|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-580 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 652.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 7 MKK--KGSWRQFLRLIRdtnPPKGILVFALLMSLLSTGASLFIPMLTKGLVDNFsLSSISTGQI----VGLVAFFVMQTI 80
Cdd:COG1132 1 MSKspRKLLRRLLRYLR---PYRGLLILALLLLLLSALLELLLPLLLGRIIDAL-LAGGDLSALllllLLLLGLALLRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 81 AAGLSIYLLNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVL 160
Cdd:COG1132 77 LSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 161 FVLDWKMTALLLTVIPLSVLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQF 240
Cdd:COG1132 157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 241 GLKEGKVQALISPVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINA 320
Cdd:COG1132 237 NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 321 ILEY--EVEDHETGVKVSNAKQSIVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGA 398
Cdd:COG1132 317 LLDEppEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 399 IKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGVEgEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGV 478
Cdd:COG1132 397 ILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRP-DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 479 KLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGS 558
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
570 580
....*....|....*....|..
gi 446376040 559 GTHDELLRTHDMYREFATQQLK 580
Cdd:COG1132 556 GTHEELLARGGLYARLYRLQFG 577
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-579 |
7.14e-175 |
|
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: 512.07 E-value: 7.14e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 8 KKKGSWRQFLRLIRdtnPPKGILVFALLMSLLSTGASLFIPMLTKGLVD----NFSLSSISTGqIVGLVAFFVMQTIAAG 83
Cdd:COG2274 139 EKPFGLRWFLRLLR---RYRRLLLQVLLASLLINLLALATPLFTQVVIDrvlpNQDLSTLWVL-AIGLLLALLFEGLLRL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 84 LSIYLLNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMtNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVL 163
Cdd:COG2274 215 LRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 164 DWKMTALLLTVIPLSVLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLK 243
Cdd:COG2274 294 SPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFK 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 244 EGKVQALISPVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINAILE 323
Cdd:COG2274 374 LRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILD 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 324 YEVEDHETGVKVS--NAKQSIVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIK 400
Cdd:COG2274 454 LPPEREEGRSKLSlpRLKGDIELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 401 LGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGVEgEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKL 480
Cdd:COG2274 534 IDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDP-DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNL 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 481 SGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGT 560
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT 692
|
570
....*....|....*....
gi 446376040 561 HDELLRTHDMYREFATQQL 579
Cdd:COG2274 693 HEELLARKGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
25-579 |
6.13e-149 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 441.06 E-value: 6.13e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 25 PPKGILVFALLMSLLSTGASLFIPMLTKGLVDN-FSLSSIS--TGQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLR 101
Cdd:TIGR02204 15 PYRGRVLAALVALLITAAATLSLPYAVRLMIDHgFSKDSSGllNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 102 ERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLI 181
Cdd:TIGR02204 95 RAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 182 LVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMA 261
Cdd:TIGR02204 175 ILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 262 LLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINAILEYEVEDHETGVKVS---NA 338
Cdd:TIGR02204 255 AIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTlpvPL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 339 KQSIVLENVHFEYNE--DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRR 416
Cdd:TIGR02204 335 RGEIEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 417 QIGYVSQDSPLIDGTIRDNICYGVEgEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLR 496
Cdd:TIGR02204 415 RMALVPQDPVLFAASVMENIRYGRP-DATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILK 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 497 NPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHDMYREFAT 576
Cdd:TIGR02204 494 DAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLAR 573
|
...
gi 446376040 577 QQL 579
Cdd:TIGR02204 574 LQF 576
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-571 |
9.14e-144 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 427.60 E-value: 9.14e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 16 FLRLIRDTNPPKGILVFALLMSLLSTGASLFIPMLTKGLVDN-FSLSSISTGQIV--GLVAFFVMQTIAAGLSIYLLNYI 92
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDgFGGRDRSVLWWVplVVIGLAVLRGICSFVSTYLLSWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 93 GQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLL 172
Cdd:TIGR02203 82 SNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 173 TVIPLSVLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALIS 252
Cdd:TIGR02203 162 VMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 253 PVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINAILEYEVEDHETG 332
Cdd:TIGR02203 242 PITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 333 VKVSNAKQSIVLENVHFEYNEDE-KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSL 411
Cdd:TIGR02203 322 RAIERARGDVEFRNVTFRYPGRDrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 412 QSWRRQIGYVSQDSPLIDGTIRDNICYGVEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIA 491
Cdd:TIGR02203 402 ASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 492 RALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHDMY 571
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
30-318 |
2.70e-129 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 380.24 E-value: 2.70e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWKKVL 109
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 110 VLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPLGRKM 189
Cdd:cd18551 81 RLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 190 YKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVIIVGY 269
Cdd:cd18551 161 RKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446376040 270 GGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18551 241 GGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-572 |
3.15e-123 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 379.45 E-value: 3.15e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 17 LRLIRDTNPPKGILVFALLMSLLSTGASLFIPMLTKGLVD----NFSLSSISTGqIVGLVAFFVMQTIAAGLSIYLLNYI 92
Cdd:TIGR00958 150 FRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDtlggDKGPPALASA-IFFMCLLSIASSVSAGLRGGSFNYT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 93 GQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLL 172
Cdd:TIGR00958 229 MARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 173 TVIPLSVLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALIS 252
Cdd:TIGR00958 309 INLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 253 PVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINAILEYEVEDHETG 332
Cdd:TIGR00958 389 WTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 333 -VKVSNAKQSIVLENVHFEY--NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSY 409
Cdd:TIGR00958 469 tLAPLNLEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 410 SLQSWRRQIGYVSQDSPLIDGTIRDNICYGVEgEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIA 489
Cdd:TIGR00958 549 DHHYLHRQVALVGQEPVLFSGSVRENIAYGLT-DTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIA 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKALNnlMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHD 569
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG 705
|
...
