGLLGRSGCGKSTLARLLLGLEKPAQGtvsfrgQDLYQLD-----RKQRRAFRRDV-QLVFQDSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 442 FlNPQFQTD--VVKPLR-----------------------IDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSA 496
Cdd:TIGR02769 101 V-NPRMTVRqiIGEPLRhltsldeseqkariaelldmvglRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 398365537 497 YLDseqRIICSKVIR--RFILHNKKTAFI-VEHDFIMATYLADKVIVFEG 543
Cdd:TIGR02769 180 NLD---MVLQAVILEllRKLQQAFGTAYLfITHDLRLVQSFCQRVAVMDK 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
66-281 |
5.42e-10 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 61.99 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 66 PFDAIQIINLPTNLEAHVTHRYSANSFKLHRL-PTPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF--DDPPEWQe 142
Cdd:TIGR02868 323 PAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVsLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtlDGVPVSS- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 143 iikyFRGSELQnyftkmleddikaiikpqyvdnipRAIKGPVQK-------VGELLKL-RMEKSPEDVKRYIKILQLENV 214
Cdd:TIGR02868 402 ----LDQDEVR------------------------RRVSVCAQDahlfdttVRENLRLaRPDATDEELWAALERVGLADW 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 215 LKRDIE-----------KLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKqrlNAAQIIRSLLAPT--KYVICVEHDL 281
Cdd:TIGR02868 454 LRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAE---TADELLEDLLAALsgRTVVLITHHL 530
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
365-527 |
6.23e-10 |
|
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: 59.57 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ--------------DIPKLNvsmkpQKIapkfpGTV 430
Cdd:TIGR02673 20 DVSLHIRKGEF-----LFLTGPSGAGKTTLLKLLYGALTPSRGQvriagedvnrlrgrQLPLLR-----RRI-----GVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 431 RQLFfkKI---RGQFLNpqfqtdVVKPLRID----DIIDQEVQH-----------------LSGGELQRVAIVLALGIPA 486
Cdd:TIGR02673 85 FQDF--RLlpdRTVYEN------VALPLEVRgkkeREIQRRVGAalrqvglehkadafpeqLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 398365537 487 DIYLIDEPSAYLDSE--QRIIcsKVIRRFILHNkKTAFIVEHD 527
Cdd:TIGR02673 157 PLLLADEPTGNLDPDlsERIL--DLLKRLNKRG-TTVIVATHD 196
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
91-296 |
7.06e-10 |
|
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: 60.84 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 91 SFKLHRlptprpGQVLGLVGTNGIGKSTALKILAGKQKPNLG-----RFD-------DPPEWQEIikyfRGSELQnyftk 158
Cdd:COG0444 25 SFDVRR------GETLGLVGESGSGKSTLARAILGLLPPPGItsgeiLFDgedllklSEKELRKI----RGREIQ----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 159 mleddikaIIkPQyvD-----NipraikgPVQKVG----ELLKLRMEKSPEDVK-RYIKILQL------ENVLKRDIEKL 222
Cdd:COG0444 90 --------MI-FQ--DpmtslN-------PVMTVGdqiaEPLRIHGGLSKAEAReRAIELLERvglpdpERRLDRYPHEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 223 SGGELQRFAIGMSCVQEADVYMFDEPSSYLDVkqrLNAAQIIRSL--------LAptkyVICVEHDLSVLDYLSDFVCII 294
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDV---TIQAQILNLLkdlqrelgLA----ILFITHDLGVVAEIADRVAVM 224
|
..
gi 398365537 295 YG 296
Cdd:COG0444 225 YA 226
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
10-73 |
7.66e-10 |
|
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: 55.83 E-value: 7.66e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 10 IVSADKCKpkKCRQeCKRSCPVvktgkLCIEVTPTSKIAFISEiLCIGCGICVKKCPFDAIQII 73
Cdd:COG1144 26 VVDEDKCI--GCGL-CWIVCPD-----GAIRVDDGKYYGIDYD-YCKGCGICAEVCPVKAIEMV 80
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
353-501 |
8.02e-10 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 61.61 E-value: 8.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 353 AFSYPSLKKTQGDFVLNVEEGEfsdsEILVMmGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFPGTVRQ 432
Cdd:TIGR02868 341 SAGYPGAPPVLDGVSLDLPPGE----RVAIL-GPSGSGKSTLLATLAGLLDPLQGE------VTLDGVPVSSLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 lffkkiRGQFLNPQ---FQTDVVKPLRI--DDIIDQEV----------------------------QHLSGGELQRVAIV 479
Cdd:TIGR02868 410 ------RVSVCAQDahlFDTTVRENLRLarPDATDEELwaalervgladwlralpdgldtvlgeggARLSGGERQRLALA 483
|
170 180
....*....|....*....|..
gi 398365537 480 LALGIPADIYLIDEPSAYLDSE 501
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAE 505
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
103-280 |
1.03e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.43 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLG-------RFDD-PPEWQEIIKYFRGSELQNYFTkmLEDDIKAIIKpqyvd 174
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGdlfigekRMNDvPPAERGVGMVFQSYALYPHLS--VAENMSFGLK----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 175 nIPRAIKGPVQKvgellklRMEKSPEdvkryikILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLD- 253
Cdd:PRK11000 102 -LAGAKKEEINQ-------RVNQVAE-------VLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDa 166
|
170 180 190
....*....|....*....|....*....|
gi 398365537 254 ---VKQRLNAAQIIRSLlapTKYVICVEHD 280
Cdd:PRK11000 167 alrVQMRIEISRLHKRL---GRTMIYVTHD 193
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
353-571 |
1.08e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.62 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 353 AFSYPSLKKTQGDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQDIPKLNVSMKPQKIapkfPGtVRQ 432
Cdd:PRK13644 8 SYSYPDGTPALENINLVIKKGEY-----IGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKL----QG-IRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 L---FFKKIRGQFLNPQFQTDV--------VKPLRIDDIIDQEV-------------QHLSGGELQRVAIVLALGIPADI 488
Cdd:PRK13644 78 LvgiVFQNPETQFVGRTVEEDLafgpenlcLPPIEIRKRVDRALaeiglekyrhrspKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 489 YLIDEPSAYLDSEQRIICSKVIRRfiLHNK-KTAFIVEHDfIMATYLADKVIVFEgiPSKNAHARAPESLLTGCNrfLKN 567
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKK--LHEKgKTIVYITHN-LEELHDADRIIVMD--RGKIVLEGEPENVLSDVS--LQT 230
|
....
gi 398365537 568 LNVT 571
Cdd:PRK13644 231 LGLT 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
102-267 |
1.11e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLG-------RFD--DPPEWQEIIKYFR--GSELQNY-----FTKMleddik 165
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGqlniaghQFDfsQKPSEKAIRLLRQkvGMVFQQYnlwphLTVM------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 166 aiikpqyvDNIpraIKGPVQkvgeLLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMF 245
Cdd:COG4161 101 --------ENL---IEAPCK----VLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180
....*....|....*....|..
gi 398365537 246 DEPSSYLDVKQRLNAAQIIRSL 267
Cdd:COG4161 166 DEPTAALDPEITAQVVEIIREL 187
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
101-284 |
1.15e-09 |
|
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: 61.15 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFD---------DPPEWQEIIKYFRgselQNYFtkMLEDDIKAIIKPQ 171
Cdd:TIGR02857 346 PPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladaDADSWRDQIAWVP----QHPF--LFAGTIAENIRLA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 172 YVDNIPRAIKGPVQKVG--ELLKLRmeksPEDvkryikilqLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPS 249
Cdd:TIGR02857 420 RPDASDAEIREALERAGldEFVAAL----PQG---------LDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190
....*....|....*....|....*....|....*..
gi 398365537 250 SYLDvkqRLNAAQIIRSL--LAPTKYVICVEHDLSVL 284
Cdd:TIGR02857 487 AHLD---AETEAEVLEALraLAQGRTVLLVTHRLALA 520
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
91-279 |
1.17e-09 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 58.66 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 91 SFKLHRLP-----TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF--------DDPPEWQEIIKYFRGSELQNYFT 157
Cdd:cd03298 7 RFSYGEQPmhfdlTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingvdvtAAPPADRPVSMLFQENNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 158 kmLEDDIKAIIKPQyvdnipraikgpvqkvgelLKLRmeksPEDVKRYIKILQ---LENVLKRDIEKLSGGELQRFAIGM 234
Cdd:cd03298 87 --VEQNVGLGLSPG-------------------LKLT----AEDRQAIEVALArvgLAGLEKRLPGELSGGERQRVALAR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365537 235 SCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKY-VICVEH 279
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMtVLMVTH 187
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
374-539 |
1.21e-09 |
|
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: 57.37 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 374 EFSDSEILVMMGENGTGKTTLIKLLAgalkpdegqdipkLNVSMKpqkiapkFPGTVRQLFFKkiRGQFlnpqfqtdvvK 453
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAIG-------------LALGGA-------QSATRRRSGVK--AGCI----------V 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 454 PLRIDDIIdQEVQHLSGGELQRVAIVLALGI----PADIYLIDEPSAYLDSEQRIICSKVIRRFILHnKKTAFIVEHDFI 529
Cdd:cd03227 65 AAVSAELI-FTRLQLSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPE 142
|
170
....*....|
gi 398365537 530 MATyLADKVI 539
Cdd:cd03227 143 LAE-LADKLI 151
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
103-282 |
1.23e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.23 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELQNYFTKMLEDDIKAIIKPQyvdNIPRAIKg 182
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-----------WLDGEHIQHYASKEVARRIGLLAQNA---TTPGDIT- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 183 pVQKV-------GELLKLRMEKSPED-VKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDV 254
Cdd:PRK10253 98 -VQELvargrypHQPLFTRWRKEDEEaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180
....*....|....*....|....*....
gi 398365537 255 KQRLNAAQIIRSLLAPTKYVI-CVEHDLS 282
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLaAVLHDLN 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
103-527 |
1.33e-09 |
|
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: 60.97 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQkpnlgrfDDPPEWQEIIkyfrgselqnYFTKMLEddikaiiKPQYVDnIPRAIKG 182
Cdd:TIGR03269 26 GEVLGILGRSGAGKSVLMHVLRGMD-------QYEPTSGRII----------YHVALCE-------KCGYVE-RPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 183 PVQKVGELLKLRM-------EKSPEDVKRYIKI-LQ-----------LENVLK--------------------------- 216
Cdd:TIGR03269 81 PCPVCGGTLEPEEvdfwnlsDKLRRRIRKRIAImLQrtfalygddtvLDNVLEaleeigyegkeavgravdliemvqlsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 217 ------RDiekLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKqrlnAAQIIRSLL--APTKY---VICVEHDLSVLD 285
Cdd:TIGR03269 161 rithiaRD---LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQ----TAKLVHNALeeAVKASgisMVLTSHWPEVIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 286 YLSDFVCIIYGvpsvyGVVTLPASVREGINIFLDGhipAENLRFRTEALQFRIADATEDLQND--SASRAfsypsLKKTQ 363
Cdd:TIGR03269 234 DLSDKAIWLEN-----GEIKEEGTPDEVVAVFMEG---VSEVEKECEVEVGEPIIKVRNVSKRyiSVDRG-----VVKAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 364 GDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ----------DIPKLNVSMKPQkiAPKFPGTVRQ- 432
Cdd:TIGR03269 301 DNVSLEVKEGE-----IFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnvrvgdewvDMTKPGPDGRGR--AKRYIGILHQe 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 --LFFKKIRGQFLNPQFQTD------------VVKPLRIDD-----IIDQEVQHLSGGELQRVAIVLALGIPADIYLIDE 493
Cdd:TIGR03269 374 ydLYPHRTVLDNLTEAIGLElpdelarmkaviTLKMVGFDEekaeeILDKYPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
490 500 510
....*....|....*....|....*....|....
gi 398365537 494 PSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHD 527
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEMEQTFIIVSHD 487
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
329-543 |
1.42e-09 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 57.61 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 329 FRTEALQFRIADATEdlqndsasrafsyPSLKktqgDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG- 407
Cdd:cd03246 1 LEVENVSFRYPGAEP-------------PVLR----NVSFSIEPGES-----LAIIGPSGSGKSTLARLILGLLRPTSGr 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 408 -----QDIPKLNVSMKPQKIapkfpGTVRQ---LFFKKIRgqflnpqfqtdvvkplridDIIdqevqhLSGGELQRVAIV 479
Cdd:cd03246 59 vrldgADISQWDPNELGDHV-----GYLPQddeLFSGSIA-------------------ENI------LSGGQRQRLGLA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 480 LAL-GIPAdIYLIDEPSAYLDSE-QRIICSKVIRRFIlhNKKTAFIVEHDfiMATY-LADKVIVFEG 543
Cdd:cd03246 109 RALyGNPR-ILVLDEPNSHLDVEgERALNQAIAALKA--AGATRIVIAHR--PETLaSADRILVLED 170
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
79-294 |
1.51e-09 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 60.13 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 79 LEAHVTHRYSANSFKLHrlpTPRPGQ-VLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELQnyft 157
Cdd:TIGR02142 1 LSARFSKRLGDFSLDAD---FTLPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI-----------VLNGRTLF---- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 158 kmleDDIKAIIKPQ------YVdnIPRAIKGPVQKVGELLKLRMEKS-PEDVK----RYIKILQLENVLKRDIEKLSGGE 226
Cdd:TIGR02142 63 ----DSRKGIFLPPekrrigYV--FQEARLFPHLSVRGNLRYGMKRArPSERRisfeRVIELLGIGHLLGRLPGRLSGGE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365537 227 LQRFAIGMSCVQEADVYMFDEPSSYLDVKQRlnaAQII---RSLLAPTKY-VICVEHDLSVLDYLSDFVCII 294
Cdd:TIGR02142 137 KQRVAIGRALLSSPRLLLMDEPLAALDDPRK---YEILpylERLHAEFGIpILYVSHSLQEVLRLADRVVVL 205
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
101-281 |
1.66e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.01 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLG--RFDDPPewqeiIKYFRGSELqnyfTKMLeddikAIIkPQYVdnipr 178
Cdd:PRK13548 26 RPGEVVAILGPNGAGKSTLLRALSGELSPDSGevRLNGRP-----LADWSPAEL----ARRR-----AVL-PQHS----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 179 AIKGP--VQKVGEL----LKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRfaigmscVQEADV---------- 242
Cdd:PRK13548 86 SLSFPftVEEVVAMgrapHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQR-------VQLARVlaqlwepdgp 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 398365537 243 --YMF-DEPSSYLDVKQRLNAAQIIRSLLAPTKY-VICVEHDL 281
Cdd:PRK13548 159 prWLLlDEPTSALDLAHQHHVLRLARQLAHERGLaVIVVLHDL 201
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
79-494 |
1.67e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.42 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 79 LEA-HVTHRYSAN------SFKLhrlptpRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGrfddppewqEIikYFRGSE 151
Cdd:COG1129 5 LEMrGISKSFGGVkaldgvSLEL------RPGEVHALLGENGAGKSTLMKILSGVYQPDSG---------EI--LLDGEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 152 LQNyftkmleDDIK-------AIIkPQ--------------YVDNIPRaiKGPVqkvgellkLRMEKSPEDVKRYIKILQ 210
Cdd:COG1129 68 VRF-------RSPRdaqaagiAII-HQelnlvpnlsvaeniFLGREPR--RGGL--------IDWRAMRRRARELLARLG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 211 LENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVK--QRLNAaqIIRSLLAPTKYVICVEHDLS-VLDyL 287
Cdd:COG1129 130 LDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTERevERLFR--IIRRLKAQGVAIIYISHRLDeVFE-I 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 288 SDFVCIIygvpsvygvvtlpasvReginiflDGHIpaenlrfrteALQFRIADATED-LQNDSASRAFS--YPSLKKTQG 364
Cdd:COG1129 207 ADRVTVL----------------R-------DGRL----------VGTGPVAELTEDeLVRLMVGRELEdlFPKRAAAPG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVE----EGEFSD-S------EILVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFPG----- 428
Cdd:COG1129 254 EVVLEVEglsvGGVVRDvSfsvragEILGIAGLVGAGRTELARALFGADPADSGE------IRLDGKPVRIRSPRdaira 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 429 ------------------TVRQ-----LFFKKIRGQFLNPQFQTDVVKPLRID-DI----IDQEVQHLSGGELQRVaiVL 480
Cdd:COG1129 328 giayvpedrkgeglvldlSIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRlRIktpsPEQPVGNLSGGNQQKV--VL 405
|
490
....*....|....*.
gi 398365537 481 A--LGIPADIYLIDEP 494
Cdd:COG1129 406 AkwLATDPKVLILDEP 421
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
378-543 |
1.97e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.93 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 378 SEILVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPKLNvsmKPQKIApkFPGTVrQLFFKKIRGQFlNPQFQTD- 450
Cdd:PRK10419 38 GETVALLGRSGCGKSTLARLLVGLESPSQGNvswrgePLAKLN---RAQRKA--FRRDI-QMVFQDSISAV-NPRKTVRe 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 451 -VVKPLR-----------------------IDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDseqRIIC 506
Cdd:PRK10419 111 iIREPLRhllsldkaerlarasemlravdlDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD---LVLQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398365537 507 SKVIRRF--ILHNKKTAFI-VEHDFIMATYLADKVIVFEG 543
Cdd:PRK10419 188 AGVIRLLkkLQQQFGTACLfITHDLRLVERFCQRVMVMDN 227
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
9-72 |
2.35e-09 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 53.97 E-value: 2.35e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 9 AIVSADKCKpkKCRQeCKRSCPVvktgkLCIEVTptSKIAFISEILCIGCGICVKKCPFDAIQI 72
Cdd:COG2768 6 PYVDEEKCI--GCGA-CVKVCPV-----GAISIE--DGKAVIDPEKCIGCGACIEVCPVGAIKI 59
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
359-565 |
2.64e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 59.00 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 359 LKKTQGDFV------LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ------DipkLNVSMKPQ--KIap 424
Cdd:COG1118 8 ISKRFGSFTllddvsLEIASGE-----LVALLGPSGSGKTTLLRIIAGLETPDSGRivlngrD---LFTNLPPRerRV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 425 kfpG------------TVRQ--LFFKKIRGQFlNPQFQTDVVKPLR---IDDIIDQEVQHLSGGELQRVAIVLALGIPAD 487
Cdd:COG1118 78 ---GfvfqhyalfphmTVAEniAFGLRVRPPS-KAEIRARVEELLElvqLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 488 IYLIDEP-SAyLDSEQRiicsKVIRRFI--LHNK--KTAFIVEHDFIMATYLADKVIVFEG-----IPSKNAHARAPESL 557
Cdd:COG1118 154 VLLLDEPfGA-LDAKVR----KELRRWLrrLHDElgGTTVFVTHDQEEALELADRVVVMNQgrieqVGTPDEVYDRPATP 228
|
250
....*....|..
gi 398365537 558 ----LTGCNRFL 565
Cdd:COG1118 229 fvarFLGCVNVL 240
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
368-526 |
2.67e-09 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 58.17 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQDI-----PKLNVSM---KPQ------KIAPKFPG--TVR 431
Cdd:COG1119 24 WTVKPGEH-----WAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgeRRGGEDVwelRKRiglvspALQLRFPRdeTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 432 QL----FFKKIrGQFLNP---QFQT--DVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQ 502
Cdd:COG1119 99 DVvlsgFFDSI-GLYREPtdeQRERarELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGA 177
|
170 180
....*....|....*....|....
gi 398365537 503 RIICSKVIRRFILHNKKTAFIVEH 526
Cdd:COG1119 178 RELLLALLDKLAAEGAPTLVLVTH 201
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
379-501 |
2.90e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.98 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 379 EILVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFPGTVRQLFF----KKIRG--------QFLNPQ 446
Cdd:TIGR01189 27 EALQVTGPNGIGKTTLLRILAGLLRPDSGE------VRWNGTPLAEQRDEPHENILYlghlPGLKPelsalenlHFWAAI 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 447 FQT------DVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSE 501
Cdd:TIGR01189 101 HGGaqrtieDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
82-281 |
3.00e-09 |
|
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: 56.28 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSAN------SFKLhrlptpRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGrfddppewqEIikyfrgselqny 155
Cdd:cd03216 5 GITKRFGGVkaldgvSLSV------RRGEVHALLGENGAGKSTLMKILSGLYKPDSG---------EI------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 156 ftkmleddikaiikpqYVDNIPRAIKGPVQkvGELLKLRMekspedvkryikILQlenvlkrdiekLSGGELQRFAIGMS 235
Cdd:cd03216 58 ----------------LVDGKEVSFASPRD--ARRAGIAM------------VYQ-----------LSVGERQMVEIARA 96
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365537 236 CVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDL 281
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRL 142
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
103-257 |
3.43e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.08 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLGRF--------DDPPEWQEIIKYFRGSELQNYFTkmLEDDIKAIIKPqyvD 174
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlsHVPPYQRPINMMFQSYALFPHMT--VEQNIAFGLKQ---D 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 175 NIPRA-IKgpvQKVGELLKLrmekspedvkryikiLQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLD 253
Cdd:PRK11607 120 KLPKAeIA---SRVNEMLGL---------------VHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
....
gi 398365537 254 VKQR 257
Cdd:PRK11607 182 KKLR 185
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
356-501 |
3.72e-09 |
|
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: 57.03 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 356 YPSLKKTQGDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ-DIPKLNVSMKPQKIAPKFP---GTVR 431
Cdd:cd03292 10 YPNGTAALDGINISISAGEF-----VFLVGPSGAGKSTLLKLIYKEELPTSGTiRVNGQDVSDLRGRAIPYLRrkiGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 432 QLF-FKKIRGQFLNPQFQTDVVK------PLRIDDIIDQ-EVQH--------LSGGELQRVAIVLALGIPADIYLIDEPS 495
Cdd:cd03292 85 QDFrLLPDRNVYENVAFALEVTGvppreiRKRVPAALELvGLSHkhralpaeLSGGEQQRVAIARAIVNSPTILIADEPT 164
|
....*.
gi 398365537 496 AYLDSE 501
Cdd:cd03292 165 GNLDPD 170
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
383-543 |
4.00e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 58.28 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 383 MMGENGTGKTTLIKLLAGALKPDEG------QDIP------KLNVSMKPQ--KIAPKFpgTVRQ--LFFKKIRGqfLNPQ 446
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGsislcgEPVPsrarhaRQRVGVVPQfdNLDPDF--TVREnlLVFGRYFG--LSAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 447 FQTDVVKPL----RIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRfILHNKKTAF 522
Cdd:PRK13537 114 AARALVPPLlefaKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRS-LLARGKTIL 192
|
170 180
....*....|....*....|.