gi 446376040 570 MYR 572
Cdd:TIGR00958 706 CYK 708
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-568 |
1.85e-122 |
|
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: 372.55 E-value: 1.85e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 18 RLIRDTNPPKGILVFALLMSLLSTG-----ASLFIPMLTKGLVDNFSLSSIsTGQIVGLVAFFVMQTIAAGLSIYLLNYI 92
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLliiaqAWLLASLLAGLIIGGAPLSAL-LPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 93 GQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTndTGV--VKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTAL 170
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLT--EGVeaLDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 171 LLTVIPLSVLILVPLGRKMYKISK----ALQDETASFTSVLtQVLSEIRLVKSSNTEKREYETGNTGIQ----KLLqfgl 242
Cdd:COG4988 164 LLVTAPLIPLFMILVGKGAAKASRrqwrALARLSGHFLDRL-RGLTTLKLFGRAKAEAERIAEASEDFRkrtmKVL---- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 243 kegKVQALISPVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINAIL 322
Cdd:COG4988 239 ---RVAFLSSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 323 EYEVEDHETGVKVSNAKQ--SIVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIK 400
Cdd:COG4988 316 DAPEPAAPAGTAPLPAAGppSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 401 LGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGvEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKL 480
Cdd:COG4988 396 INGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLG-RPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 481 SGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGT 560
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGT 554
|
....*...
gi 446376040 561 HDELLRTH 568
Cdd:COG4988 555 HEELLAKN 562
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
217-566 |
2.22e-115 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 355.67 E-value: 2.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 217 VKSSNTEKRE----------YETGNTGIQK---LLQFGlkegkvQALIspvmsfvlMAL-LVIIVGYGGMRVSSGALTTG 282
Cdd:COG5265 231 VKYFGNEAREarrydealarYERAAVKSQTslaLLNFG------QALI--------IALgLTAMMLMAAQGVVAGTMTVG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 283 ELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINAILEY--EVEDHETGVKVSNAKQSIVLENVHFEYNEDEKVLNN 360
Cdd:COG5265 297 DFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQppEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKG 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 361 IDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGV 440
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGR 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 441 EGeVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQK 520
Cdd:COG5265 457 PD-ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQA 535
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446376040 521 ALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLR 566
Cdd:COG5265 536 ALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLA 581
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
12-571 |
3.02e-115 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 354.71 E-value: 3.02e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 12 SWRQFLRLIRDTNPPK-GILVFALLMSLLSTGASLFIPMLTKGLVDNF--SLSSISTGQIVGLVAFFVMQTIAAGLSIYL 88
Cdd:PRK11176 9 TWQTFRRLWPTIAPFKaGLIVAGVALILNAASDTFMLSLLKPLLDDGFgkADRSVLKWMPLVVIGLMILRGITSFISSYC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 89 LNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMT 168
Cdd:PRK11176 89 ISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 169 ALLLTVIPL-SVLILVpLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKV 247
Cdd:PRK11176 169 LILIVIAPIvSIAIRV-VSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 248 QALISPVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINAILEYEVE 327
Cdd:PRK11176 248 SSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 328 DHETGVKVSNAKQSIVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESI 406
Cdd:PRK11176 328 KDEGKRVIERAKGDIEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 407 TSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGVEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQ 486
Cdd:PRK11176 408 RDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQ 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 487 RIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLR 566
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA 567
|
....*
gi 446376040 567 THDMY 571
Cdd:PRK11176 568 QNGVY 572
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
342-578 |
6.37e-112 |
|
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: 333.74 E-value: 6.37e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNE--DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIG 419
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 420 YVSQDSPLIDGTIRDNICYGVEgEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQ 499
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP-DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHDMYREFATQQ 578
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-574 |
9.04e-111 |
|
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: 342.52 E-value: 9.04e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 13 WRQFLRLIRdtnPPKGILVFALLMSLLSTGASLfipmltkGLvdnFSLSS--ISTGQIVGLVaFFVMQTIAA--GLSI-- 86
Cdd:COG4987 3 LLRLLRLLR---PHRGRLLLGVLLGLLTLLAGI-------GL---LALSGwlIAAAALAPPI-LNLFVPIVGvrAFAIgr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 87 ----YLLNYIGQ----KIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTgvvktlisEHLSNL--------LTGG 150
Cdd:COG4987 69 tvfrYLERLVSHdatlRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLylrvllplLVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 151 ISIVGSLIVLFVLDWKMtALLLTVIPLSVLILVPL--GRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYE 228
Cdd:COG4987 141 LVILAAVAFLAFFSPAL-ALVLALGLLLAGLLLPLlaARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 229 TGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILY---LVQIIMPMSQlsmFF 305
Cdd:COG4987 220 RLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAalaLFEALAPLPA---AA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 306 TQFQKAIGATERINAILEYE--VEDHETGVKVSNAkQSIVLENVHFEY-NEDEKVLNNIDFTIESGKVTAIVGPSGSGKT 382
Cdd:COG4987 297 QHLGRVRAAARRLNELLDAPpaVTEPAEPAPAPGG-PSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 383 TLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGVEgEVTDAEIEKVAAMAYVDAFI 462
Cdd:COG4987 376 TLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP-DATDEELWAALERVGLGDWL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 463 HDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVV 542
Cdd:COG4987 455 AALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE 534
|
570 580 590
....*....|....*....|....*....|..
gi 446376040 543 DADKIIFIEKGNLTGSGTHDELLRTHDMYREF 574
Cdd:COG4987 535 RMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
342-573 |
2.42e-106 |
|
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: 319.56 E-value: 2.42e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGY 420
Cdd:cd03251 1 VEFKNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDGTIRDNICYGVEGEvTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQI 500
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGA-TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 501 LMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHDMYRE 573
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
342-578 |
2.30e-105 |
|
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: 316.86 E-value: 2.30e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYV 421
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDGTIRDNICYGVEGeVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQIL 501
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPD-ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 502 MLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHDMYREFATQQ 578
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
342-565 |
3.45e-95 |
|
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: 290.67 E-value: 3.45e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYV 421
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDGTIRDNICYGVEgEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQIL 501
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRP-NATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446376040 502 MLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELL 565
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
29-578 |
8.89e-95 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 304.74 E-value: 8.89e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 29 ILVFALLMSLLSTGASLFIP-MLTKGLVDNfSLSSISTgQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWKK 107
Cdd:TIGR01846 144 VLLISLALQLFALVTPLLFQvVIDKVLVHR-GLSTLSV-LALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRH 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 108 VLVLPVSYYDQNRTGDTISRMTNdtgvvktliSEHLSNLLTGG-----ISIVGSLIVLFVLDW---KMTALLLTVIPLSV 179
Cdd:TIGR01846 222 LLGLPLGYFESRRVGDTVARVRE---------LEQIRNFLTGSaltvvLDLLFVVVFLAVMFFyspTLTGVVIGSLVCYA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 180 LILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVL 259
Cdd:TIGR01846 293 LLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQ 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 260 MALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINAILEYEVEDHETG-VKVSNA 338
Cdd:TIGR01846 373 KLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGlAALPEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 339 KQSIVLENVHFEYNEDE-KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQ 417
Cdd:TIGR01846 453 RGAITFENIRFRYAPDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQ 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 418 IGYVSQDSPLIDGTIRDNICYGVEGeVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRN 497
Cdd:TIGR01846 533 MGVVLQENVLFSRSIRDNIALCNPG-APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGN 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 498 PQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHDMYREFATQ 577
Cdd:TIGR01846 612 PRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQ 691
|
.
gi 446376040 578 Q 578
Cdd:TIGR01846 692 Q 692
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
107-565 |
3.58e-93 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 297.64 E-value: 3.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 107 KVLVLPVSYYDQNRTGDTISRMTNDTGVVKTL----ISEHLSNLLtggisivgSLIVL----FVLDWKMTALLLTVipls 178
Cdd:PRK13657 98 RIIQLPLAWHSQRGSGRALHTLLRGTDALFGLwlefMREHLATLV--------ALVVLlplaLFMNWRLSLVLVVL---- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 179 VLILVPLGRKMYKISKALQDETASFTSVL----TQVLSEIRLVKSSNTEKREYETGNTGIQKLLqfglkegKVQaliSPV 254
Cdd:PRK13657 166 GIVYTLITTLVMRKTKDGQAAVEEHYHDLfahvSDAIGNVSVVQSYNRIEAETQALRDIADNLL-------AAQ---MPV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 255 MS--------------FVLMALLVIivgyGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQ-FQKAIGATERIN 319
Cdd:PRK13657 236 LSwwalasvlnraastITMLAILVL----GAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQvFMAAPKLEEFFE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 320 aILE--YEVEDHETGVKVSNAKQSIVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGG 397
Cdd:PRK13657 312 -VEDavPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 398 AIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGVEGeVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERG 477
Cdd:PRK13657 391 RILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD-ATDEEMRAAAERAQAHDFIERKPDGYDTVVGERG 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 478 VKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTG 557
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
....*...
gi 446376040 558 SGTHDELL 565
Cdd:PRK13657 550 SGSFDELV 557
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
8-573 |
1.48e-87 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 286.07 E-value: 1.48e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 8 KKKGSWRQFLRLIRDTnppKGILVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSIS---TGQIVGLVAFFVMQTIAAGL 84
Cdd:TIGR03796 137 RKPSLLRALWRRLRGS---RGALLYLLLAGLLLVLPGLVIPAFSQIFVDEILVQGRQdwlRPLLLGMGLTALLQGVLTWL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 85 SIYLLNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRM-TNDTgvVKTLISEHLSNLLTGGISIVGSLIVLFVL 163
Cdd:TIGR03796 214 QLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVqLNDQ--VAEFLSGQLATTALDAVMLVFYALLMLLY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 164 DWKMTALLLTVIPLSVLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKrEYETGNTGIQ-KLLQFGL 242
Cdd:TIGR03796 292 DPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLES-DFFSRWAGYQaKLLNAQQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 243 KEGKVQALISPVMSFvLMAL-LVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINAI 321
Cdd:TIGR03796 371 ELGVLTQILGVLPTL-LTSLnSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDV 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 322 LEYEVE--DHETGVKVSNAKQS------IVLENVHFEYNE-DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFY 392
Cdd:TIGR03796 450 LRNPVDplLEEPEGSAATSEPPrrlsgyVELRNITFGYSPlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLY 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 393 EPTGGAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGvEGEVTDAEIEKVAAmayvDAFIHD----LPNG 468
Cdd:TIGR03796 530 QPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLW-DPTIPDADLVRACK----DAAIHDvitsRPGG 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 469 YATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVqkaLNNLMK-GRTTLVIAHRLSTVVDADKI 547
Cdd:TIGR03796 605 YDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII---DDNLRRrGCTCIIVAHRLSTIRDCDEI 681
|
570 580
....*....|....*....|....*.