gi 398365537 523 IVEHDFIMATYLADKVIVFEG 543
Cdd:PRK13537 193 LTTHFMEEAERLCDRLCVIEE 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
82-282 |
5.44e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 57.11 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSANS-FKLHRLPTP-RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF----DD----PPEWqeiikyfrgse 151
Cdd:cd03252 5 HVRFRYKPDGpVILDNISLRiKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdgHDlalaDPAW----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 152 LQNYFTKMLEDDIkaIIKPQYVDNIPRAIKG-PVQKVGELLKLrmekspEDVKRYIKILQL--ENVLKRDIEKLSGGELQ 228
Cdd:cd03252 74 LRRQVGVVLQENV--LFNRSIRDNIALADPGmSMERVIEAAKL------AGAHDFISELPEgyDTIVGEQGAGLSGGQRQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398365537 229 RFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLApTKYVICVEHDLS 282
Cdd:cd03252 146 RIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLS 198
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
365-547 |
6.88e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 57.30 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFSdseilVMMGENGTGKTTLIKLLAGALKPDEG---------QDIPKLNVSMKPQKIAPK--FPG--TVR 431
Cdd:PRK10253 25 NLTVEIPDGHFT-----AIIGPNGCGKSTLLRTLSRLMTPAHGhvwldgehiQHYASKEVARRIGLLAQNatTPGdiTVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 432 QLFfkkIRGQFLN-PQF-------QTDVVKPLR---IDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDS 500
Cdd:PRK10253 100 ELV---ARGRYPHqPLFtrwrkedEEAVTKAMQatgITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398365537 501 EQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLA-------DKVIVFEGIPSK 547
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYAshlialrEGKIVAQGAPKE 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
461-541 |
7.04e-09 |
|
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: 55.41 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 461 IDQEVQHLSGGELQRVAIV--LALGIPADIYLIDEPSAYLDSEQRIICSKVIRRfILHNKKTAFIVEHDFIMATYlADKV 538
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKG-LIDLGNTVILIEHNLDVLSS-ADWI 158
|
...
gi 398365537 539 IVF 541
Cdd:cd03238 159 IDF 161
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
354-540 |
7.21e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.05 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQGDFVLNVEEGefsdSEIlVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFPGTVRQ- 432
Cdd:PRK13647 12 FRYKDGTKALKGLSLSIPEG----SKT-ALLGPNGAGKSTLLLHLNGIYLPQRGR------VKVMGREVNAENEKWVRSk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 --LFFKKIRGQFLNPQFQTDV---------------------VKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIY 489
Cdd:PRK13647 81 vgLVFQDPDDQVFSSTVWDDVafgpvnmgldkdeverrveeaLKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365537 490 LIDEPSAYLD-SEQRIICSKVIRrfiLHNK-KTAFIVEHDFIMATYLADKVIV 540
Cdd:PRK13647 161 VLDEPMAYLDpRGQETLMEILDR---LHNQgKTVIVATHDVDLAAEWADQVIV 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
368-505 |
7.52e-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: 56.40 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMK--------PQKiAPKFPG-TVRQ 432
Cdd:cd03218 21 LSVKQGE-----IVGLLGPNGAGKTTTFYMIVGLVKPDSGkilldgQDITKLPMHKRarlgigylPQE-ASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 LFFKKIRGQFLNPQFQTDVVKPL----RIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD----SE-QR 503
Cdd:cd03218 95 NILAVLEIRGLSKKEREEKLEELleefHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiavQDiQK 174
|
..
gi 398365537 504 II 505
Cdd:cd03218 175 II 176
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
101-295 |
7.77e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 56.00 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPnlgrfddppewqEIIK---YFRGSELqnyfTKMLEDDikaiikpqyvdnip 177
Cdd:cd03217 24 KKGEVHALMGPNGSGKSTLAKTIMGHPKY------------EVTEgeiLFKGEDI----TDLPPEE-------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 178 RAIKGpvqkvgelLKLRMEKSPEdvkryIKILQLENVLkRDI-EKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQ 256
Cdd:cd03217 74 RARLG--------IFLAFQYPPE-----IPGVKNADFL-RYVnEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398365537 257 RLNAAQIIRSLLAPTKYVICVEHDLSVLDYL-SDFVCIIY 295
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLY 179
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
353-547 |
8.11e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.97 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 353 AFSYPSLKKTQGDFVlnveegEFSDSEILVMMGENGTGKTTLIKLL------AGALKPDE-----GQDIPKLNVSMKPQK 421
Cdd:PRK14258 14 SFYYDTQKILEGVSM------EIYQSKVTAIIGPSGCGKSTFLKCLnrmnelESEVRVEGrveffNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 422 -----IAPK---FPGTVRQLFFKKIRGQFLNPQFQTD--VVKPLRIDDIIDqEVQH--------LSGGELQRVAIVLALG 483
Cdd:PRK14258 88 rqvsmVHPKpnlFPMSVYDNVAYGVKIVGWRPKLEIDdiVESALKDADLWD-EIKHkihksaldLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 484 IPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFEGIPSK 547
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
379-501 |
9.07e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 9.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 379 EILVMMGENGTGKTTLIKLLAGALKPDEGQdipkLNVSMKPQKIAPK---------FPGTVRQL-------FFKKIRGQF 442
Cdd:PRK13543 38 EALLVQGDNGAGKTTLLRVLAGLLHVESGQ----IQIDGKTATRGDRsrfmaylghLPGLKADLstlenlhFLCGLHGRR 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 443 LNpQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSE 501
Cdd:PRK13543 114 AK-QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
103-294 |
9.51e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 56.19 E-value: 9.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLGRFD----DPpeWQEIIKYFRgselqnyftkmledDIKAII--KPQYVDNI 176
Cdd:cd03267 47 GEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglVP--WKRRKKFLR--------------RIGVVFgqKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 177 PraikgpvqkVGELLKL-----RMEKS--PEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPS 249
Cdd:cd03267 111 P---------VIDSFYLlaaiyDLPPArfKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365537 250 SYLDVKQRLNAAQIIRSLLAPTKYVICV-EHDLSVLDYLSDFVCII 294
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERGTTVLLtSHYMKDIEALARRVLVI 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
101-294 |
9.76e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.54 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF---DDPPEwqeiikyfrgselqnyftkmlEDDIKAIikPQYVDNIP 177
Cdd:PRK09536 27 REGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlvaGDDVE---------------------ALSARAA--SRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 178 R----AIKGPVQKVGELLKL----RMEKSPED----VKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMF 245
Cdd:PRK09536 84 QdtslSFEFDVRQVVEMGRTphrsRFDTWTETdraaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365537 246 DEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCII 294
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLL 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
385-543 |
1.06e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 57.77 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 385 GENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQ-KIA------PKFPG-TVRQLFF------KKIRGQF--LNPQFQ 448
Cdd:COG0488 31 GRNGAGKSTLLKILAGELEPDSGE------VSIPKGlRIGylpqepPLDDDlTVLDTVLdgdaelRALEAELeeLEAKLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 449 TDVVKPLRIDDII-----------------------------DQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:COG0488 105 EPDEDLERLAELQeefealggweaearaeeilsglgfpeedlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 500 SEqriicskVIR---RFILHNKKTAFIVEHD--FI--MATYLAD----KVIVFEG 543
Cdd:COG0488 185 LE-------SIEwleEFLKNYPGTVLVVSHDryFLdrVATRILEldrgKLTLYPG 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
375-540 |
1.11e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.17 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 375 FSDSEILVMMGENGTGKTTLIKLLAGALKPDEGqdipklNVSMKPQKIAPKFPGTVRQLF--------FKKIRG------ 440
Cdd:PRK13631 49 FEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYG------TIQVGDIYIGDKKNNHELITNpyskkiknFKELRRrvsmvf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 441 QFLNPQ-FQTDVVK-----PLRI---------------------DDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDE 493
Cdd:PRK13631 123 QFPEYQlFKDTIEKdimfgPVALgvkkseakklakfylnkmgldDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 398365537 494 PSAYLDSEQRiicsKVIRRFILHNK---KTAFIVEHDFIMATYLADKVIV 540
Cdd:PRK13631 203 PTAGLDPKGE----HEMMQLILDAKannKTVFVITHTMEHVLEVADEVIV 248
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
101-295 |
1.23e-08 |
|
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: 55.97 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDppewQEIIKyFRGSELQNYFTKM--------LEDDIKAIikp 170
Cdd:cd03261 24 RRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvlIDG----EDISG-LSEAELYRLRRRMgmlfqsgaLFDSLTVF--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 171 qyvDNIPraikgpvqkvgelLKLRME-KSPEDVKRYIKILQLENV-LKRDIEK----LSGGELQRFAIGMSCVQEADVYM 244
Cdd:cd03261 96 ---ENVA-------------FPLREHtRLSEEEIREIVLEKLEAVgLRGAEDLypaeLSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398365537 245 FDEPSSYLDVKQRLNAAQIIRSL---LAPTkyVICVEHDLSVLDYLSDFVCIIY 295
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLkkeLGLT--SIMVTHDLDTAFAIADRIAVLY 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
340-540 |
1.26e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.55 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 340 DATEDLQNDSASRAFSypslKKTQGDF-VLNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQDIP---KLNV 415
Cdd:PRK13645 2 DFSKDIILDNVSYTYA----KKTPFEFkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyAIPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 416 SMKPQK----------IAPKFP--------------------GTVRQLFFKKIrgqflnPQFQTDVVKPlriDDIIDQEV 465
Cdd:PRK13645 78 NLKKIKevkrlrkeigLVFQFPeyqlfqetiekdiafgpvnlGENKQEAYKKV------PELLKLVQLP---EDYVKRSP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 466 QHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIV 540
Cdd:PRK13645 149 FELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIV 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
357-564 |
1.43e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.00 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 357 PSLKktqgDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQDIPKLNVSMKPQkIAPKFPGTVRQlffK 436
Cdd:TIGR01271 440 PVLK----NISFKLEKGQ-----LLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ-TSWIMPGTIKD---N 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 437 KIRGQFLNPQFQTDVVKPLRIDDII------DQEVQ-----HLSGGELQRVAIVLALGIPADIYLIDEPSAYLD--SEQR 503
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLEEDIalfpekDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvTEKE 586
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 504 IICSKVIRrfiLHNKKTAFIV----EHdfimaTYLADKVIV-------FEGIPSKnAHARAPE--SLLTGCNRF 564
Cdd:TIGR01271 587 IFESCLCK---LMSNKTRILVtsklEH-----LKKADKILLlhegvcyFYGTFSE-LQAKRPDfsSLLLGLEAF 651
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
348-542 |
1.50e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.97 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 348 DSASRAFSY--PSLKKTQ-----------GDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ------ 408
Cdd:PRK10070 16 EHPQRAFKYieQGLSKEQilektglslgvKDASLAIEEGE-----IFVIMGLSGSGKSTMVRLLNRLIEPTRGQvlidgv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 409 DIPKLNVS----MKPQKIA---------PKFPGTVRQLFFKKIRGQFLNPQFQT--DVVKPLRIDDIIDQEVQHLSGGEL 473
Cdd:PRK10070 91 DIAKISDAelreVRRKKIAmvfqsfalmPHMTVLDNTAFGMELAGINAEERREKalDALRQVGLENYAHSYPDELSGGMR 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 474 QRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFE 542
Cdd:PRK10070 171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
|
|
| RLI |
pfam04068 |
Possible Fer4-like domain in RNase L inhibitor, RLI; Possible metal-binding domain in ... |
7-37 |
1.61e-08 |
|
Possible Fer4-like domain in RNase L inhibitor, RLI; Possible metal-binding domain in endoribonuclease RNase L inhibitor. Found at the N-terminal end of RNase L inhibitor proteins, adjacent to the 4Fe-4S binding domain, fer4, pfam00037. Also often found adjacent to the DUF367 domain pfam04034 in uncharacterized proteins. The RNase L system plays a major role in the anti-viral and anti-proliferative activities of interferons, and could possibly play a more general role in the regulation of RNA stability in mammalian cells. Inhibitory activity requires concentration-dependent association of RLI with RNase L.
Pssm-ID: 427689 [Multi-domain] Cd Length: 35 Bit Score: 50.59 E-value: 1.61e-08
10 20 30
....*....|....*....|....*....|....
gi 398365537 7 RIAIVSADKCKPKKCRQ-ECKRSCPV--VKTGKL 37
Cdd:pfam04068 2 RLAIVDFDQCDPKKCTGrKCIRFCPVreVRTGKK 35
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
101-281 |
1.72e-08 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 55.89 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLG--RFDDPPewqeiIKYFRGSELqnyfTKMLeddikAIIkPQYVD-NIP 177
Cdd:COG4559 25 RPGELTAIIGPNGAGKSTLLKLLTGELTPSSGevRLNGRP-----LAAWSPWEL----ARRR-----AVL-PQHSSlAFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 178 RaikgPVQKVgellkLRMEKSP---------EDVKRYIKILQLENVLKRDIEKLSGGELQRfaigmscVQEADV------ 242
Cdd:COG4559 90 F----TVEEV-----VALGRAPhgssaaqdrQIVREALALVGLAHLAGRSYQTLSGGEQQR-------VQLARVlaqlwe 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 398365537 243 -------YMF-DEPSSYLDVKQRLNAAQIIRSL----LAptkyVICVEHDL 281
Cdd:COG4559 154 pvdggprWLFlDEPTSALDLAHQHAVLRLARQLarrgGG----VVAVLHDL 200
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
191-257 |
1.79e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.78 E-value: 1.79e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365537 191 LKLR-MEKspEDVKRYI----KILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQR 257
Cdd:PRK11650 101 LKIRgMPK--AEIEERVaeaaRILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
3-74 |
1.94e-08 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 56.96 E-value: 1.94e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365537 3 DKNSRIAIVSADKCKPKKCRQeCKRSCPVVKtgklcieVTPTSKIAFISEILCIGCGICVKKCPFDAIQIIN 74
Cdd:COG4624 78 IIDKRGPSIIRDKEKCKNCYP-CVRACPVKA-------IKVDDGKAEIDEEKCISCGQCVAVCPFGAITEKS 141
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
368-543 |
2.25e-08 |
|
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: 54.46 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGalKPD----------EGQDIPKLNVS--------MKPQkIAPKFPGt 429
Cdd:cd03217 21 LTIKKGE-----VHALMGPNGSGKSTLAKTIMG--HPKyevtegeilfKGEDITDLPPEerarlgifLAFQ-YPPEIPG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 430 VRQLFFkkIRgqFLNPQFqtdvvkplriddiidqevqhlSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKV 509
Cdd:cd03217 92 VKNADF--LR--YVNEGF---------------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 398365537 510 IRRfiLHNKKTAF-IVEH-----DFIMATY---LADKVIVFEG 543
Cdd:cd03217 147 INK--LREEGKSVlIITHyqrllDYIKPDRvhvLYDGRIVKSG 187
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
7-73 |
2.28e-08 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 50.88 E-value: 2.28e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 7 RIAIVSADKCKpkKCRQeCKRSCPvvkTGklCIEVTPTSKIaFISEILCIGCGICVKKCPFDAIQII 73
Cdd:COG1149 4 KIPVIDEEKCI--GCGL-CVEVCP---EG--AIKLDDGGAP-VVDPDLCTGCGACVGVCPTGAITLE 61
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
97-267 |
2.30e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 56.27 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 97 LPTPRpGQVLGLVGTNGIGKSTALKILAGKQKPNLGR-FDDPpewQEIIKyfrgSELQNyftkmleDDIkAIIKPQYV-- 173
Cdd:PRK11432 27 LTIKQ-GTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQiFIDG---EDVTH----RSIQQ-------RDI-CMVFQSYAlf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 174 ------DNIPRAIKgpvqkvgeLLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDE 247
Cdd:PRK11432 91 phmslgENVGYGLK--------MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180
....*....|....*....|
gi 398365537 248 PSSYLDVKQRLNAAQIIRSL 267
Cdd:PRK11432 163 PLSNLDANLRRSMREKIREL 182
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
357-546 |
2.30e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.90 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 357 PSLKKTQGDFVLNVEEGEFSdseilVMMGENGTGKTTLIKLLAGALKPDEGQ----DIPKLNVSmKPQKIAP-------- 424
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYT-----ALIGHTGSGKSTLLQHLNGLLQPTEGKvtvgDIVVSSTS-KQKEIKPvrkkvgvv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 425 -KFPGTvrQLFFKKI-RGQFLNPQF------QTDVVKPLRID------DIIDQEVQHLSGGELQRVAIVLALGIPADIYL 490
Cdd:PRK13643 90 fQFPES--QLFEETVlKDVAFGPQNfgipkeKAEKIAAEKLEmvgladEFWEKSPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365537 491 IDEPSAYLDSEQRIICSKVIRRfILHNKKTAFIVEH------DFIMATYLADK-VIVFEGIPS 546
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFES-IHQSGQTVVLVTHlmddvaDYADYVYLLEKgHIISCGTPS 229
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
6-82 |
2.41e-08 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 53.12 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 6 SRIAIV-SADKCKPKKCRQ----ECKRSCPVvktGKLCIEvtpTSKIAFISEiLCIGCGICVKKCPFDAIQIINLPTNLE 80
Cdd:COG1142 36 PRIRVVrKAGVSAPVQCRHcedaPCAEVCPV---GAITRD---DGAVVVDEE-KCIGCGLCVLACPFGAITMVGEKSRAV 108
|
..
gi 398365537 81 AH 82
Cdd:COG1142 109 AV 110
|
|
| HycB_like |
cd10554 |
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ... |
5-90 |
2.43e-08 |
|
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: 53.42 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 5 NSRIAIV-SADKCKPKKCRQ-E---CKRSCPVvktGklCIEVTPTSKiaFISEILCIGCGICVKKCPFDAIQII-NLPTN 78
Cdd:cd10554 39 LPRLRVVkTGEVTAPVQCRQcEdapCANVCPV---G--AISQEDGVV--QVDEERCIGCKLCVLACPFGAIEMApTTVPG 111
|
90
....*....|..
gi 398365537 79 LEAHVTHRYSAN 90
Cdd:cd10554 112 VDWERGPRAVAV 123
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
101-253 |
2.64e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.88 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRG---SELQNYFTKMLEDDIKAIIKPQYV---- 173
Cdd:PRK10908 26 RPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI-----------WFSGhdiTRLKNREVPFLRRQIGMIFQDHHLlmdr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 174 ---DN--IPRAIKGpvqkvgellklrmeKSPEDVKRYI-----KILQLENVLKRDIEkLSGGELQRFAIGMSCVQEADVY 243
Cdd:PRK10908 95 tvyDNvaIPLIIAG--------------ASGDDIRRRVsaaldKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVL 159
|
170
....*....|
gi 398365537 244 MFDEPSSYLD 253
Cdd:PRK10908 160 LADEPTGNLD 169
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
82-294 |
2.93e-08 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 54.89 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSANSFKLHRLP----TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR-----FDdppewqeiIKYFRGSEL 152
Cdd:cd03258 6 NVSKVFGDTGGKVTALKdvslSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSvlvdgTD--------LTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 153 QNYFTKMleddikAIIKPQYvdNI--PRAIKGPVQKVGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRF 230
Cdd:cd03258 78 RKARRRI------GMIFQHF--NLlsSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 231 AIGMSCVQEADVYMFDEPSSYLDVKqrlNAAQIIRSL------LAPTkyVICVEHDLSVLDYLSDFVCII 294
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPE---TTQSILALLrdinreLGLT--IVLITHEMEVVKRICDRVAVM 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
91-295 |
3.16e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.74 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 91 SFKLHRlptprpGQVLGLVGTNGIGKSTALKILAGKQKPNLG--RFDDppewQEIIKYFRGSElqnyftKMLEDDIkaii 168
Cdd:PRK11308 35 SFTLER------GKTLAVVGESGCGKSTLARLLTMIETPTGGelYYQG----QDLLKADPEAQ------KLLRQKI---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 169 kpQYVDNIPRAIKGPVQKVGELL------------KLRMEKS----------PEDVKRYIKILqlenvlkrdieklSGGE 226
Cdd:PRK11308 95 --QIVFQNPYGSLNPRKKVGQILeepllintslsaAERREKAlammakvglrPEHYDRYPHMF-------------SGGQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 227 LQRFAIGMSCVQEADVYMFDEPSSYLDVKQRlnaAQIIrSLLAP------TKYVIcVEHDLSVLDYLSDFVCIIY 295
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQ---AQVL-NLMMDlqqelgLSYVF-ISHDLSVVEHIADEVMVMY 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
379-499 |
3.56e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 54.04 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 379 EILVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFPGTVRQLFF-------KKIRGQFLNPQFQTDV 451
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGR------VLLNGGPLDFQRDSIARGLLYlghapgiKTTLSVLENLRFWHAD 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 452 VKPLRIDDIIDQ---------EVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:cd03231 101 HSDEQVEEALARvglngfedrPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
374-542 |
3.87e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 374 EFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQ-DIP----KLNVSMKPQK-------IAPKFPGTvrQLF----FKK 437
Cdd:PRK13641 29 ELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTiTIAgyhiTPETGNKNLKklrkkvsLVFQFPEA--QLFentvLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 438 IRGQFLNPQFQTDVVKPLRI---------DDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRiicSK 508
Cdd:PRK13641 107 VEFGPKNFGFSEDEAKEKALkwlkkvglsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR---KE 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 398365537 509 VIRRFILHNKK--TAFIVEHDFIMATYLADKVIVFE 542
Cdd:PRK13641 184 MMQLFKDYQKAghTVILVTHNMDDVAEYADDVLVLE 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
103-295 |
3.89e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.59 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDDPPEWQEII-------KYFRGSELQNYFTK--MLEDDIKAIIKPQYV 173
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlKVADKNQLRLLRTRltMVFQHFNLWSHMTVL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 174 DNIPRAikgPVQKVGellklrMEKSpEDVKRYIKILQLENVLKRDIEK----LSGGELQRFAIGMSCVQEADVYMFDEPS 249
Cdd:PRK10619 111 ENVMEA---PIQVLG------LSKQ-EARERAVKYLAKVGIDERAQGKypvhLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365537 250 SYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIY 295
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLH 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
101-499 |
3.91e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.99 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQkPNlGRFDDppewqEIikYFRGSELQNYFTKMLEDDIKAIIKPQY-------- 172
Cdd:TIGR02633 25 RPGECVGLCGENGAGKSTLMKILSGVY-PH-GTWDG-----EI--YWSGSPLKASNIRDTERAGIVIIHQELtlvpelsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 173 VDNI----PRAIKGPVQKVGELLkLRMEKSPEDVKryikiLQLENVlKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEP 248
Cdd:TIGR02633 96 AENIflgnEITLPGGRMAYNAMY-LRAKNLLRELQ-----LDADNV-TRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 249 SSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIygvpsvygvvtlpasvREGINIfldGHIPAENLr 328
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVI----------------RDGQHV---ATKDMSTM- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 329 frtealqfriadATEDLQNDSASRAFS--YPSLKKTQGDFVLNVE----------------EGEFS--DSEILVMMGENG 388
Cdd:TIGR02633 229 ------------SEDDIITMMVGREITslYPHEPHEIGDVILEARnltcwdvinphrkrvdDVSFSlrRGEILGVAGLVG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 389 TGKTTLIKLLAGALkpdEGQDIPKLNVSMKP-----------QKIA--P---KFPGTVRQLFF-KKIRGQFLNPQFQTDV 451
Cdd:TIGR02633 297 AGRTELVQALFGAY---PGKFEGNVFINGKPvdirnpaqairAGIAmvPedrKRHGIVPILGVgKNITLSVLKSFCFKMR 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365537 452 VKPLRIDDIIDQEVQH--------------LSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:TIGR02633 374 IDAAAELQIIGSAIQRlkvktaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
365-545 |
4.11e-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: 54.59 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLN--------VSMKPQKiAPKFPG-T 429
Cdd:TIGR04406 19 DVSLSVKSGE-----IVGLLGPNGAGKTTSFYMIVGLVRPDAGkilidgQDITHLPmherarlgIGYLPQE-ASIFRKlT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 430 VRQLFF----------KKIRGQFLNpqfqtDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:TIGR04406 93 VEENIMavleirkdldRAEREERLE-----ALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 500 -----SEQRIIcsKVIRRF---IL---HN-KKTAFIVEHDFIMatylADKVIVFEGIP 545
Cdd:TIGR04406 168 piavgDIKKII--KHLKERgigVLitdHNvRETLDICDRAYII----SDGKVLAEGTP 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
101-494 |
4.54e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELQnyFTKM---LEDDIkAII--KPQYVdn 175
Cdd:PRK11288 28 RAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI-----------LIDGQEMR--FASTtaaLAAGV-AIIyqELHLV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 176 ipraikgPVQKVGELLKL-----RMEKSPEDVKRYIKILQLENvLKRDIE------KLSGGELQRFAIGMSCVQEADVYM 244
Cdd:PRK11288 92 -------PEMTVAENLYLgqlphKGGIVNRRLLNYEAREQLEH-LGVDIDpdtplkYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 245 FDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDfvciiygvpsvygvvtlpasvreGINIFLDGhipa 324
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCD-----------------------AITVFKDG---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 325 enlRFrtealqFRIADATEDLQNDSASRA---------FSYPSlkKTQGDFVLNVEEGE---------FS--DSEILVMM 384
Cdd:PRK11288 217 ---RY------VATFDDMAQVDRDQLVQAmvgreigdiYGYRP--RPLGEVRLRLDGLKgpglrepisFSvrAGEIVGLF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 385 GENGTGKTTLIKLLAGALKPDEGQ---DIPKLNVSMKPQKIA------P---KFPGTV-------------RQLFFKKir 439
Cdd:PRK11288 286 GLVGAGRSELMKLLYGATRRTAGQvylDGKPIDIRSPRDAIRagimlcPedrKAEGIIpvhsvadninisaRRHHLRA-- 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 440 GQFLNPQFQTDV----VKPLRIDDI-IDQEVQHLSGGELQRVAIVLALGIPADIYLIDEP 494
Cdd:PRK11288 364 GCLINNRWEAENadrfIRSLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
327-501 |
6.21e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 327 LRFRTEALQFRIADATEDLqndsaSRAFSYPSLKKtqgDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDE 406
Cdd:PRK15064 307 IRFEQDKKLHRNALEVENL-----TKGFDNGPLFK---NLNLLLEAGE-----RLAIIGENGVGKTTLLRTLVGELEPDS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 407 GQdIP---KLNVSMKPQKIAPKFPGTVrQLFfkKIRGQFLNPQFQTDVVKP-----LRIDDIIDQEVQHLSGGELQRVAI 478
Cdd:PRK15064 374 GT-VKwseNANIGYYAQDHAYDFENDL-TLF--DWMSQWRQEGDDEQAVRGtlgrlLFSQDDIKKSVKVLSGGEKGRMLF 449
|
170 180
....*....|....*....|....