gi 446376040 548 IFIEKGNLTGSGTHDELLRTHDMYRE 573
Cdd:TIGR03796 682 IVLERGKVVQRGTHEELWAVGGAYAR 707
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
45-586 |
3.17e-84 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 273.51 E-value: 3.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 45 LFIPMLTKGLVDNFSLSSISTGQIVGLVAffVMQTIAagLSIYLLNYIGQKIVAG--------LRERLWKKVLVLPVSYY 116
Cdd:PRK10789 12 LIPPKVVGIIVDGVTEQHMTTGQILMWIG--TMVLIA--VVVYLLRYVWRVLLFGasyqlaveLREDFYRQLSRQHPEFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 117 DQNRTGDTISRMTNDTGVVKTLISEhlsNLLTGGISIVGSLIVLFV----LDWKMTALLLTVIPLSVLILVPLGRKMYKI 192
Cdd:PRK10789 88 LRHRTGDLMARATNDVDRVVFAAGE---GVLTLVDSLVMGCAVLIVmstqISWQLTLLALLPMPVMAIMIKRYGDQLHER 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 193 SKALQdetASFTSVLTQV---LSEIRLVKSSNTEKR-----EYETGNTGIQKLlqfglKEGKVQALISPVMSFVL-MALL 263
Cdd:PRK10789 165 FKLAQ---AAFSSLNDRTqesLTSIRMIKAFGLEDRqsalfAADAEDTGKKNM-----RVARIDARFDPTIYIAIgMANL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 264 VIIVGyGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINAILEYE--VEDhetGVKVSNAKQS 341
Cdd:PRK10789 237 LAIGG-GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEApvVKD---GSEPVPEGRG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENV-HFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIG 419
Cdd:PRK10789 313 ELDVNIrQFTYPQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 420 YVSQDSPLIDGTIRDNICYGvEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQ 499
Cdd:PRK10789 393 VVSQTPFLFSDTVANNIALG-RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRT----HDMYRefa 575
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQsgwyRDMYR--- 548
|
570
....*....|.
gi 446376040 576 TQQLkikEGAL 586
Cdd:PRK10789 549 YQQL---EAAL 556
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
342-553 |
1.32e-81 |
|
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: 253.07 E-value: 1.32e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGY 420
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDGTIRDNIcygvegevtdaeiekvaamayvdafihdlpngyatevgergvkLSGGQRQRIAIARALLRNPQI 500
Cdd:cd03228 81 VPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446376040 501 LMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKG 553
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-572 |
9.45e-81 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 265.04 E-value: 9.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 13 WRQFLRLIRDTNPPKGILVFALLMSLLSTGASLFIPMLTKGLVDNF-SLSSISTGQIVGL-VAFFVMQTIAAGLSIY--- 87
Cdd:PRK10790 8 WPTLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMvAKGNLPLGLVAGLaAAYVGLQLLAAGLHYAqsl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 88 LLNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKM 167
Cdd:PRK10790 88 LFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 168 TALLLTVIPLSVLILV-------PLGRKMYKISKALQD---ETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKL 237
Cdd:PRK10790 168 ALVAIMIFPAVLVVMViyqrystPIVRRVRAYLADINDgfnEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 238 LQFGLKegkvqALISPVMSFVLMALLvIIVGYGGmrvsSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATER 317
Cdd:PRK10790 248 DGFLLR-----PLLSLFSALILCGLL-MLFGFSA----SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 318 INAILEYEVEDHETGVKVSNAKqSIVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGG 397
Cdd:PRK10790 318 VFELMDGPRQQYGNDDRPLQSG-RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 398 AIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGveGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERG 477
Cdd:PRK10790 397 EIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG--RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 478 VKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTG 557
Cdd:PRK10790 475 NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
570
....*....|....*....
gi 446376040 558 SGTHDELL----RTHDMYR 572
Cdd:PRK10790 555 QGTHQQLLaaqgRYWQMYQ 573
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
27-548 |
9.76e-81 |
|
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: 263.38 E-value: 9.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 27 KGILVFALLMSLLSTGASLFIPMLTKGLVDNFS-----LSSISTgQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLR 101
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQAWLLARVVDGLIsagepLAELLP-ALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 102 ERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLI 181
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 182 LVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFvLMA 261
Cdd:TIGR02857 161 MILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLEL-FAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 262 LLVIIVG-YGGMRVSSGALTtgeLVA--FILYLV-QIIMPMSQLSMFFTQFQKAIGATERINAILEY-EVEDHETGVKVS 336
Cdd:TIGR02857 240 LSVALVAvYIGFRLLAGDLD---LATglFVLLLApEFYLPLRQLGAQYHARADGVAAAEALFAVLDAaPRPLAGKAPVTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 337 NAKQSIVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRR 416
Cdd:TIGR02857 317 APASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 417 QIGYVSQDSPLIDGTIRDNICYGvEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLR 496
Cdd:TIGR02857 397 QIAWVPQHPFLFAGTIAENIRLA-RPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLR 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446376040 497 NPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKII 548
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIV 527
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
342-578 |
3.38e-80 |
|
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: 252.02 E-value: 3.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGY 420
Cdd:cd03252 1 ITFEHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDGTIRDNICYGVEGeVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQI 500
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPG-MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 501 LMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHDMYREFATQQ 578
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
9-579 |
6.69e-80 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 265.28 E-value: 6.69e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 9 KKGSWRQFLRLI-----RDtnppkgiLVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSiSTGQIVGLVAFFVMQTIAAG 83
Cdd:TIGR03797 119 KALGLRDLLRFAlrgarRD-------LLAILAMGLLGTLLGMLVPIATGILIGTAIPDA-DRSLLVQIALALLAAAVGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 84 L-----SIYLLNyIGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVgSLI 158
Cdd:TIGR03797 191 AfqlaqSLAVLR-LETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMGISQIRRILSGSTLTTLLSGIFALL-NLG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 159 VLFVLDWKMTALLLTVIPLSVLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYE--TGNTGIQK 236
Cdd:TIGR03797 269 LMFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFArwAKLFSRQR 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 237 LLQfgLKEGKVQ---ALISPVMSFVLMALLVIIVGYGGMRvssGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIG 313
Cdd:TIGR03797 349 KLE--LSAQRIEnllTVFNAVLPVLTSAALFAAAISLLGG---AGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIP 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 314 ATERINAILEYEVEDHETGVKVSNAKQSIVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFY 392
Cdd:TIGR03797 424 LWERAKPILEALPEVDEAKTDPGKLSGAIEVDRVTFRYRPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 393 EPTGGAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGVEgeVTDAEIEKVAAMAYVDAFIHDLPNGYATE 472
Cdd:TIGR03797 504 TPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAP--LTLDEAWEAARMAGLAEDIRAMPMGMHTV 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 473 VGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLmkGRTTLVIAHRLSTVVDADKIIFIEK 552
Cdd:TIGR03797 582 ISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDA 659
|
570 580
....*....|....*....|....*..
gi 446376040 553 GNLTGSGTHDELLRTHDMYREFATQQL 579
Cdd:TIGR03797 660 GRVVQQGTYDELMAREGLFAQLARRQL 686
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
33-318 |
1.70e-78 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 249.71 E-value: 1.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 33 ALLMSLLSTGASLFIPMLTKGLVDNFsLSSISTGQI----VGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWKKV 108
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAA-LGGGDTASLnqiaLLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 109 LVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPLGRK 188
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 189 MYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVIIVG 268
Cdd:cd18576 160 IRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446376040 269 YGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18576 240 YGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-573 |
1.11e-77 |
|
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: 259.67 E-value: 1.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 9 KKGSWRQFLRLIRDTNPPKGILVFA-LLMSLLSTGASLFIpmltKGLVDNF-------SLSSIStgqiVGLVAFFVMQTI 80
Cdd:TIGR01193 140 KENSLLKFIPLITRQKKLIVNIVIAaIIVTLISIAGSYYL----QKIIDTYiphkmmgTLGIIS----IGLIIAYIIQQI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 81 AAGLSIYLLNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLiVL 160
Cdd:TIGR01193 212 LSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGL-FL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 161 FVLDWKMTALLLTVIPLSVLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQF 240
Cdd:TIGR01193 291 VRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 241 GLKEGKVQALISPVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINA 320
Cdd:TIGR01193 371 SFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 321 IL--EYEVEDHETGVKVSNAKQSIVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGA 398
Cdd:TIGR01193 451 VYlvDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 399 IKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGVEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGV 478
Cdd:TIGR01193 531 ILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGS 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 479 KLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSEsvvQKALNNL--MKGRTTLVIAHRLSTVVDADKIIFIEKGNLT 556
Cdd:TIGR01193 611 SISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLlnLQDKTIIFVAHRLSVAKQSDKIIVLDHGKII 687
|
570
....*....|....*..