gi 398365537 479 -VLALGIPaDIYLIDEPSAYLDSE 501
Cdd:PRK15064 450 gKLMMQKP-NVLVMDEPTNHMDME 472
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
83-289 |
6.24e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 83 VTHRYSAN------SFKLHrlptprPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRfddppewqeiIKY-FRGSELQNY 155
Cdd:PRK11701 12 LTKLYGPRkgcrdvSFDLY------PGEVLGIVGESGSGKTTLLNALSARLAPDAGE----------VHYrMRDGQLRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 156 FTkMLEDDIKAIIKPQ--YVDNIPR-AIKGPVQ---KVGELLklrMEKSpedVKRYIKILQ-----LENV---LKRdIEK 221
Cdd:PRK11701 76 YA-LSEAERRRLLRTEwgFVHQHPRdGLRMQVSaggNIGERL---MAVG---ARHYGDIRAtagdwLERVeidAAR-IDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 222 L----SGGELQRFAIGMSCVQEAD-VYMfDEPSSYLD--VKQRLnaAQIIRSL-----LAptkyVICVEHDLSVLDYLSD 289
Cdd:PRK11701 148 LpttfSGGMQQRLQIARNLVTHPRlVFM-DEPTGGLDvsVQARL--LDLLRGLvrelgLA----VVIVTHDLAVARLLAH 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
368-542 |
6.45e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.91 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQdipklnvsmkpqKIAPKFP-GTVRQ---LFFKKIR---- 439
Cdd:PRK11247 33 LHIPAGQF-----VAVVGRSGCGKSTLLRLLAGLETPSAGE------------LLAGTAPlAEAREdtrLMFQDARllpw 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 440 -------GQFLNPQFQTDVVKPLRIDDIIDQEVQ---HLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKV 509
Cdd:PRK11247 96 kkvidnvGLGLKGQWRDAALQALAAVGLADRANEwpaALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDL 175
|
170 180 190
....*....|....*....|....*....|...
gi 398365537 510 IRRFILHNKKTAFIVEHDFIMATYLADKVIVFE 542
Cdd:PRK11247 176 IESLWQQHGFTVLLVTHDVSEAVAMADRVLLIE 208
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
17-72 |
6.48e-08 |
|
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 51.62 E-value: 6.48e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 17 KPKKCRQ----ECKRSCPvvkTGklCIEVTPTSkIAFISEILCIGCGICVKKCPFDAIQI 72
Cdd:cd04410 46 LPVSCMHcedpPCVKACP---TG--AIYKDEDG-IVLIDEDKCIGCGSCVEACPYGAIVF 99
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
375-501 |
7.37e-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: 55.33 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 375 FSDSEILVMmGENGTGKTTLIKLLAGALKPDEGQDIPK--LNVSMKPQ--KIAPKFpgTVRQLF-------------FKK 437
Cdd:TIGR03719 29 FPGAKIGVL-GLNGAGKSTLLRIMAGVDKDFNGEARPQpgIKVGYLPQepQLDPTK--TVRENVeegvaeikdaldrFNE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 438 IRGQFLNPQFQTDVV--KPLRIDDII------------------------DQEVQHLSGGELQRVAIV-LALGIPaDIYL 490
Cdd:TIGR03719 106 ISAKYAEPDADFDKLaaEQAELQEIIdaadawdldsqleiamdalrcppwDADVTKLSGGERRRVALCrLLLSKP-DMLL 184
|
170
....*....|.
gi 398365537 491 IDEPSAYLDSE 501
Cdd:TIGR03719 185 LDEPTNHLDAE 195
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
14-72 |
7.40e-08 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 49.36 E-value: 7.40e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 14 DKCKpkKCRQeCKRSCPVvktgkLCIEVTPT--SKIAFISEILCIGCGICVKKCPFDAIQI 72
Cdd:COG1143 2 DKCI--GCGL-CVRVCPV-----DAITIEDGepGKVYVIDPDKCIGCGLCVEVCPTGAISM 54
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
8-72 |
8.26e-08 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 53.57 E-value: 8.26e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 8 IAIVSADKCKpkKCRQeCKRSCPVvktgkLCIEVTPTSKIAFISEILCIGCGICVKKCPFDAIQI 72
Cdd:COG1145 176 KAVIDAEKCI--GCGL-CVKVCPT-----GAIRLKDGKPQIVVDPDKCIGCGACVKVCPVGAISL 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
354-543 |
8.29e-08 |
|
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: 53.31 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQ--GDFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKPQKIapk 425
Cdd:cd03249 8 FRYPSRPDVPilKGLSLTIPPGKT-----VALVGSSGCGKSTVVSLLERFYDPTSGeilldgVDIRDLNLRWLRSQI--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 426 fpGTVRQ---LFFKKIRGQFL---NPQFQTDVVKPLR---IDDII-------DQEV-QH---LSGGELQRVAIVLALGIP 485
Cdd:cd03249 80 --GLVSQepvLFDGTIAENIRygkPDATDEEVEEAAKkanIHDFImslpdgyDTLVgERgsqLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 486 ADIYLIDEPSAYLDSEQRIICSKVIRRFILhnKKTAFIVEHDfIMATYLADKVIVFEG 543
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHR-LSTIRNADLIAVLQN 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
365-539 |
8.91e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.55 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGqdipklnvSMKPQKIAPKFPGTVRQLFFK-------- 436
Cdd:PRK11248 19 DINLTLESGE-----LLVVLGPSGCGKTTLLNLIAGFVPYQHG--------SITLDGKPVEGPGAERGVVFQnegllpwr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 437 ----------KIRGqFLNPQFQTDVVKPLRIDDIIDQE---VQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQR 503
Cdd:PRK11248 86 nvqdnvafglQLAG-VEKMQRLEIAHQMLKKVGLEGAEkryIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 398365537 504 IICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVI 539
Cdd:PRK11248 165 EQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELV 200
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
365-545 |
9.21e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGAL-------------------KPDEGQDIPKLNV--SMKPQKIA 423
Cdd:PRK13547 19 DLSLRIEPGR-----VTALLGRNGAGKSTLLKALAGDLtgggaprgarvtgdvtlngEPLAAIDAPRLARlrAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 424 PKFPGTVRQLFfkkIRGQFlnPQFQTDVVKPLRIDDIIDQ-------------EVQHLSGGELQRV--AIVLALGIPAD- 487
Cdd:PRK13547 94 PAFAFSAREIV---LLGRY--PHARRAGALTHRDGEIAWQalalagatalvgrDVTTLSGGELARVqfARVLAQLWPPHd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 488 ------IYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMA-------TYLADKVIVFEGIP 545
Cdd:PRK13547 169 aaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAarhadriAMLADGAIVAHGAP 239
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
324-562 |
1.14e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 54.07 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 324 AENLRFRTEALQFRIADATEDLQNDSASRAFS-----YPSLKKTQGDFVLnVEEGEFSDS--EILVMMGENGTGKTTLIK 396
Cdd:PRK13536 7 AEEAPRRLELSPIERKHQGISEAKASIPGSMStvaidLAGVSKSYGDKAV-VNGLSFTVAsgECFGLLGPNGAGKSTIAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 397 LLAGALKPDEGQdIPKLNVSMKPQK--------IAPKFPG-----TVRQ--LFFKKIRGqfLNPQFQTDVVKPL----RI 457
Cdd:PRK13536 86 MILGMTSPDAGK-ITVLGVPVPARArlararigVVPQFDNldlefTVREnlLVFGRYFG--MSTREIEAVIPSLlefaRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 458 DDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQR-IICSKVirRFILHNKKTAFIVEHDFIMATYLAD 536
Cdd:PRK13536 163 ESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARhLIWERL--RSLLARGKTILLTTHFMEEAERLCD 240
|
250 260
....*....|....*....|....*....
gi 398365537 537 KVIVFEGiPSKNAHARaPESLL---TGCN 562
Cdd:PRK13536 241 RLCVLEA-GRKIAEGR-PHALIdehIGCQ 267
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
101-294 |
1.24e-07 |
|
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: 51.93 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGrfddppewqEIikYFRGSELQNYfTKMLEDDIKAIIKPQYVDNIprai 180
Cdd:cd03247 26 KQGEKIALLGRSGSGKSTLLQLLTGDLKPQQG---------EI--TLDGVPVSDL-EKALSSLISVLNQRPYLFDT---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 181 kgpvqkvgellKLRmekspedvkryikilqlENVLKRdiekLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDvkqRLNA 260
Cdd:cd03247 90 -----------TLR-----------------NNLGRR----FSGGERQRLALARILLQDAPIVLLDEPTVGLD---PITE 134
|
170 180 190
....*....|....*....|....*....|....*.
gi 398365537 261 AQIIRSLL--APTKYVICVEHDLSVLDYLsDFVCII 294
Cdd:cd03247 135 RQLLSLIFevLKDKTLIWITHHLTGIEHM-DKILFL 169
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
91-295 |
1.24e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 53.97 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 91 SFKLHRlptprpGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDppewQEIIKYfRGSELQNYFTKMleddikaii 168
Cdd:COG4608 38 SFDIRR------GETLGLVGESGCGKSTLGRLLLRLEEPTSGEilFDG----QDITGL-SGRELRPLRRRM--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 169 kpQYV--DniPRAIKGPVQKVGEL----LKLRMEKSPEDVKRYIKILqLENV-LKRD-IEK----LSGGELQRFAIGMSC 236
Cdd:COG4608 98 --QMVfqD--PYASLNPRMTVGDIiaepLRIHGLASKAERRERVAEL-LELVgLRPEhADRypheFSGGQRQRIGIARAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 237 VQEADVYMFDEPSSYLDVKQRlnaAQIIrSLLAPTK------YVIcVEHDLSVLDYLSDFVCIIY 295
Cdd:COG4608 173 ALNPKLIVCDEPVSALDVSIQ---AQVL-NLLEDLQdelgltYLF-ISHDLSVVRHISDRVAVMY 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
354-540 |
1.28e-07 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQGDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLL-------AGALKPDeGQDIPKLNVSMKPQKIapkf 426
Cdd:cd03253 8 FAYDPGRPVLKDVSFTIPAGK-----KVAIVGPSGSGKSTILRLLfrfydvsSGSILID-GQDIREVTLDSLRRAI---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 427 pGTVRQ---LFFKKIRG--QFLNPQfQTD-----VVKPLRIDDII-------DQEVQH----LSGGELQRVAIVLALGIP 485
Cdd:cd03253 78 -GVVPQdtvLFNDTIGYniRYGRPD-ATDeevieAAKAAQIHDKImrfpdgyDTIVGErglkLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 486 ADIYLIDEPSAYLDS--EQRIIcsKVIRRfiLHNKKTAFIVEHDF--IMAtylADKVIV 540
Cdd:cd03253 156 PPILLLDEATSALDThtEREIQ--AALRD--VSKGRTTIVIAHRLstIVN---ADKIIV 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
373-500 |
1.31e-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: 52.66 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 373 GEFSDSEILVMMGENGTGKTTLIKLLAG-----------------ALKPDEGQDipklNVSMKPQ--KIAPKFpgTVRQ- 432
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGrvegggttsgqilfngqPRKPDQFQK----CVAYVRQddILLPGL--TVREt 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 433 -LFFKKIRGQFLNPQFQTDVVKP-LRIDDIIDQEVQH-----LSGGELQRVAIVLALGIPADIYLIDEPSAYLDS 500
Cdd:cd03234 102 lTYTAILRLPRKSSDAIRKKRVEdVLLRDLALTRIGGnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
381-505 |
1.38e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.47 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 381 LVMMGENGTGKTTLIKLLAGALkPDEG------QDIPKLNVSMKPQKIA-----PK-FPGTVRQ-LFFKKIRgqfLNPQF 447
Cdd:PRK11174 379 IALVGPSGAGKTSLLNALLGFL-PYQGslkingIELRELDPESWRKHLSwvgqnPQlPHGTLRDnVLLGNPD---ASDEQ 454
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 448 QTDVVKPLRIDDIIDQEVQHL-----------SGGELQRVAIVLALGIPADIYLIDEPSAYLD--SEQRII 505
Cdd:PRK11174 455 LQQALENAWVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDahSEQLVM 525
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
73-283 |
1.43e-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: 54.75 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 73 INLPTNLEA-HVTHRYSANSFKLHRLP-TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGrfddppewqEIIkyFRGS 150
Cdd:TIGR01193 468 NNLNGDIVInDVSYSYGYGSNILSDISlTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSG---------EIL--LNGF 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 151 ELQNYFTKMLEDDIkaiikpQYVDNIPRAIKGPVQKvGELLKLRMEKSPEDVKRYIKILQLenvlKRDIEK--------- 221
Cdd:TIGR01193 537 SLKDIDRHTLRQFI------NYLPQEPYIFSGSILE-NLLLGAKENVSQDEIWAACEIAEI----KDDIENmplgyqtel 605
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 222 ------LSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVkqrLNAAQIIRSLLAPT-KYVICVEHDLSV 283
Cdd:TIGR01193 606 seegssISGGQKQRIALARALLTDSKVLILDESTSNLDT---ITEKKIVNNLLNLQdKTIIFVAHRLSV 671
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
103-286 |
1.50e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.55 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLGrfddppewqEIIKYFRGSELQNYFTKMLEDDIKAIIKPQYVDNIpRAIKG 182
Cdd:PRK13651 33 GEFIAIIGQTGSGKTTFIEHLNALLLPDTG---------TIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKI-KKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 183 PVQKVG--------ELLKLRMEK-----------SPEDVK----RYIKILQL-ENVLKRDIEKLSGGELQRFAIGMSCVQ 238
Cdd:PRK13651 103 IRRRVGvvfqfaeyQLFEQTIEKdiifgpvsmgvSKEEAKkraaKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398365537 239 EADVYMFDEPSSYLD---VKQRLNaaqIIRSLLAPTKYVICVEHDL-SVLDY 286
Cdd:PRK13651 183 EPDFLVFDEPTAGLDpqgVKEILE---IFDNLNKQGKTIILVTHDLdNVLEW 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
365-543 |
1.59e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.17 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQDIPKlNVSMKPQKIApkfpGTVRQ---LFFKKIRGQ 441
Cdd:PRK13633 28 DVNLEVKKGEF-----LVILGRNGSGKSTIAKHMNALLIPSEGKVYVD-GLDTSDEENL----WDIRNkagMVFQNPDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 442 FLNPQFQTDV--------VKPLRIDDIIDQEVQ------------H-LSGGELQRVAIVLALGIPADIYLIDEPSAYLDS 500
Cdd:PRK13633 98 IVATIVEEDVafgpenlgIPPEEIRERVDESLKkvgmyeyrrhapHlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365537 501 EQRIICSKVIRRFilhNKK---TAFIVEHdFIMATYLADKVIVFEG 543
Cdd:PRK13633 178 SGRREVVNTIKEL---NKKygiTIILITH-YMEEAVEADRIIVMDS 219
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
3-70 |
1.71e-07 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 50.47 E-value: 1.71e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 3 DKNSRIAIVSADKCKpkKCRQeCKRSCPV--VKTGKLCIEVTPTSKIAFISEILCIGCGICVKKCPFDAI 70
Cdd:cd10549 29 GAIARGPEIDEDKCV--FCGA-CVEVCPTgaIELTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCPVDAI 95
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
82-282 |
1.81e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.83 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRY-SANSFKLHRLPTPRP-GQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGSELQNYFTKM 159
Cdd:PRK13648 12 NVSFQYqSDASFTLKDVSFNIPkGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-----------FYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 160 LEDDIKAIIkpQYVDNipraikgpvQKVGELLK------LRMEKSP-EDVKRYIK--ILQLENVLKRDIE--KLSGGELQ 228
Cdd:PRK13648 81 LRKHIGIVF--QNPDN---------QFVGSIVKydvafgLENHAVPyDEMHRRVSeaLKQVDMLERADYEpnALSGGQKQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398365537 229 RFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLApTKYV--ICVEHDLS 282
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKS-EHNItiISITHDLS 204
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
365-542 |
1.87e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.10 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFSdseilVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPkfpgTVRQLFFKKIRG---- 440
Cdd:PRK13634 25 DVNVSIPSGSYV-----AIIGHTGSGKSTLLQHLNGLLQPTSGT------VTIGERVITA----GKKNKKLKPLRKkvgi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 441 --QFLNPQ-FQTDVVK-----PLRI---------------------DDIIDQEVQHLSGGELQRVAIVLALGIPADIYLI 491
Cdd:PRK13634 90 vfQFPEHQlFEETVEKdicfgPMNFgvseedakqkaremielvglpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398365537 492 DEPSAYLDSEQRiicSKVIRRFI-LHNKK--TAFIVEHDFIMATYLADKVIVFE 542
Cdd:PRK13634 170 DEPTAGLDPKGR---KEMMEMFYkLHKEKglTTVLVTHSMEDAARYADQIVVMH 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
365-504 |
1.89e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 51.00 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGaLKPDEGQDI---PKLNVSMKPQKiaPKFP-GTVRQLffkkirg 440
Cdd:cd03223 19 DLSFEIKPGDR-----LLITGPSGTGKSSLFRALAG-LWPWGSGRIgmpEGEDLLFLPQR--PYLPlGTLREQ------- 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 441 qflnpqfqtdVVKPLriDDIidqevqhLSGGELQRVAIV-LALGIPaDIYLIDEPSAYLD--SEQRI 504
Cdd:cd03223 84 ----------LIYPW--DDV-------LSGGEQQRLAFArLLLHKP-KFVFLDEATSALDeeSEDRL 130
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
101-284 |
1.93e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 52.68 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF-------DDPPEWQEIIKY----FRGSELQnYFTKMLEDDIKAiik 169
Cdd:PRK13644 26 KKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtGDFSKLQGIRKLvgivFQNPETQ-FVGRTVEEDLAF--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 170 pqyvdnipraikGPvqkvgELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPS 249
Cdd:PRK13644 102 ------------GP-----ENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190
....*....|....*....|....*....|....*
gi 398365537 250 SYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVL 284
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL 199
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
18-73 |
1.94e-07 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 50.09 E-value: 1.94e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 18 PKKCRQ--ECKRSCPvvkTGklCIEVTPTSKIAFISEI---LCIGCGICVKKCPFDAIQII 73
Cdd:cd10549 5 PEKCIGcgICVKACP---TD--AIELGPNGAIARGPEIdedKCVFCGACVEVCPTGAIELT 60
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
383-540 |
1.99e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 53.18 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 383 MMGENGTGKTTLIKLLAGALKPDEGQ-----------DIPKLNVSMKPQKIApKFP----------GTvrqlffkKIRGQ 441
Cdd:PRK11432 37 LLGPSGCGKTTVLRLVAGLEKPTEGQifidgedvthrSIQQRDICMVFQSYA-LFPhmslgenvgyGL-------KMLGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 442 fLNPQFQTDVVKPLRIDDII---DQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNK 518
Cdd:PRK11432 109 -PKEERKQRVKEALELVDLAgfeDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFN 187
|
170 180
....*....|....*....|..
gi 398365537 519 KTAFIVEHDFIMATYLADKVIV 540
Cdd:PRK11432 188 ITSLYVTHDQSEAFAVSDTVIV 209
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
365-543 |
2.55e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.88 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALK--PDEGQ-DIPKLNVSMKP---QKIAPKfpGTVRQLFfkki 438
Cdd:COG2401 48 DLNLEIEPGE-----IVLIVGASGSGKSTLLRLLAGALKgtPVAGCvDVPDNQFGREAsliDAIGRK--GDFKDAV---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 439 rgQFLNPQFQTDVVKPLRiddiidqEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNK 518
Cdd:COG2401 117 --ELLNAVGLSDAVLWLR-------RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAG 187
|
170 180
....*....|....*....|....*
gi 398365537 519 KTAFIVEHDFIMATYLADKVIVFEG 543
Cdd:COG2401 188 ITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
82-282 |
2.80e-07 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSANSFKLHRLP-TPRPGQVLGLVGTNGIGKSTALKILAgkqkpnlgRFDDPPEWQEIIKyfrGSELQNYFTKML 160
Cdd:cd03253 5 NVTFAYDPGRPVLKDVSfTIPAGKKVAIVGPSGSGKSTILRLLF--------RFYDVSSGSILID---GQDIREVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 161 EddiKAI-IKPQ----YVDNIPRAIK-GpvqkvgellklRMEKSPEDVKRYIKILQLENVLKRDIE-----------KLS 223
Cdd:cd03253 74 R---RAIgVVPQdtvlFNDTIGYNIRyG-----------RPDATDEEVIEAAKAAQIHDKIMRFPDgydtivgerglKLS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 224 GGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLApTKYVICVEHDLS 282
Cdd:cd03253 140 GGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLS 197
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
373-513 |
2.94e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 51.76 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 373 GEFSDSEILVMMGENGTGKTTLIKLLAGALkPDEGQ------DIPKLNV-------SMKPQKIAPKFPGTVrqlffkkir 439
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEillngrPLSDWSAaelarhrAYLSQQQSPPFAMPV--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 440 GQFL--------NPQFQTDVV----KPLRIDDIIDQEVQHLSGGELQRV---AIVL----ALGIPADIYLIDEPSAYLDS 500
Cdd:COG4138 87 FQYLalhqpagaSSEAVEQLLaqlaEALGLEDKLSRPLTQLSGGEWQRVrlaAVLLqvwpTINPEGQLLLLDEPMNSLDV 166
|
170
....*....|...
gi 398365537 501 EQRIICSKVIRRF 513
Cdd:COG4138 167 AQQAALDRLLREL 179
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
102-501 |
3.05e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.40 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLGRfddppewqeiikyfrgselqnyftKMLEDDIKAIIKPQ--YVDNiPRA 179
Cdd:TIGR03719 30 PGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE------------------------ARPQPGIKVGYLPQepQLDP-TKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 180 IKGPVQK-VGELLKL----------------RMEKSPEDVKRYIKILQ------LENVLKR------------DIEKLSG 224
Cdd:TIGR03719 85 VRENVEEgVAEIKDAldrfneisakyaepdaDFDKLAAEQAELQEIIDaadawdLDSQLEIamdalrcppwdaDVTKLSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 225 GELQRFAIGMSCVQEADVYMFDEPSSYLDVKqrlNAAQIIRSLLAPTKYVICVEHDLSVLDylsdfvciiygvpsvygvv 304
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHDRYFLD------------------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 305 tlpaSVREGInIFLD-GH-IPAE-NLRFRTEALQFRIA--DATED-----LQND--------------SASRAFSYPSLK 360
Cdd:TIGR03719 223 ----NVAGWI-LELDrGRgIPWEgNYSSWLEQKQKRLEqeEKEESarqktLKRElewvrqspkgrqakSKARLARYEELL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 361 KTQ------------------GDFVLNVE--EGEFSD-------------SEILVMMGENGTGKTTLIKLLAGALKPDEG 407
Cdd:TIGR03719 298 SQEfqkrnetaeiyippgprlGDKVIEAEnlTKAFGDklliddlsfklppGGIVGVIGPNGAGKSTLFRMITGQEQPDSG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 408 qdipklnvsmkpqkiAPKFPGTVRQLFFKKIRGQfLNPQ---FQ-----TDVvkpLRIDDII---------------DQE 464
Cdd:TIGR03719 378 ---------------TIEIGETVKLAYVDQSRDA-LDPNktvWEeisggLDI---IKLGKREipsrayvgrfnfkgsDQQ 438
|
490 500 510
....*....|....*....|....*....|....*....
gi 398365537 465 --VQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSE 501
Cdd:TIGR03719 439 kkVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
365-539 |
3.07e-07 |
|
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: 51.51 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGqdipKLNVSMKPQKIAPK------------FPGT--V 430
Cdd:cd03269 18 DISFSVEKGE-----IFGLLGPNGAGKTTTIRMILGIILPDSG----EVLFDGKPLDIAARnrigylpeerglYPKMkvI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 431 RQL-FFKKIRGqfLNPQFQ----TDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRII 505
Cdd:cd03269 89 DQLvYLAQLKG--LKKEEArrriDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVEL 166
|
170 180 190
....*....|....*....|....*....|....
gi 398365537 506 CSKVIRRfILHNKKTAFIVEHDFIMATYLADKVI 539
Cdd:cd03269 167 LKDVIRE-LARAGKTVILSTHQMELVEELCDRVL 199
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
374-499 |
3.39e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 51.74 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 374 EFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQDIPKLNvSMKPQKIAPKFPGTVRQLFFKKirgQF--LNPQFQT-- 449
Cdd:PRK11629 31 SIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ-PMSKLSSAAKAELRNQKLGFIY---QFhhLLPDFTAle 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 450 DVVKPLRIDDI-----------------IDQEVQH----LSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:PRK11629 107 NVAMPLLIGKKkpaeinsralemlaavgLEHRANHrpseLSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
66-267 |
3.52e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 53.24 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 66 PFDAIQIINLPTNLEA-HVTHRYSAN-------SFKLhrlptpRPGQVLGLVGTNGIGKSTALKILAgkqkpnlgRFDDP 137
Cdd:COG1132 327 PPGAVPLPPVRGEIEFeNVSFSYPGDrpvlkdiSLTI------PPGETVALVGPSGSGKSTLVNLLL--------RFYDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 138 PEwQEI------IKYFRGSELQNYF------TKMLEDDIKaiikpqyvDNIpraikgpvqKVGellklRMEKSPEDVKRY 205
Cdd:COG1132 393 TS-GRIlidgvdIRDLTLESLRRQIgvvpqdTFLFSGTIR--------ENI---------RYG-----RPDATDEEVEEA 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365537 206 IKILQLENVLKR-----DIE------KLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKqrlNAAQIIRSL 267
Cdd:COG1132 450 AKAAQAHEFIEAlpdgyDTVvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTE---TEALIQEAL 519
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
102-495 |
4.14e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLGR---------FDDPPEWQE----IIKyfrgSELQnyftkmleddikaiI 168
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSilylgkevtFNGPKSSQEagigIIH----QELN--------------L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 169 KPQYvdNIPRAI---KGPVQKVGELLKLRMEkspEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMF 245
Cdd:PRK10762 91 IPQL--TIAENIflgREFVNRFGRIDWKKMY---AEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 246 DEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVciiygvpsvygvvtlpasvregiNIFLDGHIPAE 325
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDV-----------------------TVFRDGQFIAE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 326 NlrfrtealqfRIADATED-LQNDSASRAFS--YPSLKKTQGDFVLNVEE--GE------FS--DSEILVMMGENGTGKT 392
Cdd:PRK10762 223 R----------EVADLTEDsLIEMMVGRKLEdqYPRLDKAPGEVRLKVDNlsGPgvndvsFTlrKGEILGVSGLMGAGRT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 393 TLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFP------------------GTVRQL------------FFKKIRGQF 442
Cdd:PRK10762 293 ELMKVLYGALPRTSGY------VTLDGHEVVTRSPqdglangivyisedrkrdGLVLGMsvkenmsltalrYFSRAGGSL 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 443 LNPQFQTDVVKPLRIDDI----IDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPS 495
Cdd:PRK10762 367 KHADEQQAVSDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
368-540 |
4.28e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.15 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGaLKPDEGQDI-----------PKL-NVSMKPQKIA--PKFpgTVRQ- 432
Cdd:PRK11650 25 LDVADGEF-----IVLVGPSGCGKSTLLRMVAG-LERITSGEIwiggrvvnelePADrDIAMVFQNYAlyPHM--SVREn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 ----LffkKIRGqflNPQFQ-----TDVVKPLRIDDIIDQEVQHLSGGELQRVA----IVLAlgiPAdIYLIDEPSAYLD 499
Cdd:PRK11650 97 maygL---KIRG---MPKAEieervAEAARILELEPLLDRKPRELSGGQRQRVAmgraIVRE---PA-VFLFDEPLSNLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 398365537 500 SEQRIICSKVIRRfiLHN--KKTAFIVEHDFIMATYLADKVIV 540
Cdd:PRK11650 167 AKLRVQMRLEIQR--LHRrlKTTSLYVTHDQVEAMTLADRVVV 207
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
83-291 |
4.31e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.73 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 83 VTHRYSANSFKLHRLP--TPRpGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF---DDPPEWQEI--IKYFRGSELQN- 154
Cdd:PRK13652 9 LCYSYSGSKEALNNINfiAPR-NSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirGEPITKENIreVRKFVGLVFQNp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 155 ---YFTKMLEDDIKAiikpqyvdnipraikGPVQkvgelLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFA 231
Cdd:PRK13652 88 ddqIFSPTVEQDIAF---------------GPIN-----LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365537 232 IGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLlaPTKY---VICVEHDLSVLDYLSDFV 291
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDL--PETYgmtVIFSTHQLDLVPEMADYI 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
82-286 |
4.33e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 51.61 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSANSFK--------LHRLP-TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLG--RFDDPPEWQ---EIIKYF 147
Cdd:PRK10419 8 GLSHHYAHGGLSgkhqhqtvLNNVSlSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGnvSWRGEPLAKlnrAQRKAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 148 RGsELQNYFtkmlEDDIKAIiKPQYvdNIPRAIKGPVQ------------KVGELLKLrMEKSPEDvkryikilqlenvL 215
Cdd:PRK10419 88 RR-DIQMVF----QDSISAV-NPRK--TVREIIREPLRhllsldkaerlaRASEMLRA-VDLDDSV-------------L 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365537 216 KRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDvkqRLNAAQIIRSLLA-----PTKYVIcVEHDLSVLDY 286
Cdd:PRK10419 146 DKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD---LVLQAGVIRLLKKlqqqfGTACLF-ITHDLRLVER 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
373-513 |
4.70e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.47 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 373 GEFSDSEILVMMGENGTGKTTLIKLLAGALkPDEGQ-DIPKLNVSMKPQ-KIApkfpgTVRQLFFKKIRGQFLNPQFQ-- 448
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSiQFAGQPLEAWSAaELA-----RHRAYLSQQQTPPFAMPVFQyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 449 -----------------TDVVKPLRIDDIIDQEVQHLSGGELQRV---AIVL----ALGIPADIYLIDEPSAYLDSEQRI 504
Cdd:PRK03695 91 tlhqpdktrteavasalNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaAVVLqvwpDINPAGQLLLLDEPMNSLDVAQQA 170
|
....*....
gi 398365537 505 ICSKVIRRF 513
Cdd:PRK03695 171 ALDRLLSEL 179
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
368-543 |
4.71e-07 |
|
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: 51.04 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLN---VSMKPQKIapkfpGTVRQLFfkki 438
Cdd:cd03258 26 LSVPKGE-----IFGIIGRSGAGKSTLIRCINGLERPTSGsvlvdgTDLTLLSgkeLRKARRRI-----GMIFQHF---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 439 rGQFLNPQFQTDVVKPLRIDDI----IDQEVQH-----------------LSGGELQRVAIVLALGIPADIYLIDEPSAY 497
Cdd:cd03258 92 -NLLSSRTVFENVALPLEIAGVpkaeIEERVLEllelvgledkadaypaqLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 398365537 498 LDSE--QRII--CSKVIRRFILhnkkTAFIVEHDFIMATYLADKVIVFEG 543
Cdd:cd03258 171 LDPEttQSILalLRDINRELGL----TIVLITHEMEVVKRICDRVAVMEK 216
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
46-74 |
5.02e-07 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 47.03 E-value: 5.02e-07
10 20
....*....|....*....|....*....
gi 398365537 46 KIAFISEILCIGCGICVKKCPFDAIQIIN 74
Cdd:COG1149 4 KIPVIDEEKCIGCGLCVEVCPEGAIKLDD 32
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
368-559 |
5.23e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 51.25 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLL-------AGALKPDeGQDI--PKLNVSMKPQKiapkfPGTVRQLF---- 434
Cdd:PRK09493 22 LNIDQGE-----VVVIIGPSGSGKSTLLRCInkleeitSGDLIVD-GLKVndPKVDERLIRQE-----AGMVFQQFylfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 435 ---------FKKIRGQFLNPQFQTDVVKPLRIDDIIDQEVQH----LSGGELQRVAIVLALGIPADIYLIDEPSAYLDSE 501
Cdd:PRK09493 91 hltalenvmFGPLRVRGASKEEAEKQARELLAKVGLAERAHHypseLSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 502 QRIICSKVIRRfILHNKKTAFIVEHDFIMATYLADKVIVFEGipSKNAHARAPESLLT 559
Cdd:PRK09493 171 LRHEVLKVMQD-LAEEGMTMVIVTHEIGFAEKVASRLIFIDK--GRIAEDGDPQVLIK 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
101-281 |
5.39e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.09 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGkQKPNLGrfddppewqEIikYFRGSELQNYFTKMLeddikAIIKPQYVDNIPRAI 180
Cdd:PRK03695 20 RAGEILHLVGPNGAGKSTLLARMAG-LLPGSG---------SI--QFAGQPLEAWSAAEL-----ARHRAYLSQQQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 181 KGPVQKVGEL---LKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQ-------EADVYMFDEPSS 250
Cdd:PRK03695 83 AMPVFQYLTLhqpDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMN 162
|
170 180 190
....*....|....*....|....*....|.
gi 398365537 251 YLDVKQRLNAAQIIRSLLAPTKYVICVEHDL 281
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQGIAVVMSSHDL 193
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
8-72 |
5.47e-07 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 47.01 E-value: 5.47e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365537 8 IAIVSADKCKpkKCRqECKRSCPVVktgklCIEVTPTSKIAF-ISEILCIGCGICVKKCPFDAIQI 72
Cdd:COG1146 2 MPVIDTDKCI--GCG-ACVEVCPVD-----VLELDEEGKKALvINPEECIGCGACELVCPVGAITV 59
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
83-296 |
5.55e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.42 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 83 VTHRYSANSFKLHRLPTPRpGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikyfrgSELQNYFTKMLED 162
Cdd:PRK15056 14 VTWRNGHTALRDASFTVPG-GSIAALVGVNGSGKSTLFKALMGFVRLASGKI---------------SILGQPTRQALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 163 DIKAIIkPQY--VD-NIPRAIKGPVQ--KVGELLKLRMEKsPEDVKRYIKILQLENVLK---RDIEKLSGGELQRFAIGM 234
Cdd:PRK15056 78 NLVAYV-PQSeeVDwSFPVLVEDVVMmgRYGHMGWLRRAK-KRDRQIVTAALARVDMVEfrhRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365537 235 SCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIYG 296
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
91-503 |
5.97e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 91 SFKLHRlptprpGQVLGLVGTNGIGKS-TALKILAGKQKPNlGRFDDPPEW-----QEIIKYFRGSELQnyFTKMLEDDI 164
Cdd:PRK10261 36 SFSLQR------GETLAIVGESGSGKSvTALALMRLLEQAG-GLVQCDKMLlrrrsRQVIELSEQSAAQ--MRHVRGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 165 KAIIKPqyvdniPRAIKGPVQKVGELL--KLRM------EKSPEDVKRY---IKILQLENVLKRDIEKLSGGELQRFAIG 233
Cdd:PRK10261 107 AMIFQE------PMTSLNPVFTVGEQIaeSIRLhqgasrEEAMVEAKRMldqVRIPEAQTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 234 MSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKY-VICVEHDLSVLDYLSDFVCIIYgvpsvYGVVTLPASVRE 312
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMY-----QGEAVETGSVEQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 313 ginIFldgHIPAENLrfrTEALQFRIADATEdLQNDSASRAFSYPSLKKTQ-------------GDFVLN---------- 369
Cdd:PRK10261 256 ---IF---HAPQHPY---TRALLAAVPQLGA-MKGLDYPRRFPLISLEHPAkqeppieqdtvvdGEPILQvrnlvtrfpl 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 370 --------------VEEGEFS--DSEILVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIaPKFPGTVRQL 433
Cdd:PRK10261 326 rsgllnrvtrevhaVEKVSFDlwPGETLSLVGESGSGKSTTGRALLRLVESQGGE------IIFNGQRI-DTLSPGKLQA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 434 FFKKIRGQFLNPQFQTD--------VVKPLRIDDIIDQEV----------------QH-------LSGGELQRVAIVLAL 482
Cdd:PRK10261 399 LRRDIQFIFQDPYASLDprqtvgdsIMEPLRVHGLLPGKAaaarvawllervgllpEHawrypheFSGGQRQRICIARAL 478
|
490 500
....*....|....*....|.
gi 398365537 483 GIPADIYLIDEPSAYLDSEQR 503
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIR 499
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
383-543 |
6.05e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 383 MMGENGTGKTTLIKLLAGALKPDEGQDIpkLN---------------VSMKPQKIAPKFPGTVRQLF------FKKIRGQ 441
Cdd:PRK10575 42 LIGHNGSGKSTLLKMLGRHQPPSEGEIL--LDaqpleswsskafarkVAYLPQQLPAAEGMTVRELVaigrypWHGALGR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 442 FLNPQFQtdvvkplRIDDIID---------QEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRR 512
Cdd:PRK10575 120 FGAADRE-------KVEEAISlvglkplahRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHR 192
|
170 180 190
....*....|....*....|....*....|.
gi 398365537 513 FILHNKKTAFIVEHDFIMATYLADKVIVFEG 543
Cdd:PRK10575 193 LSQERGLTVIAVLHDINMAARYCDYLVALRG 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
101-249 |
6.16e-07 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 50.51 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLG--RFDD------PPEwqEIIKyfRG----SELQNYFTKM-LEDDIKAI 167
Cdd:cd03224 24 PEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsiRFDGrditglPPH--ERAR--AGigyvPEGRRIFPELtVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 168 IKPQYVDNIPRAIkgpvQKVGELLklrmeksPEdvkryikilqLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDE 247
Cdd:cd03224 100 AYARRRAKRKARL----ERVYELF-------PR----------LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
..
gi 398365537 248 PS 249
Cdd:cd03224 159 PS 160
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
91-282 |
6.28e-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: 50.61 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 91 SFKLHRlptprpGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDdppewqeiikyFRGS-----ELQNYFTKML--EDD 163
Cdd:cd03220 42 SFEVPR------GERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-----------VRGRvssllGLGGGFNPELtgREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 164 IKaiikpqyvdnipraikgpvqKVGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVY 243
Cdd:cd03220 105 IY--------------------LNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 398365537 244 MFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLS 282
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPS 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
103-267 |
6.28e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.78 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLG-------RFD--DPPEWQEIIKYFR--GSELQNY-----FTKMleddika 166
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlniagnHFDfsKTPSDKAIRELRRnvGMVFQQYnlwphLTVQ------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 167 iikpqyvDNIpraIKGPVqKVgelLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFD 246
Cdd:PRK11124 101 -------QNL---IEAPC-RV---LGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180
....*....|....*....|.
gi 398365537 247 EPSSYLDVKQRLNAAQIIRSL 267
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIREL 187
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
375-510 |
7.52e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.87 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 375 FSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQDIPKLNVSMKPQKIAPKFPGtvRQLFFKKIRGQFLNPQFQTDV--- 451
Cdd:PRK13541 23 FLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG--HNLGLKLEMTVFENLKFWSEIyns 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365537 452 -------VKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVI 510
Cdd:PRK13541 101 aetlyaaIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-524 |
7.65e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.68 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 374 EFSDSEILVMMGENGTGKTTLIKLLAG--ALKPD---------EGQDIPKLNVSMKPQKIAPKF--PGTVRQL-FFKKIR 439
Cdd:PRK14247 25 EIPDNTITALMGPSGSGKSTLLRVFNRliELYPEarvsgevylDGQDIFKMDVIELRRRVQMVFqiPNPIPNLsIFENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 440 -GQFLN------PQFQTDVVKPLR-------IDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQrii 505
Cdd:PRK14247 105 lGLKLNrlvkskKELQERVRWALEkaqlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEN--- 181
|
170
....*....|....*....
gi 398365537 506 cSKVIRRFILHNKKTAFIV 524
Cdd:PRK14247 182 -TAKIESLFLELKKDMTIV 199
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
353-542 |
8.74e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.89 E-value: 8.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 353 AFSYPSlkKTQG--DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPKLNVSMKPQKIap 424
Cdd:PRK13657 341 SFSYDN--SRQGveDVSFEAKPGQ-----TVAIVGPTGAGKSTLINLLQRVFDPQSGRilidgtDIRTVTRASLRRNI-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 425 kfpGTVRQ---LFFKKIRGqflNPQF------------------QTDVV--KPLRIDDIIDQEVQHLSGGELQRVAIVLA 481
Cdd:PRK13657 412 ---AVVFQdagLFNRSIED---NIRVgrpdatdeemraaaeraqAHDFIerKPDGYDTVVGERGRQLSGGERQRLAIARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365537 482 LGIPADIYLIDEPSAYLDSEQRIICSKVIRRfILHNkKTAFIVEHDfiMATYL-ADKVIVFE 542
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDE-LMKG-RTTFIIAHR--LSTVRnADRILVFD 543
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
375-543 |
8.91e-07 |
|
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: 52.32 E-value: 8.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 375 FSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQ------------DIPKLNVSMKPQKIAPKFPGTVRQ--LFFKKIRG 440
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTvlvggkdietnlDAVRQSLGMCPQHNILFHHLTVAEhiLFYAQLKG 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 441 Q-FLNPQFQTD-VVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFilHNK 518
Cdd:TIGR01257 1033 RsWEEAQLEMEaMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY--RSG 1110
|
170 180
....*....|....*....|....*.
gi 398365537 519 KTAFIVEHDFIMATYLADKV-IVFEG 543
Cdd:TIGR01257 1111 RTIIMSTHHMDEADLLGDRIaIISQG 1136
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
366-499 |
9.32e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 50.35 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 366 FVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPD------EGQD-----IPKLNVSMKPQKiAPKFPG-TVRQl 433
Cdd:PRK10771 18 FDLTVERGE-----RVAILGPSGAGKSTLLNLIAGFLTPAsgsltlNGQDhtttpPSRRPVSMLFQE-NNLFSHlTVAQ- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 434 ffkKIrGQFLNP-------QFQT--DVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:PRK10771 91 ---NI-GLGLNPglklnaaQREKlhAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
380-509 |
9.36e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.95 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 380 ILVMMGENGTGKTTLIKLLAGALKPD------EGQDIPKLNVSMKPQ--------KIAPKFpgTVRQLFFKKIRGQFLNP 445
Cdd:PRK13540 29 LLHLKGSNGAGKTTLLKLIAGLLNPEkgeilfERQSIKKDLCTYQKQlcfvghrsGINPYL--TLRENCLYDIHFSPGAV 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 446 QFqTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQ-RIICSKV 509
Cdd:PRK13540 107 GI-TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSlLTIITKI 170
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
461-539 |
9.55e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 50.74 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 461 IDQEVQ-----HLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEqriICSKVIR--RFILHNKKTAFIVEHDFIMATY 533
Cdd:PRK10619 141 IDERAQgkypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRimQQLAEEGKTMVVVTHEMGFARH 217
|
....*.