gi 446376040 557 GSGTHDELLRTHDMYRE 573
Cdd:TIGR01193 688 EQGSHDELLDRNGFYAS 704
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
48-564 |
2.76e-75 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 250.58 E-value: 2.76e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 48 PMLTKGLVDNFSLSSISTGQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISR 127
Cdd:TIGR01192 39 PILFGRIIDAISSKSDVLPTLALWAGFGVFNTIAYVLVAREADRLAHGRRATLLTEAFGRIISMPLSWHQQRGTSNALHT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 128 MTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPLGRKMYKISKALQDETASFTSVL 207
Cdd:TIGR01192 119 LLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSIVLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 208 TQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAF 287
Cdd:TIGR01192 199 SDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVLDWWALASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 288 ILYLVQIIMPMSQLSMFFTQFQKAIGATERInAILEYEVEDHETGV---KVSNAKQSIVLENVHFEYNEDEKVLNNIDFT 364
Cdd:TIGR01192 279 IGFANLLIGRLDQMSGFITQIFEARAKLEDF-FDLEDSVFQREEPAdapELPNVKGAVEFRHITFEFANSSQGVFDVSFE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 365 IESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGVEGeV 444
Cdd:TIGR01192 358 AKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREG-A 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 445 TDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNN 524
Cdd:TIGR01192 437 TDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDA 516
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446376040 525 LMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDEL 564
Cdd:TIGR01192 517 LRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQEL 556
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
345-555 |
3.35e-74 |
|
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: 236.21 E-value: 3.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 345 ENVHFEY--NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVS 422
Cdd:cd03248 15 QNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 423 QDSPLIDGTIRDNICYGVeGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQILM 502
Cdd:cd03248 95 QEPVLFARSLQDNIAYGL-QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446376040 503 LDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNL 555
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
30-318 |
8.43e-74 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 237.32 E-value: 8.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDN-FSLSSISTGQIV--GLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWK 106
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDiFVEKDLEALLLVplAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 107 KVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPLG 186
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 187 RKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVII 266
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446376040 267 VGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
30-318 |
1.51e-73 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 236.68 E-value: 1.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNFSLS---SISTGQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWK 106
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAgdlSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 107 KVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPLG 186
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 187 RKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVII 266
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446376040 267 VGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
341-559 |
1.75e-69 |
|
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: 223.62 E-value: 1.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNEDE-KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIG 419
Cdd:cd03245 2 RIEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 420 YVSQDSPLIDGTIRDNICYGVeGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQ 499
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGA-PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSG 559
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
287-578 |
6.67e-68 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 230.89 E-value: 6.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 287 FILYLV-QIIMPMSQLSMFFTQFQKAIGATERINAILEYEVEDHETGVKVSNAKQSIVLENVHFE-YNEDEKVL-NNIDF 363
Cdd:PRK11174 292 FVLILApEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEKELASNDPVTIEAEDLEiLSPDGKTLaGPLNF 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 364 TIESGKVTAIVGPSGSGKTTLFSLLERF--YEptgGAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGvE 441
Cdd:PRK11174 372 TLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG-N 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 442 GEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKA 521
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 522 LNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHDMYREFATQQ 578
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-538 |
1.32e-67 |
|
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: 228.40 E-value: 1.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 17 LRLIRDTNPPKGILVFALLMSLLSTGASLFIPMLTKGLVdnfSLSSIS------TGQIVGLVAFfvmqTIAAGLSIYLLN 90
Cdd:TIGR02868 2 LRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLI---SRAAEMppvlylSVAAVAVRAF----GIGRAVFRYLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 91 YIGQ----KIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWK 166
Cdd:TIGR02868 75 LVGHdaalRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 167 MtALLLTVIPLSVLILVPL--GRKMYKISKALQDETASFTSVLTQVL---SEIRLVKSSNTEKREYETGNTGIQKLLQFG 241
Cdd:TIGR02868 155 A-ALILAAGLLLAGFVAPLvsLRAARAAEQALARLRGELAAQLTDALdgaAELVASGALPAALAQVEEADRELTRAERRA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 242 LK-EGKVQALISPVMSFVLMALLVIivgyGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINA 320
Cdd:TIGR02868 234 AAaTALGAALTLLAAGLAVLGALWA----GGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 321 ILEYEVE----DHETGVKVSNAKQSIVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTG 396
Cdd:TIGR02868 310 VLDAAGPvaegSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 397 GAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGvEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGER 476
Cdd:TIGR02868 390 GEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA-RPDATDEELWAALERVGLADWLRALPDGLDTVLGEG 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446376040 477 GVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRL 538
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
33-318 |
1.52e-67 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 220.89 E-value: 1.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 33 ALLMSLLSTGASLFIPMLTKGLVDNFSLSSIS---TGQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWKKVL 109
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLdvlNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 110 VLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPLGRKM 189
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 190 YKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVIIVGY 269
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446376040 270 GGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
30-318 |
9.39e-66 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 216.61 E-value: 9.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQ-------IVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRE 102
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNtslllllVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 103 RLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLIL 182
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 183 VPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMAL 262
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 263 LVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
341-560 |
5.68e-65 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 211.97 E-value: 5.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIG 419
Cdd:cd03244 2 DIEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 420 YVSQDSPLIDGTIRDNICygVEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQ 499
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLD--PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGT 560
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
247-566 |
3.74e-63 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 217.31 E-value: 3.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 247 VQALISPVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAfilylVQIIM-----PMSQLSMFFTQFQKAIGATERINAI 321
Cdd:COG4618 237 RAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIA-----ASILMgralaPIEQAIGGWKQFVSARQAYRRLNEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 322 LEyEVEDHETGVKVSNAKQSIVLENVHFEY-NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIK 400
Cdd:COG4618 312 LA-AVPAEPERMPLPRPKGRLSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 401 LGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYgvEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKL 480
Cdd:COG4618 391 LDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIAR--FGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 481 SGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNL-MKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSG 559
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFG 548
|
....*..