gi 398365537 534 LADKVI 539
Cdd:PRK10619 218 VSSHVI 223
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
102-296 |
9.63e-07 |
|
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: 50.23 E-value: 9.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF-----DDPPEWQEIikyfrGSELQNYftkmleddikaiikpQYVDNI 176
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVkvagaSPGKGWRHI-----GYVPQRH---------------EFAWDF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 177 PRAIKGPVQ--KVGELLKLRMEKSPE--DVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYL 252
Cdd:TIGR03771 65 PISVAHTVMsgRTGHIGWLRRPCVADfaAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 398365537 253 DVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIYG 296
Cdd:TIGR03771 145 DMPTQELLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLLNG 188
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
101-281 |
9.70e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.50 E-value: 9.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDDPPEWQeiIKYFrgselqnyftkmleddikaiikPQ--YVD-NIP 177
Cdd:PRK09544 28 KPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR--IGYV----------------------PQklYLDtTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 178 RAikgpvqkVGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQR 257
Cdd:PRK09544 84 LT-------VNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|....*
gi 398365537 258 LNAAQIIRSLLAPTKY-VICVEHDL 281
Cdd:PRK09544 157 VALYDLIDQLRRELDCaVLMVSHDL 181
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
368-542 |
1.01e-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: 50.13 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ----------DIpklnVSMKPQKIApkfpgTVRqlffKK 437
Cdd:COG4778 32 FSVAAGEC-----VALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdggwvDL----AQASPREIL-----ALR----RR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 438 IRG---QFLN--PQFQT-DVV-KPLRiDDIIDQEV---------------QHL--------SGGELQRVAIVLALGIPAD 487
Cdd:COG4778 94 TIGyvsQFLRviPRVSAlDVVaEPLL-ERGVDREEarararellarlnlpERLwdlppatfSGGEQQRVNIARGFIADPP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 488 IYLIDEPSAYLDSEQRiicSKVIRrfILHNKK---TAFI-VEHDF-IMATyLADKVIVFE 542
Cdd:COG4778 173 LLLLDEPTASLDAANR---AVVVE--LIEEAKargTAIIgIFHDEeVREA-VADRVVDVT 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
379-543 |
1.07e-06 |
|
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: 50.18 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 379 EILVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPKLNVSMKPQKIapkfpGTVRQ---LFFKKIRGQFLNPQFQT 449
Cdd:cd03252 29 EVVGIVGRSGSGKSTLTKLIQRFYVPENGRvlvdghDLALADPAWLRRQV-----GVVLQenvLFNRSIRDNIALADPGM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 450 DVVK-----------------PLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSE-QRIICSKVir 511
Cdd:cd03252 104 SMERvieaaklagahdfiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYEsEHAIMRNM-- 181
|
170 180 190
....*....|....*....|....*....|..
gi 398365537 512 RFILHNkKTAFIVEHDfIMATYLADKVIVFEG 543
Cdd:cd03252 182 HDICAG-RTVIIIAHR-LSTVKNADRIIVMEK 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
103-280 |
1.36e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.85 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDdppewqeiikyFRGSEL--------------QNY--FTKMleddika 166
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIR-----------FHGTDVsrlhardrkvgfvfQHYalFRHM------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 167 iikpQYVDNI-------PR-------AIKgpvQKVGELLKlrmekspedvkryikILQLENVLKRDIEKLSGGELQRFAI 232
Cdd:PRK10851 90 ----TVFDNIafgltvlPRrerpnaaAIK---AKVTQLLE---------------MVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365537 233 GMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYV-ICVEHD 280
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTsVFVTHD 196
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
5-74 |
1.48e-06 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 50.32 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 5 NSRIAIVSADKCKpkKCrQECKRSCPvvktgKLCIEVTPTSKIAFIS--------------EILCIGCGICVKKCPFDAI 70
Cdd:PRK07118 159 ENGLPVVDEDKCT--GC-GACVKACP-----RNVIELIPKSARVFVAcnskdkgkavkkvcEVGCIGCGKCVKACPAGAI 230
|
....
gi 398365537 71 QIIN 74
Cdd:PRK07118 231 TMEN 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
91-133 |
1.59e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 49.69 E-value: 1.59e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 398365537 91 SFKLHRlptprpGQVLGLVGTNGIGKSTALKILAGKQKPNLGR 133
Cdd:COG1134 46 SFEVER------GESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
354-531 |
1.60e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.13 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQGDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFPGTVRQL 433
Cdd:PRK10522 330 FAYQDNGFSVGPINLTIKRGE-----LLFLIGGNGSGKSTLAMLLTGLYQPQSGE------ILLDGKPVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 434 F---FKKIR--GQFLNPQFQTdvVKPLRIDDIIDQ-EVQH-------------LSGGELQRVAIVLALGIPADIYLIDEP 494
Cdd:PRK10522 399 FsavFTDFHlfDQLLGPEGKP--ANPALVEKWLERlKMAHkleledgrisnlkLSKGQKKRLALLLALAEERDILLLDEW 476
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398365537 495 SAYLDSEQRIICSKVIRRFILHNKKTAFIVEHD---FIMA 531
Cdd:PRK10522 477 AADQDPHFRREFYQVLLPLLQEMGKTIFAISHDdhyFIHA 516
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
360-510 |
1.65e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.51 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 360 KKTQGDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKPQK---IAPKFPGTV 430
Cdd:PRK10895 16 RRVVEDVSLTVNSGE-----IVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddEDISLLPLHARARRgigYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 431 RQL-------FFKKIRGQFLNPQFQ---TDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDS 500
Cdd:PRK10895 91 RRLsvydnlmAVLQIRDDLSAEQREdraNELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170
....*....|
gi 398365537 501 EQRIICSKVI 510
Cdd:PRK10895 171 ISVIDIKRII 180
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
330-547 |
1.67e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 50.23 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 330 RTEALQFRIADATEDLQndsasrafsypslkktqgDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ- 408
Cdd:PRK13636 7 KVEELNYNYSDGTHALK------------------GININIKKGE-----VTAILGGNGAGKSTLFQNLNGILKPSSGRi 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 409 --DIPKLNVSMK-----PQKIAPKFPGTVRQLF----FKKIRGQFLNPQFQTDVVKPlRIDDII---------DQEVQHL 468
Cdd:PRK13636 64 lfDGKPIDYSRKglmklRESVGMVFQDPDNQLFsasvYQDVSFGAVNLKLPEDEVRK-RVDNALkrtgiehlkDKPTHCL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 469 SGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIV-------F 541
Cdd:PRK13636 143 SFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVmkegrviL 222
|
....*.
gi 398365537 542 EGIPSK 547
Cdd:PRK13636 223 QGNPKE 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
103-279 |
1.72e-06 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 49.19 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQkPNLGRFD----------DPPEWQEIIKYFRGSE-LQNYFTkmLEDDIKAIIKpq 171
Cdd:cd03234 33 GQVMAILGSSGSGKTTLLDAISGRV-EGGGTTSgqilfngqprKPDQFQKCVAYVRQDDiLLPGLT--VRETLTYTAI-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 172 yvdnipraIKGPVQKVGEllklrmEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSY 251
Cdd:cd03234 108 --------LRLPRKSSDA------IRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180
....*....|....*....|....*...
gi 398365537 252 LDVKQRLNAAQIIRSLLAPTKYVICVEH 279
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
101-282 |
1.76e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 49.75 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF---------DDP-PEWQEIIKYFR---GSELQNYftkmleddiKAI 167
Cdd:PRK11264 27 KPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtARSlSQQKGLIRQLRqhvGFVFQNF---------NLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 168 IKPQYVDNIpraIKGPVQKVGELLKLRMEKSPEDVKRyIKILQLENVLKRdieKLSGGELQRFAIGMSCVQEADVYMFDE 247
Cdd:PRK11264 98 PHRTVLENI---IEGPVIVKGEPKEEATARARELLAK-VGLAGKETSYPR---RLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 398365537 248 PSSYLD---VKQRLNAaqiIRSLLAPTKYVICVEHDLS 282
Cdd:PRK11264 171 PTSALDpelVGEVLNT---IRQLAQEKRTMVIVTHEMS 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
101-267 |
1.98e-06 |
|
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: 49.08 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDppewQEIIKY--FRGSEL--------QNYFTKM-LEDDIKAI 167
Cdd:cd03218 24 KQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilLDG----QDITKLpmHKRARLgigylpqeASIFRKLtVEENILAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 168 IKPQYVDNIPRAikgpvQKVGELLKLrmekspedvkryikiLQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDE 247
Cdd:cd03218 100 LEIRGLSKKERE-----EKLEELLEE---------------FHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180
....*....|....*....|
gi 398365537 248 PSSYLDVKQRLNAAQIIRSL 267
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKIL 179
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
215-291 |
2.01e-06 |
|
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: 48.47 E-value: 2.01e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 215 LKRDIEKLSGGELQRFAIG--MSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYlSDFV 291
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWI 158
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
84-295 |
2.22e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.40 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 84 THRYSANSFKLHRLP-------TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF--DDPPewqeiIKY----FRGS 150
Cdd:PRK15112 13 TFRYRTGWFRRQTVEavkplsfTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliDDHP-----LHFgdysYRSQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 151 ELqnyftKMLEDDikaiikpqyvdniPRAIKGPVQKVGEL----LKLRMEKSPEDVKRYIkILQLENV-LKRD-----IE 220
Cdd:PRK15112 88 RI-----RMIFQD-------------PSTSLNPRQRISQIldfpLRLNTDLEPEQREKQI-IETLRQVgLLPDhasyyPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 221 KLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRlnaAQIIRSLLAPTK-----YVICVEHdLSVLDYLSDFVCIIY 295
Cdd:PRK15112 149 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR---SQLINLMLELQEkqgisYIYVTQH-LGMMKHISDQVLVMH 224
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
4-73 |
2.30e-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: 319872 [Multi-domain] Cd Length: 130 Bit Score: 47.19 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 4 KNSRIAIVS---ADKCKPKKCRQ----ECKRSCPV------VKTGklcievtptskIAFISEILCIGCGICVKKCPFDAI 70
Cdd:cd10550 29 SLSRIRVVRfepEGLDVPVVCRQcedaPCVEACPVgaisrdEETG-----------AVVVDEDKCIGCGMCVEACPFGAI 97
|
...
gi 398365537 71 QII 73
Cdd:cd10550 98 RVD 100
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
11-77 |
2.48e-06 |
|
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: 49.22 E-value: 2.48e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 11 VSADKCKPKKCRQECKRSCPVVKTgKLCIEVTPTSKIAFIS-----EILCIGCGICVKKCPFDAIQIIN--LPT 77
Cdd:COG2878 91 VEAGPLDPEVAVVRCNGGCEKAKP-KYEYDGIKDCRAAVIGgpkgcEYGCIGCGDCIKACPFDAIVGAAkgMHT 163
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
330-542 |
2.66e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 50.18 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 330 RTEALQFRIADATEDLQNDSASRA-------------FSYPSLKKTQGdFVLNVEEGEFSDSEILVMMGENGTGKTTLIK 396
Cdd:COG4615 298 KIEELELALAAAEPAAADAAAPPApadfqtlelrgvtYRYPGEDGDEG-FTLGPIDLTIRRGELVFIVGGNGSGKSTLAK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 397 LLAGALKPDEGQdipklnVSMKPQKIAPKFPGTVRQLF---------FKK---IRGQFLNPQFQTDVVKpLRIDD---II 461
Cdd:COG4615 377 LLTGLYRPESGE------ILLDGQPVTADNREAYRQLFsavfsdfhlFDRllgLDGEADPARARELLER-LELDHkvsVE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 462 DQEV--QHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRiicskviRRF---ILHN-K---KTAFIVEHD---Fi 529
Cdd:COG4615 450 DGRFstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFR-------RVFyteLLPElKargKTVIAISHDdryF- 521
|
250
....*....|...
gi 398365537 530 matYLADKVIVFE 542
Cdd:COG4615 522 ---DLADRVLKMD 531
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
378-523 |
2.66e-06 |
|
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: 48.41 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 378 SEILVMMGENGTGKTTLIKLLAGALKPDEGqdiPKLNVS---MKPQKIAPKFPG---------------TVRQL--FFKK 437
Cdd:cd03233 33 GEMVLVLGRPGSGCSTLLKALANRTEGNVS---VEGDIHyngIPYKEFAEKYPGeiiyvseedvhfptlTVRETldFALR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 438 IRGqflnpqfqtdvvkplriddiiDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHN 517
Cdd:cd03233 110 CKG---------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVL 168
|
....*.
gi 398365537 518 KKTAFI 523
Cdd:cd03233 169 KTTTFV 174
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
381-540 |
2.69e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.40 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 381 LVMMGENGTGKTTLIKLLAGALKPDEGQ---DIPKL---NVSMKPQKIAPKFPGTVRQLFFKKIRGQFLN-P-QFQTDVV 452
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTSGElliDDHPLhfgDYSYRSQRIRMIFQDPSTSLNPRQRISQILDfPlRLNTDLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 453 KPLRIDDIIDQEVQ------H-------LSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRiicSKVIRRFI-LHNK 518
Cdd:PRK15112 122 PEQREKQIIETLRQvgllpdHasyyphmLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR---SQLINLMLeLQEK 198
|
170 180
....*....|....*....|....
gi 398365537 519 K-TAFI-VEHDFIMATYLADKVIV 540
Cdd:PRK15112 199 QgISYIyVTQHLGMMKHISDQVLV 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
102-296 |
3.03e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 49.44 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLGR---FDDP-PEWQEIIKYFRGselqnyftkmleddikaiIKPQYvDNIP 177
Cdd:PRK13536 66 SGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvLGVPvPARARLARARIG------------------VVPQF-DNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 178 R--AIKGPVQKVGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVK 255
Cdd:PRK13536 127 LefTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 398365537 256 QRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIYG 296
Cdd:PRK13536 207 ARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEA 247
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
360-542 |
3.09e-06 |
|
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: 50.19 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 360 KKTQGDFVLNVEEGEFSDSEILVMMGENGTGKTTLIKLLAG--ALKPDEGQDI----------------------PKLNV 415
Cdd:TIGR03269 8 KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIyhvalcekcgyverpskvgepcPVCGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 416 SMKPQKIAP-KFPGTVRQLFFKKIRGQFL-------NPQFQTDVVKPL------------RIDDIIDQ-EVQH------- 467
Cdd:TIGR03269 88 TLEPEEVDFwNLSDKLRRRIRKRIAIMLQrtfalygDDTVLDNVLEALeeigyegkeavgRAVDLIEMvQLSHrithiar 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365537 468 -LSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFE 542
Cdd:TIGR03269 168 dLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLE 243
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
101-281 |
3.12e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 48.68 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQkPNLGR--FDDPPewqeiIKYFRGSEL---QNYFtkmleddikaiikPQYVDN 175
Cdd:COG4138 20 NAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEilLNGRP-----LSDWSAAELarhRAYL-------------SQQQSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 176 ipraikGPVQKVGELLKLRMEKSPEDVKRYIKI------LQLENVLKRDIEKLSGGELQRFAIGMSCVQ-------EADV 242
Cdd:COG4138 81 ------PFAMPVFQYLALHQPAGASSEAVEQLLaqlaeaLGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 398365537 243 YMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDL 281
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDL 193
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
91-296 |
3.14e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.06 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 91 SFKLhrlptpRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDdppewqeIIKYFRGSELQNYFTKMLEDDIKAIIK- 169
Cdd:PRK13641 27 SFEL------EEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTIT-------IAGYHITPETGNKNLKKLRKKVSLVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 170 --PQYVDN-IPRAIK-GPVQkvgelLKLRMEKSPEDVKRYIKILQL-ENVLKRDIEKLSGGELQRFAIGMSCVQEADVYM 244
Cdd:PRK13641 94 peAQLFENtVLKDVEfGPKN-----FGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365537 245 FDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDL-SVLDYLSDFVCIIYG 296
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHG 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
82-281 |
3.34e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 48.93 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 82 HVTHRYSaNSFKLH----RLPtprPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDppewQEIIKYfRGSELqny 155
Cdd:COG4604 6 NVSKRYG-GKVVLDdvslTIP---KGGITALIGPNGAGKSTLLSMISRLLPPDSGEvlVDG----LDVATT-PSREL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 156 fTKMLeddikAIIKpQyvDN--IPRAikgpvqKVGELL--------KLRMekSPED---VKRYIKILQLENVLKRDIEKL 222
Cdd:COG4604 74 -AKRL-----AILR-Q--ENhiNSRL------TVRELVafgrfpysKGRL--TAEDreiIDEAIAYLDLEDLADRYLDEL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365537 223 SGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQrlnAAQIIRSL--LAPT--KYVICVEHDL 281
Cdd:COG4604 137 SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKH---SVQMMKLLrrLADElgKTVVIVLHDI 196
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
365-504 |
3.59e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.81 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGaLKPD-EGQ-DIPKLNVSM-KPQKiaPKFP-GTVR-QLFFKKIR 439
Cdd:COG4178 381 DLSLSLKPGER-----LLITGPSGSGKSTLLRAIAG-LWPYgSGRiARPAGARVLfLPQR--PYLPlGTLReALLYPATA 452
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365537 440 GQFLNPQFQtDVVKPLRIDDIIDQ--EVQH----LSGGELQRVAIVLALGIPADIYLIDEPSAYLD--SEQRI 504
Cdd:COG4178 453 EAFSDAELR-EALEAVGLGHLAERldEEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDeeNEAAL 524
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
91-289 |
3.63e-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: 48.58 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 91 SFKLH-----RLP-------TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDPPEW--------QEIIkYFR 148
Cdd:COG4778 13 TFTLHlqggkRLPvldgvsfSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWvdlaqaspREIL-ALR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 149 GSELqNYFTkmleddikaiikpQYVDNIPRaiKGPVQKVGELLkLRMEKSPEDVKRyikilQLENVLKR-DI-EKL---- 222
Cdd:COG4778 92 RRTI-GYVS-------------QFLRVIPR--VSALDVVAEPL-LERGVDREEARA-----RARELLARlNLpERLwdlp 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 223 ----SGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSD 289
Cdd:COG4778 150 patfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVAD 220
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
90-263 |
3.65e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 90 NSFKLHRLPTPRpgqvLGLVGTNGIGKSTALKILAGKQKPNLGRfddppewqeiIKYFRGSELqNYFTkmleddikaiik 169
Cdd:PRK10636 329 DSIKLNLVPGSR----IGLLGRNGAGKSTLIKLLAGELAPVSGE----------IGLAKGIKL-GYFA------------ 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 170 pQYVDNIPRAIKGPVQKVGELLKLRMEKSPEDvkrYIKILQLENVLKRDI-EKLSGGELQRFAIGMSCVQEADVYMFDEP 248
Cdd:PRK10636 382 -QHQLEFLRADESPLQHLARLAPQELEQKLRD---YLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170
....*....|....*..
gi 398365537 249 SSYLDV--KQRLNAAQI 263
Cdd:PRK10636 458 TNHLDLdmRQALTEALI 474
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
101-282 |
3.86e-06 |
|
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: 48.29 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--------FDDPPEWQEIIKYFrGSELQNY--FTKM--LEDDIKAII 168
Cdd:cd03262 24 KKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTiiidglklTDDKKNINELRQKV-GMVFQQFnlFPHLtvLENITLAPI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 169 KpqyVDNIPRAikgpvqkvgELLKLRMEkspedvkrYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEP 248
Cdd:cd03262 103 K---VKGMSKA---------EAEERALE--------LLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 398365537 249 SSYLD---VKQRLnaaQIIRSLLAPTKYVICVEHDLS 282
Cdd:cd03262 163 TSALDpelVGEVL---DVMKDLAEEGMTMVVVTHEMG 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
101-295 |
4.58e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 48.58 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLG--RFDD------------PPEWQEIIKYFRGSELQNYFTKMLEDdikA 166
Cdd:PRK13643 30 KKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvTVGDivvsstskqkeiKPVRKKVGVVFQFPESQLFEETVLKD---V 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 167 IIKPQYV----DNIPRAIKGPVQKVGeLLKLRMEKSPEDvkryikilqlenvlkrdiekLSGGELQRFAIGMSCVQEADV 242
Cdd:PRK13643 107 AFGPQNFgipkEKAEKIAAEKLEMVG-LADEFWEKSPFE--------------------LSGGQMRRVAIAGILAMEPEV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365537 243 YMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHdlsVLDYLSDFVCIIY 295
Cdd:PRK13643 166 LVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH---LMDDVADYADYVY 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
374-541 |
4.67e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.23 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 374 EFSDSEILVMMGENGTGKTTLIKLL--AGALKPD---------EGQDI--PKLN-------VSMKPQKIAPkFPGTVRQ- 432
Cdd:PRK14239 27 DFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtitgsivyNGHNIysPRTDtvdlrkeIGMVFQQPNP-FPMSIYEn 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 -LFFKKIRGQFLNPQFQTDVVKPLRIDDIIDqEVQ---H-----LSGGELQRVAIVLALGIPADIYLIDEPSAYLDSeqr 503
Cdd:PRK14239 106 vVYGLRLKGIKDKQVLDEAVEKSLKGASIWD-EVKdrlHdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDP--- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398365537 504 iICSKVIRR--FILHNKKTAFIVEHDFIMATYLADKVIVF 541
Cdd:PRK14239 182 -ISAGKIEEtlLGLKDDYTMLLVTRSMQQASRISDRTGFF 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
379-541 |
5.25e-06 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 47.04 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 379 EILVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFPGTVRQLffkkirGQFLNPQ--FQTDVVKPLR 456
Cdd:cd03215 27 EIVGIAGLVGNGQTELAEALFGLRPPASGE------ITLDGKPVTRRSPRDAIRA------GIAYVPEdrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 457 IDD--IIdqeVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD--SEQRIIcsKVIRRfiLHNKKTAFIV---EHDFI 529
Cdd:cd03215 95 VAEniAL---SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDvgAKAEIY--RLIRE--LADAGKAVLLissELDEL 167
|
170
....*....|..
gi 398365537 530 MAtyLADKVIVF 541
Cdd:cd03215 168 LG--LCDRILVM 177
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
365-545 |
5.41e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.22 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPD------EGQDIPKLNVSMKPqkiapkfpgTVRqlffKKI 438
Cdd:PRK11831 25 NISLTVPRGK-----ITAIMGPSGIGKTTLLRLIGGQIAPDhgeilfDGENIPAMSRSRLY---------TVR----KRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 439 RGQFLNPQFQTD------VVKPLRIDDIIDQEVQH----------------------LSGGELQRVAIVLALGIPADIYL 490
Cdd:PRK11831 87 SMLFQSGALFTDmnvfdnVAYPLREHTQLPAPLLHstvmmkleavglrgaaklmpseLSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365537 491 IDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHD----FIMATY---LADKVIVFEGIP 545
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDvpevLSIADHayiVADKKIVAHGSA 228
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
369-527 |
5.49e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.60 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 369 NVEEGEFsDSEILVMMGENGTGKTTLIKLLAGALKpdeGQDIPKLNVSMKPQKIAPKfpGTVR---QLFFKKIRG----- 440
Cdd:cd03240 14 ERSEIEF-FSPLTLIVGQNGAGKTTIIEALKYALT---GELPPNSKGGAHDPKLIRE--GEVRaqvKLAFENANGkkyti 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 441 -----QFLNPQF--QTDvvkplrIDDIIDQEVQHLSGGE--LQRVAIVLAL----GIPADIYLIDEPSAYLDSEQRiiCS 507
Cdd:cd03240 88 trslaILENVIFchQGE------SNWPLLDMRGRCSGGEkvLASLIIRLALaetfGSNCGILALDEPTTNLDEENI--EE 159
|
170 180
....*....|....*....|...
gi 398365537 508 KVIRRFILHNKKTAF---IVEHD 527
Cdd:cd03240 160 SLAEIIEERKSQKNFqliVITHD 182
|
|
| DMSOR_beta_like |
cd16371 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
38-72 |
5.61e-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: 46.40 E-value: 5.61e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 398365537 38 CIEVTPT---SK----IAFISEILCIGCGICVKKCPFDAIQI 72
Cdd:cd16371 62 CVKVCPTgaiTKredgIVVVDQDKCIGCGYCVWACPYGAPQY 103
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
365-503 |
6.38e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.20 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFSdseilVMMGENGTGKTTLIKLLAGALKPDEGQ---DIPKLNVSMKPQKIAP---------KFPGTvrQ 432
Cdd:PRK13649 25 DVNLTIEDGSYT-----AFIGHTGSGKSTIMQLLNGLHVPTQGSvrvDDTLITSTSKNKDIKQirkkvglvfQFPES--Q 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 LFFKKI-RGQFLNPQ----FQTDVVKPLR--------IDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:PRK13649 98 LFEETVlKDVAFGPQnfgvSQEEAEALAReklalvgiSESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
....
gi 398365537 500 SEQR 503
Cdd:PRK13649 178 PKGR 181
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
103-279 |
6.49e-06 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 47.49 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDDPPewqEIIKYFRGSELQNyftkMLeddikaiikpqYVDNIPrAIKG 182
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---GPLDFQRDSIARG----LL-----------YLGHAP-GIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 183 PVQKVGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQ 262
Cdd:cd03231 87 TLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170
....*....|....*..
gi 398365537 263 IIRSLLAPTKYVICVEH 279
Cdd:cd03231 167 AMAGHCARGGMVVLTTH 183
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
55-74 |
7.18e-06 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 45.85 E-value: 7.18e-06
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
25-70 |
7.32e-06 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 45.47 E-value: 7.32e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 398365537 25 CKRSCPVvktGKLCIEVTPTSKIafiSEILCIGCGICVKKCPFDAI 70
Cdd:cd10549 86 CVKVCPV---DAITLEDELEIVI---DKEKCIGCGICAEVCPVNAI 125
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
104-286 |
7.95e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 48.31 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 104 QVLGLVGTNGIGKSTALKILAGKQKPNLG-------RFDDPPEWQEIIKYFRGSELQNYftKMLEDDIKAIIK-PQYV-- 173
Cdd:PRK13631 53 KIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiYIGDKKNNHELITNPYSKKIKNF--KELRRRVSMVFQfPEYQlf 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 174 -DNIPRAIK-GPVQkvgelLKLRMEKSPEDVKRYIKILQL-ENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSS 250
Cdd:PRK13631 131 kDTIEKDIMfGPVA-----LGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTA 205
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398365537 251 YLDVKQRLNAAQIIRSLLAPTKYVICV----EHDLSVLDY 286
Cdd:PRK13631 206 GLDPKGEHEMMQLILDAKANNKTVFVIthtmEHVLEVADE 245
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
104-296 |
8.68e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 47.72 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 104 QVLGLVGTNGIGKSTALKILAgkqkpNLGRFDDPPEWQEIIKYFRGS--ELQNYFTKMLEDDIKAIIKPQYV-----DNI 176
Cdd:PRK14258 34 KVTAIIGPSGCGKSTFLKCLN-----RMNELESEVRVEGRVEFFNQNiyERRVNLNRLRRQVSMVHPKPNLFpmsvyDNV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 177 PRAIKgpvqKVGELLKLRMEkspEDVKRYIKILQLENVLKRDIEK----LSGGELQRFAIGMSCVQEADVYMFDEPSSYL 252
Cdd:PRK14258 109 AYGVK----IVGWRPKLEID---DIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398365537 253 DVKQRLNAAQIIRSL-LAPTKYVICVEHDLSVLDYLSDFVCIIYG 296
Cdd:PRK14258 182 DPIASMKVESLIQSLrLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
18-74 |
9.04e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 48.70 E-value: 9.04e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 18 PKKCRQeCKRscpvvktgklCIEVTPTSKI-------AFISEILCIGCGICVKKCPFDAIQIIN 74
Cdd:COG1148 495 PEKCTG-CGR----------CVEVCPYGAIsidekgvAEVNPALCKGCGTCAAACPSGAISLKG 547
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
11-72 |
9.42e-06 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 43.50 E-value: 9.42e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365537 11 VSADKCKpkKCRqECKRSCPVvktgkLCIEVTpTSKIAFISEiLCIGCGICVKKCPFDAIQI 72
Cdd:COG2221 12 IDEEKCI--GCG-LCVAVCPT-----GAISLD-DGKLVIDEE-KCIGCGACIRVCPTGAIKG 63
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
99-592 |
9.98e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 99 TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDDPPEWQeiikyfrgSELQNYFTKMLedDIKAIikpQYV---DN 175
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQ--------LAWVNQETPAL--PQPAL---EYVidgDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 176 IPRAIKGPVQKVGE--------LL--KLRMEKSPEDVKRYIKILQ----LENVLKRDIEKLSGGELQRFAIGMSCVQEAD 241
Cdd:PRK10636 90 EYRQLEAQLHDANErndghaiaTIhgKLDAIDAWTIRSRAASLLHglgfSNEQLERPVSDFSGGWRMRLNLAQALICRSD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 242 VYMFDEPSSYLDvkqrLNAaqII---RSLLAPTKYVICVEHDLSVLDYLSDFVCII--------YGVPSVYGV------- 303
Cdd:PRK10636 170 LLLLDEPTNHLD----LDA--VIwleKWLKSYQGTLILISHDRDFLDPIVDKIIHIeqqslfeyTGNYSSFEVqratrla 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 304 --VTLPASVREGInifldGHIPAENLRFRTEA-----LQFR---------IADATEDLQNDSASRA---FSYPSLKKTQ- 363
Cdd:PRK10636 244 qqQAMYESQQERV-----AHLQSYIDRFRAKAtkakqAQSRikmlermelIAPAHVDNPFHFSFRApesLPNPLLKMEKv 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 364 ----GDFV------LNVEEGefsdSEIlVMMGENGTGKTTLIKLLAGALKPDEGqDIP-----KLNVSMKPQ-------- 420
Cdd:PRK10636 319 sagyGDRIildsikLNLVPG----SRI-GLLGRNGAGKSTLIKLLAGELAPVSG-EIGlakgiKLGYFAQHQleflrade 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 421 -------KIAPKfpGTVRQLffKKIRGQFlnpQFQTDVVKplriddiidQEVQHLSGGELQRVAIVLALGIPADIYLIDE 493
Cdd:PRK10636 393 splqhlaRLAPQ--ELEQKL--RDYLGGF---GFQGDKVT---------EETRRFSGGEKARLVLALIVWQRPNLLLLDE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 494 PSAYLDSEQRIICSKVIRRFilhnKKTAFIVEHD--FIMAT----YLA--DKVIVFEG--------------IPSKNAHA 551
Cdd:PRK10636 457 PTNHLDLDMRQALTEALIDF----EGALVVVSHDrhLLRSTtddlYLVhdGKVEPFDGdledyqqwlsdvqkQENQTDEA 532
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 398365537 552 RAPESLLTGCNRF-LKNLNVTFRRDPNSFRPRINKLDSQMDK 592
Cdd:PRK10636 533 PKENNANSAQARKdQKRREAELRTQTQPLRKEIARLEKEMEK 574
|
|
| FDH_beta_like |
cd16366 |
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ... |
25-72 |
1.03e-05 |
|
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: 45.85 E-value: 1.03e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 398365537 25 CKRSCPvvkTGklCIEVTPTSKIAFISEiLCIGCGICVKKCPFDAIQI 72
Cdd:cd16366 78 CLAACP---TG--AIIRTETGTVVVDPE-TCIGCGYCVNACPFDIPRF 119
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
101-285 |
1.04e-05 |
|
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: 46.81 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDPPEWQeiikyfrgselqnyftkMLEDDIKAIIK--PQYV--- 173
Cdd:cd03245 28 RAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSvlLDGTDIRQ-----------------LDPADLRRNIGyvPQDVtlf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 174 -----DNIprAIKGPVQKVGELLK-LRMEKSPEDVKRYIKILQLEnVLKRDiEKLSGGELQRFAIGMSCVQEADVYMFDE 247
Cdd:cd03245 91 ygtlrDNI--TLGAPLADDERILRaAELAGVTDFVNKHPNGLDLQ-IGERG-RGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 398365537 248 PSSYLD------VKQRLNAaqiirslLAPTKYVICVEHDLSVLD 285
Cdd:cd03245 167 PTSAMDmnseerLKERLRQ-------LLGDKTLIIITHRPSLLD 203
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
48-74 |
1.07e-05 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 43.57 E-value: 1.07e-05
10 20
....*....|....*....|....*..
gi 398365537 48 AFISEILCIGCGICVKKCPFDAIQIIN 74
Cdd:COG2768 6 PYVDEEKCIGCGACVKVCPVGAISIED 32
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
101-295 |
1.08e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.09 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNL--GRFDdppewqeiikyFRGSELQNyftkmLEDDIKAiikpqyVDNIPR 178
Cdd:PRK09580 25 RPGEVHAIMGPNGSGKSTLSATLAGREDYEVtgGTVE-----------FKGKDLLE-----LSPEDRA------GEGIFM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 179 AIKGPVQKVGELLKLRMEKSPEDVKRY------------------IKILQL-ENVLKRDI-EKLSGGELQRFAIGMSCVQ 238
Cdd:PRK09580 83 AFQYPVEIPGVSNQFFLQTALNAVRSYrgqepldrfdfqdlmeekIALLKMpEDLLTRSVnVGFSGGEKKRNDILQMAVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 239 EADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLS-DFVCIIY 295
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLY 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
359-501 |
1.09e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 46.91 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 359 LKKTQGDFV------LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ--------DIPKLNVSMKPQKIap 424
Cdd:COG1126 7 LHKSFGDLEvlkgisLDVEKGE-----VVVIIGPSGSGKSTLLRCINLLEEPDSGTitvdgedlTDSKKDINKLRRKV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 425 kfpGTVRQLF--F-------------KKIRG-----------QFLnpqfqtDVVkplRIDDIIDQEVQHLSGGELQRVAI 478
Cdd:COG1126 80 ---GMVFQQFnlFphltvlenvtlapIKVKKmskaeaeeramELL------ERV---GLADKADAYPAQLSGGQQQRVAI 147
|
170 180
....*....|....*....|....
gi 398365537 479 VLALGIPADIYLIDEP-SAyLDSE 501
Cdd:COG1126 148 ARALAMEPKVMLFDEPtSA-LDPE 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
385-501 |
1.10e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 385 GENGTGKTTLIKLLAGALKPDEGQDI--PKLNVSMKPQKiaPKF-PG-TVRQLF-------------FKKIRGQFLNPQF 447
Cdd:PRK11819 40 GLNGAGKSTLLRIMAGVDKEFEGEARpaPGIKVGYLPQE--PQLdPEkTVRENVeegvaevkaaldrFNEIYAAYAEPDA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 448 QTDVV--KPLRIDDII------------------------DQEVQHLSGGELQRVAIV-LALGIPaDIYLIDEPSAYLDS 500
Cdd:PRK11819 118 DFDALaaEQGELQEIIdaadawdldsqleiamdalrcppwDAKVTKLSGGERRRVALCrLLLEKP-DMLLLDEPTNHLDA 196
|
.
gi 398365537 501 E 501
Cdd:PRK11819 197 E 197
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
380-543 |
1.14e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.79 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 380 ILVMMGENGTGKTTLIKLLAGALKPDEGQDIPKLNVSMKPQKIAPKFPGTVRQLFFkkirGQFLNPQFQTDVVKPLRI-D 458
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILF----GKALNEKYYQQVLEACALlP 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 459 DI----------IDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSE-QRIICSKVIRRFILHNKKTAFIVEHD 527
Cdd:TIGR00957 742 DLeilpsgdrteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPEGVLKNKTRILVTHG 821
|
170
....*....|....*...
gi 398365537 528 FimaTYL--ADKVIVFEG 543
Cdd:TIGR00957 822 I---SYLpqVDVIIVMSG 836
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
83-294 |
1.14e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 47.36 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 83 VTHRYSA----NSFKLHrLPTprpGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikyFRGS----ELQN 154
Cdd:PRK11247 18 VSKRYGErtvlNQLDLH-IPA---GQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------------LAGTaplaEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 155 YfTKMLEDDIKAIIKPQYVDNIPRAIKGpvqkvgellKLRmekspEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGM 234
Cdd:PRK11247 82 D-TRLMFQDARLLPWKKVIDNVGLGLKG---------QWR-----DAALQALAAVGLADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 235 SCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKY-VICVEHDLSVLDYLSDFVCII 294
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFtVLLVTHDVSEAVAMADRVLLI 207
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
374-541 |
1.15e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.77 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 374 EFSDSEILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNVSMKPQKIAPKFpgTVRQLFFKKIRG------- 440
Cdd:PRK13651 29 EINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifKDEKNKKKTKEKEKVLEKL--VIQKTRFKKIKKikeirrr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 441 -----QFLNPQ-FQTDVVKplridDII---------DQEVQ----------------------HLSGGELQRVAIVLALG 483
Cdd:PRK13651 107 vgvvfQFAEYQlFEQTIEK-----DIIfgpvsmgvsKEEAKkraakyielvgldesylqrspfELSGGQKRRVALAGILA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 484 IPADIYLIDEPSAYLDSEQRIICSKVIRRfiLH-NKKTAFIVEHDFIMATYLADKVIVF 541
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDN--LNkQGKTIILVTHDLDNVLEWTKRTIFF 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
383-541 |
1.16e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 383 MMGENGTGKTTLIKLLAGALKPDEGQdipkLNVSMKPQKIA--------------------PKFpgTVRQ-LFFKKI--R 439
Cdd:PRK11288 35 LMGENGAGKSTLLKILSGNYQPDAGS----ILIDGQEMRFAsttaalaagvaiiyqelhlvPEM--TVAEnLYLGQLphK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 440 GQFLN-PQFQTDVVKPL-RIDDIIDQE--VQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRfiL 515
Cdd:PRK11288 109 GGIVNrRLLNYEAREQLeHLGVDIDPDtpLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRE--L 186
|
170 180
....*....|....*....|....*....
gi 398365537 516 HNKKTAFI-VEH--DFIMAtyLADKVIVF 541
Cdd:PRK11288 187 RAEGRVILyVSHrmEEIFA--LCDAITVF 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
102-295 |
1.17e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAgkqkpnlgRFDDPPEWQEIIKYFRGSELQNYFTKMLEDDIKAIIKPQYVDNIPR--- 178
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALL--------RLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPRqtv 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 179 --AIKGPV------------QKVGELLKlRMEKSPEDVKRYikilqlenvlkrdIEKLSGGELQRFAIGMSCVQEADVYM 244
Cdd:PRK10261 421 gdSIMEPLrvhgllpgkaaaARVAWLLE-RVGLLPEHAWRY-------------PHEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 245 FDEPSSYLDVKQRlnaAQIIRSLLAPTKYV----ICVEHDLSVLDYLSDFVCIIY 295
Cdd:PRK10261 487 ADEAVSALDVSIR---GQIINLLLDLQRDFgiayLFISHDMAVVERISHRVAVMY 538
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
368-539 |
1.25e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 47.31 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKpdeGQDIPKLNVSMKPQKI--APKFPGTVRQL------------ 433
Cdd:PRK09984 25 LNIHHGE-----MVALLGPSGSGKSTLLRHLSGLIT---GDKSAGSHIELLGRTVqrEGRLARDIRKSrantgyifqqfn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 434 --------------------FFKKIRGQFLNPQFQTDVVKPLRID--DIIDQEVQHLSGGELQRVAIVLALGIPADIYLI 491
Cdd:PRK09984 97 lvnrlsvlenvligalgstpFWRTCFSWFTREQKQRALQALTRVGmvHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365537 492 DEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVI 539
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIV 224
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
8-74 |
1.26e-05 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 47.02 E-value: 1.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 8 IAIVSADKCKPKKCRQECKRSCPVVKTGKLCIEVTPTSKIAFISEILCIGCGICVKKCPFDAIQIIN 74
Cdd:COG1145 137 AALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKD 203
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
101-294 |
1.35e-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: 46.39 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKP---------NlGRFDDPPEWQEIIKYFRgselqnyftkmlEDDIkaiIKPQ 171
Cdd:cd03213 33 KPGELTAIMGPSGAGKSTLLNALAGRRTGlgvsgevliN-GRPLDKRSFRKIIGYVP------------QDDI---LHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 172 yvdnipraikgpvQKVGELL----KLRmekspedvkryikilqlenvlkrdieKLSGGELQRFAIGMSCVQEADVYMFDE 247
Cdd:cd03213 97 -------------LTVRETLmfaaKLR--------------------------GLSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365537 248 PSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDY-LSDFVCII 294
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFeLFDKLLLL 185
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
373-500 |
1.42e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.12 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 373 GEFSDSEILVMMGENGTGKTTLIKLLAGALKPD-EGQDIPKLN-VSMKPQKIApKFPGTVRQ--LFFKK--------IRG 440
Cdd:TIGR00955 46 GVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvKGSGSVLLNgMPIDAKEMR-AISAYVQQddLFIPTltvrehlmFQA 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 441 QFLNPQFQTDVVKPLRIDDIIDQ---------------EVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDS 500
Cdd:TIGR00955 125 HLRMPRRVTKKEKRERVDEVLQAlglrkcantrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
101-295 |
1.45e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.41 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNlGRFDDPPEwqeiikyFRGSELQNY----FTKMLEDDIKAIIKPqyvdni 176
Cdd:PRK09473 40 RAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIGGSAT-------FNGREILNLpekeLNKLRAEQISMIFQD------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 177 PRAIKGPVQKVG----ELLKL--RMEKSP---EDVKRY--IKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMF 245
Cdd:PRK09473 106 PMTSLNPYMRVGeqlmEVLMLhkGMSKAEafeESVRMLdaVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 246 DEPSSYLDVKQRlnaAQIIrSLLAPTKY-----VICVEHDLSVLDYLSDFVCIIY 295
Cdd:PRK09473 186 DEPTTALDVTVQ---AQIM-TLLNELKRefntaIIMITHDLGVVAGICDKVLVMY 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
102-279 |
1.50e-05 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 46.20 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLG--RFDDPP------EWQEIIKYFRGSelqnyftkmleDDIKAIIKPqyV 173
Cdd:TIGR01189 25 AGEALQVTGPNGIGKTTLLRILAGLLRPDSGevRWNGTPlaeqrdEPHENILYLGHL-----------PGLKPELSA--L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 174 DNIP--RAIKGPVQkvgellklrmeKSPEDVKRYIKILQLENVLKRdieKLSGGELQRFAIGMSCVQEADVYMFDEPSSY 251
Cdd:TIGR01189 92 ENLHfwAAIHGGAQ-----------RTIEDALAAVGLTGFEDLPAA---QLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*...
gi 398365537 252 LDVKQRLNAAQIIRSLLAPTKYVICVEH 279
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
368-543 |
1.57e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.01 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQdipklnVSMKPQKIAPKFPGTVRQ---LFFKKIRGQFLN 444
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGK------VKIDGELLTAENVWNLRRkigMVFQNPDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 445 PQFQTDVVKPL------------RID---------DIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQR 503
Cdd:PRK13642 97 ATVEDDVAFGMenqgipreemikRVDeallavnmlDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398365537 504 IICSKVIRRFILHNKKTAFIVEHDFIMATYlADKVIVFEG 543
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKA 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
365-542 |
1.61e-05 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 46.46 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 365 DFVLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEGQ------DIPKLNVSMKPQKIAPK------FPGTVRQ 432
Cdd:cd03251 20 DISLDIPAGET-----VALVGPSGSGKSTLVNLIPRFYDVDSGRilidghDVRDYTLASLRRQIGLVsqdvflFNDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 433 lffkKIRgqFLNPQF-QTDVVKPLRI--------------DDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAY 497
Cdd:cd03251 95 ----NIA--YGRPGAtREEVEEAARAanahefimelpegyDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 398365537 498 LDSEQRIICSKVIRRfiLHNKKTAFIVEHDF--IMAtylADKVIVFE 542
Cdd:cd03251 169 LDTESERLVQAALER--LMKNRTTFVIAHRLstIEN---ADRIVVLE 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
364-541 |
1.86e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.63 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 364 GDFVLNVEEGEFSDSEILVMMGENGTGKTTLIK-----------------LLAGALKPDEGQDIPKLN--VSMKPQKIAP 424
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRtlnrmndkvsgyrysgdVLLGGRSIFNYRDVLEFRrrVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 425 kFPGTVRQLFFKKIRGQFLNPQFQTDVVKPLR---------IDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPS 495
Cdd:PRK14271 113 -FPMSIMDNVLAGVRAHKLVPRKEFRGVAQARltevglwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365537 496 AYLDSEQRIICSKVIRRfiLHNKKTAFIVEHDFIMATYLADKVIVF 541
Cdd:PRK14271 192 SALDPTTTEKIEEFIRS--LADRLTVIIVTHNLAQAARISDRAALF 235
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
102-288 |
1.87e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.35 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLGrfddppewqEIIkyFRG-----------SELQNY-------FTKMLED- 162
Cdd:PRK11629 34 EGEMMAIVGSSGSGKSTLLHLLGGLDTPTSG---------DVI--FNGqpmsklssaakAELRNQklgfiyqFHHLLPDf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 163 -DIKAIIKPQYVDNIPRAikgpvqkvgellklrmeKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEAD 241
Cdd:PRK11629 103 tALENVAMPLLIGKKKPA-----------------EINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398365537 242 VYMFDEPSSYLDvkQRlNAAQIIRSL-----LAPTKYVIcVEHDLSVLDYLS 288
Cdd:PRK11629 166 LVLADEPTGNLD--AR-NADSIFQLLgelnrLQGTAFLV-VTHDLQLAKRMS 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
101-543 |
1.87e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFD---------DPPE---------WQEIIKYFRGSELQNYFTKMLed 162
Cdd:PRK09700 29 YPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITinninynklDHKLaaqlgigiiYQELSVIDELTVLENLYIGRH-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 163 dikaiikpqyvdnipraikgPVQKVGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADV 242
Cdd:PRK09700 107 --------------------LTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 243 YMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIYGVPSVYGVVTLPASVREGINIFLDghi 322
Cdd:PRK09700 167 IIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVG--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 323 paenlrfrtEALQFRIADATEDLQNDSASRAFSYPSLKKTQGDFVLNVeEGEFSDSEILVMMGENGTGKTTLIKLLAGAL 402
Cdd:PRK09700 244 ---------RELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVRDI-SFSVCRGEILGFAGLVGSGRTELMNCLFGVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 403 KPDEGQdipklnVSMKPQKIAPKFP------------------------------GTVRQLFFKKIRGQ--FLNPQFQTD 450
Cdd:PRK09700 314 KRAGGE------IRLNGKDISPRSPldavkkgmayitesrrdngffpnfsiaqnmAISRSLKDGGYKGAmgLFHEVDEQR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 451 VVKPLRID-----DIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRfILHNKKTAFIVE 525
Cdd:PRK09700 388 TAENQRELlalkcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDGKVILMVS 466
|
490 500
....*....|....*....|.