gi 446376040 560 THDELLR 566
Cdd:COG4618 549 PRDEVLA 555
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
30-318 |
3.28e-62 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 206.90 E-value: 3.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNFslssISTGQ-------IVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRE 102
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSV----IGGGLrellwllALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 103 RLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLIL 182
Cdd:cd18542 77 DLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 183 VPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMAL 262
Cdd:cd18542 157 YVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQ 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 263 LVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18542 237 IVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-554 |
2.67e-59 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 214.51 E-value: 2.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 2 EVRNEMKKKGSWRQFlRLIRDTNPP------------KGILVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQIV 69
Cdd:PTZ00265 23 EVEKELNKKGTFELY-KKIKTQKIPfflpfkclpashRKLLGVSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDIIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 70 GLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRTgdtiSRMTNDTGV----VKTLISEHLSN 145
Cdd:PTZ00265 102 SLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPG----SKLTSDLDFyleqVNAGIGTKFIT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 146 LLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPLGRKMyKISKALQDETASFT-SVLTQVLSEIRLVKSSNTEK 224
Cdd:PTZ00265 178 IFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKV-KINKKTSLLYNNNTmSIIEEALVGIRTVVSYCGEK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 225 REYETGNTGIQKLLQFGLKEGKVQAL-ISPVMSFVLMALLV-------IIVGYGGMRVSSGALTTGELVAFIL------Y 290
Cdd:PTZ00265 257 TILKKFNLSEKLYSKYILKANFMESLhIGMINGFILASYAFgfwygtrIIISDLSNQQPNNDFHGGSVISILLgvlismF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 291 LVQIIMPMsqlsmfFTQFQKAIGATERINAILEYE--VEDHETGVKVSNAKQsIVLENVHFEYN--EDEKVLNNIDFTIE 366
Cdd:PTZ00265 337 MLTIILPN------ITEYMKSLEATNSLYEIINRKplVENNDDGKKLKDIKK-IQFKNVRFHYDtrKDVEIYKDLNFTLT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 367 SGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLG-KESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGV----- 440
Cdd:PTZ00265 410 EGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkd 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 441 ----------------EGE-----------------------------------VTDAEIEKVAAMAYVDAFIHDLPNGY 469
Cdd:PTZ00265 490 lealsnyynedgndsqENKnkrnscrakcagdlndmsnttdsneliemrknyqtIKDSEVVDVSKKVLIHDFVSALPDKY 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 470 ATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLmKG---RTTLVIAHRLSTVVDADK 546
Cdd:PTZ00265 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL-KGnenRITIIIAHRLSTIRYANT 648
|
650
....*....|.
gi 446376040 547 IIFI---EKGN 554
Cdd:PTZ00265 649 IFVLsnrERGS 659
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
30-318 |
5.72e-59 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 198.38 E-value: 5.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQIVGLVA--FFVMQTIAAGLS---IYLLNYIGQKIVAGLRERL 104
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLAllYLGLLLLSFLLQylqTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 105 WKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVP 184
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 185 LGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLV 264
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446376040 265 IIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
95-574 |
1.71e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 205.06 E-value: 1.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 95 KIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDtgvVKTLisEHL-----SNLLTGGISIVGSLIVLFVLDWKMtA 169
Cdd:PRK11160 90 RVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVAD---VDTL--DHLylrliSPLVAALVVILVLTIGLSFFDLTL-A 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 170 LLLTVIPLSVLILVP-----LGRKmykISKALQDETASFTSVLT---QVLSEIRLVkssNTEKREYETGNTGIQKLLQFG 241
Cdd:PRK11160 164 LTLGGILLLLLLLLPllfyrLGKK---PGQDLTHLRAQYRVQLTewlQGQAELTLF---GAEDRYRQQLEQTEQQWLAAQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 242 LKEGKVQALISPVMSFVLMALLVIIV-----GYGGmRVSSGALTTgeLVAF-ILYLVQIIMPmsqLSMFFTQFQKAIGAT 315
Cdd:PRK11160 238 RRQANLTGLSQALMILANGLTVVLMLwlaagGVGG-NAQPGALIA--LFVFaALAAFEALMP---VAGAFQHLGQVIASA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 316 ERINAILEYEVE---DHETGVKVSNAkqSIVLENVHFEY-NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERF 391
Cdd:PRK11160 312 RRINEITEQKPEvtfPTTSTAAADQV--SLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 392 YEPTGGAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGVEgEVTDAEIEKVAAMAYVDAFIHDlPNGYAT 471
Cdd:PRK11160 390 WDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAP-NASDEALIEVLQQVGLEKLLED-DKGLNA 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 472 EVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIE 551
Cdd:PRK11160 468 WLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMD 547
|
490 500
....*....|....*....|...
gi 446376040 552 KGNLTGSGTHDELLRTHDMYREF 574
Cdd:PRK11160 548 NGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
30-318 |
4.61e-58 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 196.22 E-value: 4.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQI----VGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLW 105
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLlglaLLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 106 KKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPL 185
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 186 GRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVI 265
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446376040 266 IVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18778 241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
30-318 |
6.76e-58 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 195.70 E-value: 6.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQI---------VGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGL 100
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVdfsgllrilLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 101 RERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVL 180
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 181 ILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLM 260
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 261 ALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
33-318 |
5.65e-57 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 193.24 E-value: 5.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 33 ALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQ---------IVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRER 103
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEealralnqaVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 104 LWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILV 183
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 184 PLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALL 263
Cdd:cd18780 161 IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 264 VIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18780 241 VLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
33-318 |
1.20e-56 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 192.34 E-value: 1.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 33 ALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQI--------VGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERL 104
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFglslktfaLALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 105 WKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVP 184
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 185 LGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLV 264
Cdd:cd18573 161 YGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446376040 265 IIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18573 241 SVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
33-318 |
8.47e-56 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 190.00 E-value: 8.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 33 ALLMSLLSTGASLFIPMLTKGLVDNFsLSSISTGQI----VGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWKKV 108