gi 398365537 526 HDF--IMAtyLADKVIVF-EG 543
Cdd:PRK09700 467 SELpeIIT--VCDRIAVFcEG 485
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
4-76 |
1.98e-05 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 46.85 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 4 KNSRIAIVSADKCKPKKCRQECKRSCpvvkTG-KLCIEVTPTSKIA---FISEI---LCIGCGICVKKCPFDAIQIINLP 76
Cdd:PRK07118 190 KSARVFVACNSKDKGKAVKKVCEVGC----IGcGKCVKACPAGAITmenNLAVIdqeKCTSCGKCVEKCPTKAIRILNKP 265
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
79-264 |
2.12e-05 |
|
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: 47.02 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 79 LEAHVTHRYSanSFKLH-RLPTPRPGqVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDPPeWQeiikyfrgselqny 155
Cdd:COG4148 3 LEVDFRLRRG--GFTLDvDFTLPGRG-VTALFGPSGSGKTTLLRAIAGLERPDSGRirLGGEV-LQ-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 156 ftkmleDDIKAIikpqyvdNIP---RAIkGPV-Q--------KVGELLKLRMEKSPEDVKRY-----IKILQLENVLKRD 218
Cdd:COG4148 65 ------DSARGI-------FLPphrRRI-GYVfQearlfphlSVRGNLLYGRKRAPRAERRIsfdevVELLGIGHLLDRR 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365537 219 IEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRlnaAQII 264
Cdd:COG4148 131 PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK---AEIL 173
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
50-71 |
2.22e-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: 2.22e-05
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
350-536 |
2.27e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 350 ASRAFSY-PSLKKTQgdfvLNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG-----QDipkLNVSMKPQKIA 423
Cdd:PRK11147 9 AWLSFSDaPLLDNAE----LHIEDNER-----VCLVGRNGAGKSTLMKILNGEVLLDDGriiyeQD---LIVARLQQDPP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 424 PKFPGTV---------------------RQLFFKKIRGQFLNP--------------QFQT---DVVKPLRIDDiiDQEV 465
Cdd:PRK11147 77 RNVEGTVydfvaegieeqaeylkryhdiSHLVETDPSEKNLNElaklqeqldhhnlwQLENrinEVLAQLGLDP--DAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 466 QHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDseqrIICSKVIRRFILHNKKTAFIVEHD--FI--MATYLAD 536
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDrsFIrnMATRIVD 225
|
|
| DMSOR_beta_like |
cd16367 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
27-73 |
2.62e-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: 319889 [Multi-domain] Cd Length: 138 Bit Score: 44.22 E-value: 2.62e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 398365537 27 RSCpvvkTGKLCIEVTPTSKIA-------FISEIlCIGCGICVKKCPFDAIQII 73
Cdd:cd16367 58 RHC----VDPVCMIGCPTGAIHrddggevVISDA-CCGCGNCASACPYGAIQMV 106
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
3-74 |
3.56e-05 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 46.56 E-value: 3.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365537 3 DKNSRIAIVSADKCKPKKCRQECKRSCPVVKTGKLCIEVTPTSKIAFISEILCIGCGICVKKCPFDAIQIIN 74
Cdd:COG4624 41 HVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDD 112
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
8-73 |
3.56e-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: 319895 [Multi-domain] Cd Length: 154 Bit Score: 44.17 E-value: 3.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365537 8 IAIVSADKC----KPKKCRQeCKRSCPvvkTGKLCIEVTPTSKIAFISEILCIGCGICVKKCP---FDAIQII 73
Cdd:cd16373 85 VAVIDKDRClawqGGTDCGV-CVEACP---TEAIAIVLEDDVLRPVVDEDKCVGCGLCEYVCPvepPKAIVVE 153
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
83-325 |
3.57e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 45.52 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 83 VTHRYsaNSFKLHRLPTPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDD------PPE-------WQEiikyf 147
Cdd:COG3840 7 LTYRY--GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRilWNGqdltalPPAerpvsmlFQE----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 148 rgselQNYFTKM-LEDDIKAIIKPQyvdnipraikgpvqkvgelLKLrmekSPEDVKRYIKILQ---LENVLKRDIEKLS 223
Cdd:COG3840 80 -----NNLFPHLtVAQNIGLGLRPG-------------------LKL----TAEQRAQVEQALErvgLAGLLDRLPGQLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 224 GGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKY-VICVEHDLSVLDYLSDFVCIIYGvpsvyG 302
Cdd:COG3840 132 GGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLtVLMVTHDPEDAARIADRVLLVAD-----G 206
|
250 260
....*....|....*....|...
gi 398365537 303 VVTLPASVREginiFLDGHIPAE 325
Cdd:COG3840 207 RIAADGPTAA----LLDGEPPPA 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
91-291 |
3.92e-05 |
|
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: 46.60 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 91 SFKLhrlptpRPGQVLGLVGTNGIGKST-ALKIL-----AGKQkpnlgRFDDppewQEIIKyFRGSELQNYFTKMleddi 164
Cdd:COG4172 306 SLTL------RRGETLGLVGESGSGKSTlGLALLrlipsEGEI-----RFDG----QDLDG-LSRRALRPLRRRM----- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 165 kaiikpQYV--D-----NiPRAIKGpvQKVGE-LLKLRMEKSPEDV-KRYIKILQ----LENVLKRDIEKLSGGELQRFA 231
Cdd:COG4172 365 ------QVVfqDpfgslS-PRMTVG--QIIAEgLRVHGPGLSAAERrARVAEALEevglDPAARHRYPHEFSGGQRQRIA 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 232 IGMSCVQEADVYMFDEPSSYLDVKQRlnaAQII---RSL-----LAptkYvICVEHDLSVLDYLSDFV 291
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDVSVQ---AQILdllRDLqrehgLA---Y-LFISHDLAVVRALAHRV 496
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
221-499 |
3.96e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 221 KLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRlnaAQIIrSLLAPTKY-----VICVEHDLSVLDYLSDFVCIIY 295
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQ---AQIL-QLLRELQQelnmgLLFITHNLSIVRKLADRVAVMQ 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 296 G---VPSVYGVVTLPASVREGINIFLDghipAENlRFRTEALQfriADATEDLQNDSASRAFSYPS--LKKTQG-DFVLN 369
Cdd:PRK15134 232 NgrcVEQNRAATLFSAPTHPYTQKLLN----SEP-SGDPVPLP---EPASPLLDVEQLQVAFPIRKgiLKRTVDhNVVVK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 370 VEEGEFSDSEILVMMGENGTGKTT----LIKLLA--GALKPDeGQDIPKLNvsmkPQKIAPkfpgtVR---QLFFKKIRG 440
Cdd:PRK15134 304 NISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFD-GQPLHNLN----RRQLLP-----VRhriQVVFQDPNS 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 441 QfLNPQF-------------QTDVVKPLRIDDII--------DQEVQH-----LSGGELQRVAIVLALGIPADIYLIDEP 494
Cdd:PRK15134 374 S-LNPRLnvlqiieeglrvhQPTLSAAQREQQVIavmeevglDPETRHrypaeFSGGQRQRIAIARALILKPSLIILDEP 452
|
....*
gi 398365537 495 SAYLD 499
Cdd:PRK15134 453 TSSLD 457
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
354-543 |
4.11e-05 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 45.15 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPSLKKTQgdfVLNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQDIpklnVSMKP----------QKIA 423
Cdd:cd03248 19 FAYPTRPDTL---VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVL----LDGKPisqyehkylhSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 424 pkFPGTVRQLFFKKIRGQ--FLNPQFQTDVVK---------------PLRIDDIIDQEVQHLSGGELQRVAIVLALGIPA 486
Cdd:cd03248 92 --LVGQEPVLFARSLQDNiaYGLQSCSFECVKeaaqkahahsfiselASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 487 DIYLIDEPSAYLDSEQRIICSKVIRRFilHNKKTAFIVEHDfIMATYLADKVIVFEG 543
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDW--PERRTVLVIAHR-LSTVERADQILVLDG 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
368-505 |
4.57e-05 |
|
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: 45.12 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 368 LNVEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLN----VSMKPQKIapkfpGTVRQLFfkk 437
Cdd:COG4181 33 LEVEAGES-----VAIVGASGSGKSTLLGLLAGLDRPTSGtvrlagQDLFALDedarARLRARHV-----GFVFQSF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 438 irgQFL-------NpqfqtdVVKPLRIDDIID---------QEV----------QHLSGGELQRVAIVLALGIPADIYLI 491
Cdd:COG4181 100 ---QLLptltaleN------VMLPLELAGRRDarararallERVglghrldhypAQLSGGEQQRVALARAFATEPAILFA 170
|
170
....*....|....*.
gi 398365537 492 DEPSAYLDSE--QRII 505
Cdd:COG4181 171 DEPTGNLDAAtgEQII 186
|
|
| IOR_alpha |
TIGR03336 |
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin ... |
10-70 |
4.85e-05 |
|
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin oxidoreductase (IOR) is an alpha 2/beta 2 tetramer related to ketoacid oxidoreductases for pyruvate (1.2.7.1, POR), 2-ketoglutarate (1.2.7.3, KOR), and 2-oxoisovalerate (1.2.7.7, VOR). These multi-subunit enzymes typically are found in anaerobes and are inactiviated by oxygen. IOR in Pyrococcus acts in fermentation of all three aromatic amino acids, following removal of the amino group by transamination. In Methanococcus maripaludis, by contrast, IOR acts in the opposite direction, in pathways of amino acid biosynthesis from phenylacetate, indoleacetate, and p-hydroxyphenylacetate. In M. maripaludis and many other species, iorA and iorB are found next to an apparent phenylacetate-CoA ligase.
Pssm-ID: 274526 [Multi-domain] Cd Length: 595 Bit Score: 46.26 E-value: 4.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365537 10 IVSADKCKpkKCRQeCKRS--CPVVKTGKLCIEVTPtskiafiseiLCIGCGICVKKCPFDAI 70
Cdd:TIGR03336 546 KVDQDKCI--GCKK-CIKElgCPAIEPEDKEAVIDP----------LCTGCGVCAQICPFDAI 595
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
43-70 |
4.96e-05 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 44.55 E-value: 4.96e-05
10 20
....*....|....*....|....*...
gi 398365537 43 PTSKIAFISEILCIGCGICVKKCPFDAI 70
Cdd:PRK05113 104 PARKVAFIDEDNCIGCTKCIQACPVDAI 131
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
354-564 |
4.98e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 46.36 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPslkkTQGDFVLN-----VEEGEFsdseiLVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLN-------V 415
Cdd:PRK11160 346 FTYP----DQPQPVLKglslqIKAGEK-----VALLGRTGCGKSTLLQLLTRAWDPQQGeillngQPIADYSeaalrqaI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 416 SMKPQKIApKFPGTVRQ-LffkkirgQFLNPQFQ----TDVVKPLRIDDIIDQEV----------QHLSGGELQRVAIVL 480
Cdd:PRK11160 417 SVVSQRVH-LFSATLRDnL-------LLAAPNASdealIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 481 ALGIPADIYLIDEPSAYLDS--EQRIIcsKVIRRFILHnkKTAFIVEHDfimATYLA--DKVIVFEG--IPSKNAHarap 554
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAetERQIL--ELLAEHAQN--KTVLMITHR---LTGLEqfDRICVMDNgqIIEQGTH---- 557
|
250
....*....|
gi 398365537 555 ESLLTGCNRF 564
Cdd:PRK11160 558 QELLAQQGRY 567
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
215-290 |
5.13e-05 |
|
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: 44.94 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 215 LKRDIEKLSGGELQRFA----IGMSCVqeADVYMFDEPSSYL---DvKQRLNAAqiIRSLLAPTKYVICVEHDLSVL--- 284
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRlatqIGSGLT--GVLYVLDEPSIGLhprD-NDRLIET--LKRLRDLGNTVLVVEHDEDTIraa 205
|
....*.
gi 398365537 285 DYLSDF 290
Cdd:cd03270 206 DHVIDI 211
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
47-70 |
5.61e-05 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 45.17 E-value: 5.61e-05
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
101-284 |
5.69e-05 |
|
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: 44.13 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikyfrgselqnyftkmleddikaiikpqYVDNIP--- 177
Cdd:cd03246 26 EPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-------------------------------------RLDGADisq 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 178 --RAIKGpvQKVGELlklrmeksPEDVKRYIKILqLENVlkrdiekLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVK 255
Cdd:cd03246 69 wdPNELG--DHVGYL--------PQDDELFSGSI-AENI-------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190
....*....|....*....|....*....|.
gi 398365537 256 --QRLNAAqiIRSLLAPTKYVICVEHDLSVL 284
Cdd:cd03246 131 geRALNQA--IAALKAAGATRIVIAHRPETL 159
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
101-294 |
6.78e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQkPNlGRFDDppewqEIikYFRGSELQNYFTKMLEDDIKAIIKPQ--YVDNIpr 178
Cdd:PRK13549 29 RAGEIVSLCGENGAGKSTLMKVLSGVY-PH-GTYEG-----EI--IFEGEELQASNIRDTERAGIAIIHQElaLVKEL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 179 aikgpvqKVGELLKLRMEKSP----EDVKRYIKILQLENVLKRDI------EKLSGGELQRFAIGMSCVQEADVYMFDEP 248
Cdd:PRK13549 98 -------SVLENIFLGNEITPggimDYDAMYLRAQKLLAQLKLDInpatpvGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 398365537 249 SSYL---DVKQRLNaaqIIRSLLAptKYVICV--EHDLSVLDYLSDFVCII 294
Cdd:PRK13549 171 TASLtesETAVLLD---IIRDLKA--HGIACIyiSHKLNEVKAISDTICVI 216
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
99-280 |
6.93e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.70 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 99 TPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikYFRGselqnyftkmleDDIKAIIKPQYVDNIPR 178
Cdd:PRK10247 29 SLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL-----------LFEG------------EDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 179 AIKGPV---QKVGELLKL--RMEKSPEDVKRYIKILQL----ENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPS 249
Cdd:PRK10247 86 CAQTPTlfgDTVYDNLIFpwQIRNQQPDPAIFLDDLERfalpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190
....*....|....*....|....*....|..
gi 398365537 250 SYLDVKQRLNAAQIIRSLLAPTKY-VICVEHD 280
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIaVLWVTHD 197
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
379-408 |
7.63e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.02 E-value: 7.63e-05
10 20 30
....*....|....*....|....*....|
gi 398365537 379 EILVMMGENGTGKTTLIKLLAGALKPDEGQ 408
Cdd:PRK13538 28 ELVQIEGPNGAGKTSLLRILAGLARPDAGE 57
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
462-539 |
7.82e-05 |
|
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: 44.56 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 462 DQEVQHLSGGELQRVAIVLALGIPAD--IYLIDEPSAYL---DSEQRIICSKVIRRfiLHNkkTAFIVEHD--FIMAtyl 534
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLhprDNDRLIETLKRLRD--LGN--TVLVVEHDedTIRA--- 204
|
....*
gi 398365537 535 ADKVI 539
Cdd:cd03270 205 ADHVI 209
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
457-541 |
7.90e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.77 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 457 IDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSeqriICSKVIRRFI--LHNKKTAFIVEHDFIMATYL 534
Cdd:PRK14243 141 VKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP----ISTLRIEELMheLKEQYTIIIVTHNMQQAARV 216
|
....*..
gi 398365537 535 ADKVIVF 541
Cdd:PRK14243 217 SDMTAFF 223
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
108-295 |
8.77e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.99 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 108 LVGTNGIGKSTALK----ILAGKQKPNLGRFD------DPPEWQEIIKYFrGSELQNYFTKMLEDDIKAIIKPQYvDNIP 177
Cdd:COG3593 28 LVGENNSGKSSILEalrlLLGPSSSRKFDEEDfylgddPDLPEIEIELTF-GSLLSRLLRLLLKEEDKEELEEAL-EELN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 178 RAIKGPVQKVGELLK-----------LRMEKSPEDVKRYIKILQL--ENVLKRDIEKLSGGELQRFAIGMSCV------- 237
Cdd:COG3593 106 EELKEALKALNELLSeylkelldgldLELELSLDELEDLLKSLSLriEDGKELPLDRLGSGFQRLILLALLSAlaelkra 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 238 QEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDyLSDFVCIIY 295
Cdd:COG3593 186 PANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLS-EVPLENIRR 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
354-500 |
8.92e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.74 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 354 FSYPS--LKKTQGDFVLNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQDIP-KLNVSMKPQkIAPKFPGTV 430
Cdd:PLN03232 622 FSWDSktSKPTLSDINLEIPVGS-----LVAIVGGTGEGKTSLISAMLGELSHAETSSVViRGSVAYVPQ-VSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 431 RQ--LF---------FKKIRGQFLnpQFQTDVVKPLRIDDIIDQEVqHLSGGELQRVAIVLALGIPADIYLIDEPSAYLD 499
Cdd:PLN03232 696 REniLFgsdfeseryWRAIDVTAL--QHDLDLLPGRDLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
.
gi 398365537 500 S 500
Cdd:PLN03232 773 A 773
|
|
| DMSOR_beta_like |
cd16374 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
18-72 |
9.32e-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: 319896 [Multi-domain] Cd Length: 139 Bit Score: 42.65 E-value: 9.32e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365537 18 PKKCRQeCKRSCpvvktgklCIEVTPTSKI-------AFISEILCIGCGICVKKCPFDAIQI 72
Cdd:cd16374 40 PVRCRH-CEDAP--------CMEVCPTGAIyrdedgaVLVDPDKCIGCGMCAMACPFGVPRF 92
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
55-73 |
9.90e-05 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 40.50 E-value: 9.90e-05
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
55-77 |
1.03e-04 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 40.23 E-value: 1.03e-04
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-538 |
1.18e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 44.27 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 341 ATEDLQNdsASRAFSYPSLKKTQGDFVLNVeegefSDSEILVMMGENGTGKTTLIKLLA-------GALKPDE-----GQ 408
Cdd:PRK14246 6 SAEDVFN--ISRLYLYINDKAILKDITIKI-----PNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGkvlyfGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 409 DIPKLN-------VSMKPQKIAPkFP---------------GTVRQLFFKKIRGQFLNpqfQTDVVKplRIDDIIDQEVQ 466
Cdd:PRK14246 79 DIFQIDaiklrkeVGMVFQQPNP-FPhlsiydniayplkshGIKEKREIKKIVEECLR---KVGLWK--EVYDRLNSPAS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 467 HLSGGELQRVAIVLALGIPADIYLIDEPSAYLDseqrIICSKVIRRFI--LHNKKTAFIVEHDFIMATYLADKV 538
Cdd:PRK14246 153 QLSGGQQQRLTIARALALKPKVLLMDEPTSMID----IVNSQAIEKLIteLKNEIAIVIVSHNPQQVARVADYV 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
103-296 |
1.42e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 43.91 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 103 GQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDPPewqeiIKYFRGSEL----------QN----YFTKMLEDDIKA 166
Cdd:PRK13639 28 GEMVALLGPNGAGKSTLFLHFNGILKPTSGEvlIKGEP-----IKYDKKSLLevrktvgivfQNpddqLFAPTVEEDVAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 167 iikpqyvdnipraikGPVQkvgelLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFD 246
Cdd:PRK13639 103 ---------------GPLN-----LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398365537 247 EPSSYLDvkqRLNAAQIIRSLLAPTK---YVICVEHDLSVLDYLSDFVCIIYG 296
Cdd:PRK13639 163 EPTSGLD---PMGASQIMKLLYDLNKegiTIIISTHDVDLVPVYADKVYVMSD 212
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
21-75 |
1.51e-04 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 42.23 E-value: 1.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 21 CRQeCKRSCPVVktgklCIEVTPTSKIAFISEI---LCIGCGICVKKCPFDAIQIINL 75
Cdd:cd10564 88 CRS-CQDACPTQ-----AIRFRPRLGGIALPELdadACTGCGACVSVCPVGAITLTPL 139
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
91-296 |
1.63e-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: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 91 SFKLHRlptprpGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFddppewqeiikyfrgselqnyftkmleddikaiikp 170
Cdd:cd03215 20 SFEVRA------GEIVGIAGLVGNGQTELAEALFGLRPPASGEI------------------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 171 qYVDNIPRAIKGPvqkvGELLKLRMEKSPEDVKRYIKILQL---ENVLKRDIekLSGGELQRFAIGMSCVQEADVYMFDE 247
Cdd:cd03215 58 -TLDGKPVTRRSP----RDAIRAGIAYVPEDRKREGLVLDLsvaENIALSSL--LSGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398365537 248 PSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIYG 296
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYE 179
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
104-295 |
1.85e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.84 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 104 QVLGLVGTNGIGKSTALKILAG-----KQKPNLGRFDDPPEWQEIIKyfrgselqnyfTKMLEDDIKAIIK-PQYV---D 174
Cdd:PRK13645 38 KVTCVIGTTGSGKSTMIQLTNGliiseTGQTIVGDYAIPANLKKIKE-----------VKRLRKEIGLVFQfPEYQlfqE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 175 NIPRAIK-GPVQkVGELLKLRMEKSPEdvkrYIKILQL-ENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYL 252
Cdd:PRK13645 107 TIEKDIAfGPVN-LGENKQEAYKKVPE----LLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398365537 253 DVK---------QRLNAAQiirsllapTKYVICVEHDLSVLDYLSDFVCIIY 295
Cdd:PRK13645 182 DPKgeedfinlfERLNKEY--------KKRIIMVTHNMDQVLRIADEVIVMH 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
101-294 |
1.85e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.53 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKS----TALKIL-AGKQKPNlGR--FDDPPEWQEIIkyfRG----SELQNyftkmleddikaiik 169
Cdd:PRK10418 27 QRGRVLALVGGSGSGKSltcaAALGILpAGVRQTA-GRvlLDGKPVAPCAL---RGrkiaTIMQN--------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 170 pqyvdniPRAIKGPVQKVG----ELLKLRmeKSPEDVKRYIKILQ---LEN---VLKRDIEKLSGGELQRFAIGMSCVQE 239
Cdd:PRK10418 88 -------PRSAFNPLHTMHtharETCLAL--GKPADDATLTAALEavgLENaarVLKLYPFEMSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 240 ADVYMFDEPSSYLDVkqrLNAAQIIrSLLAPTKY-----VICVEHDLSVLDYLSDFVCII 294
Cdd:PRK10418 159 APFIIADEPTTDLDV---VAQARIL-DLLESIVQkralgMLLVTHDMGVVARLADDVAVM 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
358-408 |
1.94e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 43.56 E-value: 1.94e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 358 SLKKTQGDFV------LNVEEGEfsdseILVMMGENGTGKTTLIKLLAGALKPDEGQ 408
Cdd:COG4152 6 GLTKRFGDKTavddvsFTVPKGE-----IFGLLGPNGAGKTTTIRIILGILAPDSGE 57
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
91-134 |
1.98e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 44.16 E-value: 1.98e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 398365537 91 SFKLhrlptPrPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF 134
Cdd:TIGR03719 342 SFKL-----P-PGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
54-74 |
2.01e-04 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 40.03 E-value: 2.01e-04
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
379-408 |
2.08e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 43.38 E-value: 2.08e-04
10 20 30
....*....|....*....|....*....|
gi 398365537 379 EILVMMGENGTGKTTLIKLLAGALKPDEGQ 408
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSARLAPDAGE 62
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
25-70 |
2.10e-04 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 39.46 E-value: 2.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 398365537 25 CKRSCPVvktgKLCIEVTPTSKIAF-ISEILCIGCGICVKKCPFDAI 70
Cdd:pfam13187 8 CVAACPA----GAIVPDLVGQTIRGdIAGLACIGCGACVDACPRGAI 50
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
40-70 |
2.13e-04 |
|
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]
Pssm-ID: 273887 [Multi-domain] Cd Length: 165 Bit Score: 42.09 E-value: 2.13e-04
10 20 30
....*....|....*....|....*....|.
gi 398365537 40 EVTPTSKIAFISEILCIGCGICVKKCPFDAI 70
Cdd:TIGR01944 100 GTIQPPMVALIDEDNCIGCTKCIQACPVDAI 130
|
|
| PorD_KorD |
TIGR02179 |
2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number ... |
10-73 |
2.25e-04 |
|
2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes a subfamily of delta subunits, representing mostly pyruvate, 2-ketoisovalerate, and 2-oxoglutarate specific enzymes. The delta subunit is the smallest and resembles ferredoxins.
Pssm-ID: 131234 [Multi-domain] Cd Length: 78 Bit Score: 40.01 E-value: 2.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 10 IVSADKCKpkKCRqECKRSCPvvktgKLCIEVTPTSKIAFISEiLCIGCGICVKKCPFDAIQII 73
Cdd:TIGR02179 21 VVDKEKCI--KCK-NCWLYCP-----EGAIQEDEGGFVGIDYD-YCKGCGICANVCPVKAIEMV 75
|
|
| FDH-O_like |
cd10560 |
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ... |
12-72 |
2.33e-04 |
|
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: 42.76 E-value: 2.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365537 12 SADKCKpkKCRQE-CKRSCPvvkTGklCIEVTPTSKIaFISEILCIGCGICVKKCPFDAIQI 72
Cdd:cd10560 74 MSDVCK--HCTDAgCLEACP---TG--AIFRTEFGTV-YIQPDICNGCGYCVAACPFGVIDR 127
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
466-548 |
2.71e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 466 QHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDfIMATYLADKVIVFEGiP 545
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR-IASIKRSDKIVVFNN-P 1434
|
...
gi 398365537 546 SKN 548
Cdd:PTZ00265 1435 DRT 1437
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
382-543 |
2.72e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 382 VMMGENGTGKTTLIKLLAGALKPDEGQDIPKLNVSMKPQKiAPKFPGTVRQ--LFFKKIRGQFLNP-----QFQTDVVK- 453
Cdd:PTZ00243 690 VVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQ-AWIMNATVRGniLFFDEEDAARLADavrvsQLEADLAQl 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 454 PLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEqriICSKVIRRFILHN--KKTAFIVEH----- 526
Cdd:PTZ00243 769 GGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH---VGERVVEECFLGAlaGKTRVLATHqvhvv 845
|
170 180
....*....|....*....|
gi 398365537 527 ---DFIMAtyLADKVIVFEG 543
Cdd:PTZ00243 846 praDYVVA--LGDGRVEFSG 863
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
105-295 |
2.97e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 43.11 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 105 VLGLVGTNGIGKSTALKILagkqKPNLGRFDDPPEWQEIIKYFRGSELQNYFTKMLEDDIKAIIKPQ------YVDNIPR 178
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVL----NRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNpfphlsIYDNIAY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 179 AIKGPVQKVGELLKLRMEKSPEDVKRYIKIlqlENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRL 258
Cdd:PRK14246 114 PLKSHGIKEKREIKKIVEECLRKVGLWKEV---YDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQ 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 398365537 259 NAAQIIRSLLAPTKYVIcVEHDLSVLDYLSDFVCIIY 295
Cdd:PRK14246 191 AIEKLITELKNEIAIVI-VSHNPQQVARVADYVAFLY 226
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
463-524 |
3.03e-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: 42.63 E-value: 3.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365537 463 QEVQHLSGGELQRVAIVLALGI----PADIYLIDEPSAYLDSEQRIICSKVIRRFilhNKKTAFIV 524
Cdd:cd03272 154 QEMQQLSGGQKSLVALALIFAIqkcdPAPFYLFDEIDAALDAQYRTAVANMIKEL---SDGAQFIT 216
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
6-73 |
3.12e-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: 319894 [Multi-domain] Cd Length: 125 Bit Score: 40.78 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 6 SRIAIVSA-DKCKPKKCRQ--ECKRSCP----------VVKTGK-------LCIEVTPTSKIAFISEIL----CIGCGIC 61
Cdd:cd16372 33 SCIRITETeGGYAINVCNQcgECIDVCPtgaitrdangVVMINKklcvgclMCVGFCPEGAMFKHEDYPepfkCIACGIC 112
|
90
....*....|..
gi 398365537 62 VKKCPFDAIQII 73
Cdd:cd16372 113 VKACPTGALELV 124
|
|
| FDH_b_like |
cd10562 |
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ... |
38-72 |
3.67e-04 |
|
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.
Pssm-ID: 319884 [Multi-domain] Cd Length: 161 Bit Score: 41.52 E-value: 3.67e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 398365537 38 CIEVTPT-------SKIAFISEILCIGCGICVKKCPFDAIQI 72
Cdd:cd10562 78 CVKVCPTgalykteNGAVVVDEDKCIGCGYCVAACPFDVPRY 119
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
77-254 |
4.04e-04 |
|
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: 42.54 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 77 TNLEAHVTHRYSANSFKLHRlptprpGQVLGLVGTNGIGKSTALKILAGKQKPNLGRfddppewqeiIKYFRGSELQNYF 156
Cdd:cd03291 43 SNLCLVGAPVLKNINLKIEK------GEMLAITGSTGSGKTSLLMLILGELEPSEGK----------IKHSGRISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 157 TKMLEDDIKaiikpqyvDNIPRAIKgpvqkvgellklrmekspEDVKRY---IKILQLENVLKRDIEK-----------L 222
Cdd:cd03291 107 SWIMPGTIK--------ENIIFGVS------------------YDEYRYksvVKACQLEEDITKFPEKdntvlgeggitL 160
|
170 180 190
....*....|....*....|....*....|..
gi 398365537 223 SGGELQRFAIGMSCVQEADVYMFDEPSSYLDV 254
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
1-72 |
4.87e-04 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 42.36 E-value: 4.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 1 MSDKNSRIAIVSADKCKpkKCRQeCKRSCPV---VKTGKlcievtptskiafISEILCIGCGICVKKCPFDAIQI 72
Cdd:COG0348 197 LSDLSTLRVRYDRGDCI--DCGL-CVKVCPMgidIRKGE-------------INQSECINCGRCIDACPKDAIRF 255
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
91-133 |
4.92e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 41.78 E-value: 4.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 398365537 91 SFKLhrlptpRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR 133
Cdd:PRK13539 22 SFTL------AAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGT 58
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
198-294 |
4.94e-04 |
|
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: 41.69 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 198 SPEDVKRYIKILQLeNVLKRDIEK---------------LSGGELQRFAIGMSCVQEADVYMFDEPSSYLD--VKQRLnA 260
Cdd:cd03250 90 KPFDEERYEKVIKA-CALEPDLEIlpdgdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDahVGRHI-F 167
|
90 100 110
....*....|....*....|....*....|....
gi 398365537 261 AQIIRSLLAPTKYVICVEHDLSVLDYlSDFVCII 294
Cdd:cd03250 168 ENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVL 200
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
82-133 |
5.48e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 42.71 E-value: 5.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 82 HVTHRYS---AN---SFKLhrlptpRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGR 133
Cdd:COG3845 10 GITKRFGgvvANddvSLTV------RPGEIHALLGENGAGKSTLMKILYGLYQPDSGE 61
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
55-74 |
5.93e-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: 41.77 E-value: 5.93e-04
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
467-538 |
5.95e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.14 E-value: 5.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365537 467 HLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSeqriICSKVIRRFILHNKK--TAFIVEHDFIMATYLADKV 538
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDP----VGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYV 218
|
|
| FDH-N |
cd10558 |
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ... |
38-68 |
6.05e-04 |
|
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups.
Pssm-ID: 319880 [Multi-domain] Cd Length: 208 Bit Score: 41.60 E-value: 6.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 398365537 38 CIEVTPTSK---------IAFISEiLCIGCGICVKKCPFD 68
Cdd:cd10558 78 CLKACPSPGaivqyangiVDFQSD-KCIGCGYCIKGCPFD 116
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
345-539 |
6.11e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 42.79 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 345 LQNDSASRafSYPSlkktqGDFVLNVEEG---EFSDSEILVMMGENGTGKTTLIKLLAGALKPDEG------QDIPKLNV 415
Cdd:PRK10535 5 LELKDIRR--SYPS-----GEEQVEVLKGislDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyrvagQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 416 SMKPQ-------------------------KIAPKFPGTVRQLffKKIRGQFLnpqfqtdvVKPLRIDDIIDQEVQHLSG 470
Cdd:PRK10535 78 DALAQlrrehfgfifqryhllshltaaqnvEVPAVYAGLERKQ--RLLRAQEL--------LQRLGLEDRVEYQPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365537 471 GELQRVAIVLALGIPADIYLIDEPSAYLDSEqriicSKVIRRFILHNKK----TAFIVEHDFIMATYlADKVI 539
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSH-----SGEEVMAILHQLRdrghTVIIVTHDPQVAAQ-AERVI 214
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
221-302 |
6.93e-04 |
|
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: 40.81 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 221 KLSGGELQR----FAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIYG 296
Cdd:cd03227 77 QLSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKV 156
|
....*.
gi 398365537 297 VPSVYG 302
Cdd:cd03227 157 ITGVYK 162
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
27-72 |
7.60e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 42.54 E-value: 7.60e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 398365537 27 RSCPVVKTGKLCIEVTptskIAFISEILCIGCGICVKKCPFDAIQI 72
Cdd:COG1148 474 RAIQLLSKGELGVEPS----VAEVDPEKCTGCGRCVEVCPYGAISI 515
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
18-79 |
9.37e-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: 41.52 E-value: 9.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365537 18 PKKCRQEC------KRSCPVVktgklCIEVTPTsKIAFISEILCIGCGICVKKCPFDAIQIINLPTNL 79
Cdd:COG2878 132 PKGCEYGCigcgdcIKACPFD-----AIVGAAK-GMHTVDEDKCTGCGLCVEACPVDCIEMVPVSPTV 193
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
48-85 |
1.00e-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: 434137 [Multi-domain] Cd Length: 59 Bit Score: 37.65 E-value: 1.00e-03
10 20 30
....*....|....*....|....*....|....*...
gi 398365537 48 AFISEILCIGCGICVKKCPFDAIQIINLPTNLEAHVTH 85
Cdd:pfam14697 1 ARIDEDTCIGCGKCYIACPDTSHQAIVGDGKRHHTVIE 38
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
196-254 |
1.08e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.78 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365537 196 EKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDV 254
Cdd:PRK11144 103 KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
25-71 |
1.12e-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: 39.56 E-value: 1.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 398365537 25 CKRSCPvvkTGKLciEVTPTSKIAFISEiLCIGCGICVKKCPFDAIQ 71
Cdd:cd16370 61 CAEACP---TGAL--EPRKGGGVVLDKE-KCIGCGNCVKACIVGAIF 101
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
54-84 |
1.21e-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: 319895 [Multi-domain] Cd Length: 154 Bit Score: 39.93 E-value: 1.21e-03
10 20 30
....*....|....*....|....*....|.
gi 398365537 54 LCIGCGICVKKCPFDAIQIINLPTNLEAHVT 84
Cdd:cd16373 15 LCIRCGLCVEACPTGVIQPAGLEDGLEGGRT 45
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
102-132 |
1.23e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 1.23e-03
10 20 30
....*....|....*....|....*....|.
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLG 132
Cdd:PRK11819 32 PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG 62
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
200-281 |
1.25e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 41.30 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 200 EDVKRYIKILQLENVLKRDIE-----KLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSL-LAPTKY 273
Cdd:PRK13646 119 DEVKNYAHRLLMDLGFSRDVMsqspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKT 198
|
....*...
gi 398365537 274 VICVEHDL 281
Cdd:PRK13646 199 IILVSHDM 206
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
7-82 |
1.32e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 41.66 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 7 RIAIVSADKCK-PKKCRQ----ECKRSCPvvkTGKLcieVTPTSKIAFISEiLCIGCGICVKKCPFDAIQIINLPTNLEA 81
Cdd:PRK12769 41 RITVIKHQQQRsAVTCHHcedaPCARSCP---NGAI---SHVDDSIQVNQQ-KCIGCKSCVVACPFGTMQIVLTPVAAGK 113
|
.
gi 398365537 82 H 82
Cdd:PRK12769 114 V 114
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
102-125 |
1.63e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 40.84 E-value: 1.63e-03
10 20
....*....|....*....|....
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAG 125
Cdd:COG4586 47 PGEIVGFIGPNGAGKSTTIKMLTG 70
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
18-66 |
1.65e-03 |
|
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: 36.84 E-value: 1.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 398365537 18 PKKCRQ--ECKRSCPVVKTGklcIEVTPTSKIAFISEIL---CIGCGICVKKCP 66
Cdd:pfam13237 6 PDKCIGcgRCTAACPAGLTR---VGAIVERLEGEAVRIGvwkCIGCGACVEACP 56
|
|
| PhsB_like |
cd10553 |
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ... |
38-71 |
1.72e-03 |
|
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319875 [Multi-domain] Cd Length: 146 Bit Score: 39.27 E-value: 1.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 398365537 38 CIEVTPTSK--------IAFISEILCIGCGICVKKCPFDAIQ 71
Cdd:cd10553 66 CVKACPTGAmqkrekdgIVYVDQELCIGCKACIEACPWGIPQ 107
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
11-74 |
1.77e-03 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 40.69 E-value: 1.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 11 VSADKCKPKKCRQECKRSCPVVKTgKLCIEVTPTSKIAFISE-------ILCIGCGICVKKCPFDAIQIIN 74
Cdd:PRK07118 91 KEAAESEPKVAVVRCQGTCDKAKE-RYEYQGIKDCAAAALLFggpkgcsYGCLGLGSCVAACPFDAIHIEN 160
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
101-294 |
1.79e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAGKQKPNLGrfddppewqEIIkyFRGSELQNYFTK--------MLEDDIKAIIKPQY 172
Cdd:PRK10982 22 RPHSIHALMGENGAGKSTLLKCLFGIYQKDSG---------SIL--FQGKEIDFKSSKealengisMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 173 VDNI-----PRaiKGPVqkvgellkLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDE 247
Cdd:PRK10982 91 MDNMwlgryPT--KGMF--------VDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 398365537 248 PSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCII 294
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
91-134 |
1.92e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 1.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 398365537 91 SFKLhrlptPrPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRF 134
Cdd:PRK11819 344 SFSL-----P-PGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
462-539 |
1.97e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 462 DQEVQHLSGGELQRVAIVLALG--IPADIYLIDEPSAYL---DSEQRIicsKVIRRfiLHNK-KTAFIVEHDFIMATyLA 535
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGaeLIGITYILDEPSIGLhpqDTHKLI---NVIKK--LRDQgNTVLLVEHDEQMIS-LA 544
|
....
gi 398365537 536 DKVI 539
Cdd:PRK00635 545 DRII 548
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
44-72 |
2.33e-03 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 36.94 E-value: 2.33e-03
10 20
....*....|....*....|....*....
gi 398365537 44 TSKIAFISEILCIGCGICVKKCPFDAIQI 72
Cdd:COG4231 13 TAMRYVIDEDKCTGCGACVKVCPADAIEE 41
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
468-542 |
2.43e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 40.07 E-value: 2.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 468 LSGGELQRVAIVLALGIPADIYLIDEPSAYLD--SEQRIIcsKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFE 542
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDvvAQARIL--DLLESIVQKRALGMLLVTHDMGVVARLADDVAVMS 215
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
102-209 |
2.63e-03 |
|
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: 38.89 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKP--------NLGRFDDPPEWQEIIKYFRGSELQNYFTKMLEDDIKAIIKPQY- 172
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPpgggviyiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPd 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 398365537 173 ---VDNIPRAIKGPVQKVGELLKLRMEKSPEDVKRYIKIL 209
Cdd:smart00382 81 vliLDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
54-74 |
2.93e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 40.75 E-value: 2.93e-03
|
| flavo_MJ0208 |
TIGR02700 |
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ... |
38-70 |
3.19e-03 |
|
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: 39.47 E-value: 3.19e-03
10 20 30
....*....|....*....|....*....|....*....
gi 398365537 38 CIEVTPTSKI------AFISEILCIGCGICVKKCPFDAI 70
Cdd:TIGR02700 156 CVDACPRSAIdmvdgkAFIRLLKCVGCGKCKEACPYNAI 194
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
383-512 |
3.48e-03 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 39.15 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 383 MMGENGTGKTTLIKLLAGalKPDEGQDIPKLNVSMKPQKIA-PKFPGTVRQlffkkirgQFLNPQFQTdVVKPLRIDDII 461
Cdd:cd03232 38 LMGESGAGKTTLLDVLAG--RKTAGVITGEILINGRPLDKNfQRSTGYVEQ--------QDVHSPNLT-VREALRFSALL 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 398365537 462 dqevQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRR 512
Cdd:cd03232 107 ----RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKK 153
|
|
| Fer4_16 |
pfam13484 |
4Fe-4S double cluster binding domain; |
20-67 |
3.65e-03 |
|
4Fe-4S double cluster binding domain;
Pssm-ID: 463893 [Multi-domain] Cd Length: 65 Bit Score: 36.31 E-value: 3.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365537 20 KCRQeCKRSCPV--------VKTGKLCIEVTPTSKIAFISEIL-------CIGCGICVKKCPF 67
Cdd:pfam13484 3 SCGK-CIDACPTgaivgpegVLDARRCISYLTIEKKGLIPDELrcllgnrCYGCDICQDVCPW 64
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
215-291 |
4.35e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 215 LKRDIEKLSGGELQRFAIG---MSCVQEADVYMFDEPSSYL---DVKQRLnaaQIIRSLLAPTKYVICVEHDLSVLDyLS 288
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLhthDIKALI---YVLQSLTHQGHTVVIIEHNMHVVK-VA 878
|
...
gi 398365537 289 DFV 291
Cdd:PRK00635 879 DYV 881
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
20-69 |
4.60e-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: 35.58 E-value: 4.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 398365537 20 KCRQeCKRSCPVVKTGKLCIEVTPTSKIAFISEILCIGCGICVKKCPFDA 69
Cdd:pfam12838 3 GCGA-CVAACPVGAITLDEVGEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
54-72 |
4.76e-03 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 38.39 E-value: 4.76e-03
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
222-282 |
4.94e-03 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 38.92 E-value: 4.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 222 LSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLS 282
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
198-253 |
5.62e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.11 E-value: 5.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365537 198 SPEDVKRYIKILQLeNVLKRDIEKL---------------SGGELQRFAIGMSCVQEADVYMFDEPSSYLD 253
Cdd:PLN03130 703 SPFDPERYERAIDV-TALQHDLDLLpggdlteigergvniSGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
215-289 |
6.33e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 215 LKRDIEKLSGGELQRFAI------GMSCVqeadVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHD---LSVLD 285
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLatqigsGLTGV----LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDedtIRAAD 557
|
....
gi 398365537 286 YLSD 289
Cdd:TIGR00630 558 YVID 561
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
217-280 |
6.77e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 6.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 217 RDIEKLSGGELQ------RFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHD 280
Cdd:PRK03918 784 RPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHD 853
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
25-71 |
7.05e-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: 434137 [Multi-domain] Cd Length: 59 Bit Score: 35.33 E-value: 7.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 398365537 25 CKRSCPVvkTGKLCIEVTPTSKIAFISEiLCIGCGICVKKCP-FDAIQ 71
Cdd:pfam14697 14 CYIACPD--TSHQAIVGDGKRHHTVIED-ECTGCNLCVSVCPvDDCIT 58
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
374-501 |
7.19e-03 |
|
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: 38.40 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 374 EFSDSEILVMMGENGTGKTTLIKLLAGAL------KPDEGQDIPKLNVSMKPQKIAPKFpgTVRQLFFKKIRGQFLN-PQ 446
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAITYALygktprYGRQENLRSVFAPGEDTAEVSFTF--QLGGKKYRVERSRGLDyDQ 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365537 447 FQTDVVKPL-RIDDIIDQEVQHLSGGELQRVAIVLAL----------GIPADIYLIDEPSAYLDSE 501
Cdd:cd03279 102 FTRIVLLPQgEFDRFLARPVSTLSGGETFLASLSLALalsevlqnrgGARLEALFIDEGFGTLDPE 167
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
222-289 |
7.58e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 7.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365537 222 LSGGELQRFAIGMSCVQEAD---VYMFDEPSSYL---DVKQRLNaaqIIRSLLAPTKYVICVEHDLSVL---DYLSD 289
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfdDIKKLLE---VLQRLVDKGNTVVVIEHNLDVIktaDYIID 903
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
55-72 |
7.84e-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: 7.84e-03
|
| Fer4_6 |
pfam12837 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
54-70 |
7.92e-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: 7.92e-03
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
101-125 |
8.15e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 38.65 E-value: 8.15e-03
10 20
....*....|....*....|....*
gi 398365537 101 RPGQVLGLVGTNGIGKSTALKILAG 125
Cdd:PRK13547 25 EPGRVTALLGRNGAGKSTLLKALAG 49
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
102-282 |
8.38e-03 |
|
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: 38.36 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 102 PGQVLGLVGTNGIGKSTALKILAGKQKPNLGR--FDDppewQEIIKYFRgSELQNYFTKMLEDDIkaIIKPQYVDNI--- 176
Cdd:cd03254 28 PGETVAIVGPTGAGKTTLINLLMRFYDPQKGQilIDG----IDIRDISR-KSLRSMIGVVLQDTF--LFSGTIMENIrlg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365537 177 -PRAIKGPVQKVGELLKLR--MEKSPEDvkryikilqLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLD 253
Cdd:cd03254 101 rPNATDEEVIEAAKEAGAHdfIMKLPNG---------YDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190
....*....|....*....|....*....|.
gi 398365537 254 VK--QRLNAAqiIRSLLApTKYVICVEHDLS 282
Cdd:cd03254 172 TEteKLIQEA--LEKLMK-GRTSIIIAHRLS 199
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
44-80 |
8.99e-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: 38.14 E-value: 8.99e-03
10 20 30
....*....|....*....|....*....|....*..
gi 398365537 44 TSKIAFISEILCIGCGICVKKCPFDAiqIINLPTNLE 80
Cdd:cd03110 55 GGKKAFIDQEKCIRCGNCERVCKFGA--ILEFFQKLI 89
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
221-295 |
9.52e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 38.54 E-value: 9.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365537 221 KLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSlLAPTKYVICVEHDLSVLDYLSDFVCIIY 295
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS-LADRLTVIIVTHNLAQAARISDRAALFF 236
|
|
| |