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQG-FAAGNTALLnrafLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 109 LVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPLGRK 188
Cdd:cd18575 80 LRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 189 MYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVIIVG 268
Cdd:cd18575 160 VRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446376040 269 YGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18575 240 LGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
249-565 |
1.98e-55 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 196.03 E-value: 1.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 249 ALISPVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINAILEyEVED 328
Cdd:TIGR01842 225 GMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLA-NYPS 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 329 HETGVKVSNAKQSIVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESIT 407
Cdd:TIGR01842 304 RDPAMPLPEPEGHLSVENVTIVPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 408 SYSLQSWRRQIGYVSQDSPLIDGTIRDNICYgVEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQR 487
Cdd:TIGR01842 384 QWDRETFGKHIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQR 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 488 IAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELL 565
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
30-318 |
9.80e-55 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 187.29 E-value: 9.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTG--QIVGL-VAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWK 106
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGllIIALLfLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 107 KVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPLG 186
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 187 RKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVII 266
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446376040 267 VGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18545 242 YWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
342-555 |
1.36e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.17 E-value: 1.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYV 421
Cdd:COG4619 1 LELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDGTIRDNI--CYGVEGEVTDAEIEKvAAMAYVdafihDLPNGY-ATEVGErgvkLSGGQRQRIAIARALLRNP 498
Cdd:COG4619 80 PQEPALWGGTVRDNLpfPFQLRERKFDRERAL-ELLERL-----GLPPDIlDKPVER----LSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 499 QILMLDEATSSLDSKSESVVQKALNNLM--KGRTTLVIAH------RLstvvdADKIIFIEKGNL 555
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
342-555 |
8.35e-53 |
|
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: 177.79 E-value: 8.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEY-NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGY 420
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDGTIRDNIcygvegevtdaeiekvaamayvdafihdlpngyatevgergvkLSGGQRQRIAIARALLRNPQI 500
Cdd:cd03246 81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 501 LMLDEATSSLDSKSESVVQKALNNL-MKGRTTLVIAHRLSTVVDADKIIFIEKGNL 555
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
33-318 |
1.94e-52 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 181.20 E-value: 1.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 33 ALLMSLLSTGASLFIPMLT----KGLVDNFSLSSIsTGQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWKKV 108
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTgaviDAVVADGSREAF-YRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 109 LVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPLGRK 188
Cdd:cd18572 80 LRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 189 MYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVIIVG 268
Cdd:cd18572 160 YRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446376040 269 YGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18572 240 YGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
30-318 |
8.48e-51 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 176.83 E-value: 8.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQIVGLVAFFVMQTIAAG----LSIYLLNYIGQKIVAGLRERLW 105
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGifrfLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 106 KKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTalLLTVIPLSVLILVP- 184
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLT--LIALLPLPLLALLVy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 185 -LGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALL 263
Cdd:cd18541 159 rLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 264 VIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18541 239 LIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
342-569 |
8.92e-51 |
|
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: 174.44 E-value: 8.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYV 421
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDsP---LIDGTIRDNICYGVE--GeVTDAEIEKVA--AMAYVDafihdlpngyATEVGERGV-KLSGGQRQRIAIARA 493
Cdd:COG1122 81 FQN-PddqLFAPTVEEDVAFGPEnlG-LPREEIRERVeeALELVG----------LEHLADRPPhELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 494 LLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIA-HRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRTHD 569
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
30-318 |
2.44e-50 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 176.16 E-value: 2.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQI------------------VGLVAFFVMQTIAAGLSIYLLNY 91
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLglapllgpdplallllaaAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 92 IGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALL 171
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 172 LTVIPLSVLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALI 251
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 252 SPVMSfVLMAL-LVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18564 241 SPVVD-VLVAVgTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
72-574 |
5.75e-50 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 186.77 E-value: 5.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 72 VAFFVMQTiaagLSIYLLNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRtgdtisrmtNDTGVVKTLISEHLSNLLTG-- 149
Cdd:PTZ00265 877 IAMFISET----LKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDK---------HAPGLLSAHINRDVHLLKTGlv 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 150 -GISIVGSLIVLFVLDWKMT-------ALLLTVIPLsVLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSN 221
Cdd:PTZ00265 944 nNIVIFTHFIVLFLVSMVMSfyfcpivAAVLTGTYF-IFMRVFAIRARLTANKDVEKKEINQPGTVFAYNSDDEIFKDPS 1022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 222 TEKRE-YETGNTGI------------QKLLQFGLKEGKVQALISPVM-SFVLMALLVI---IVGYGGMRVSSGALTTGEl 284
Cdd:PTZ00265 1023 FLIQEaFYNMNTVIiygledyfcnliEKAIDYSNKGQKRKTLVNSMLwGFSQSAQLFInsfAYWFGSFLIRRGTILVDD- 1101
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 285 vaFILYLVQIIMPMSqlsmFFTQFQKAIGATEriNAILEYE-------------VEDhETGVKVSNA---KQSIVLENVH 348
Cdd:PTZ00265 1102 --FMKSLFTFLFTGS----YAGKLMSLKGDSE--NAKLSFEkyypliirksnidVRD-NGGIRIKNKndiKGKIEIMDVN 1172
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 349 FEY--NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFY------------EPTG------------------ 396
Cdd:PTZ00265 1173 FRYisRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEHTNdmtneqdyqgdeeqnvgm 1252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 397 ------------------------GAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGVEgEVTDAEIEKV 452
Cdd:PTZ00265 1253 knvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE-DATREDVKRA 1331
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 453 AAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRT 530
Cdd:PTZ00265 1332 CKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKT 1411
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 446376040 531 TLVIAHRLSTVVDADKIIFIEKGNLTGS-----GTHDELLRTHD-MYREF 574
Cdd:PTZ00265 1412 IITIAHRIASIKRSDKIVVFNNPDRTGSfvqahGTHEELLSVQDgVYKKY 1461
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
30-318 |
2.07e-48 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 170.36 E-value: 2.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNfSLSSISTGQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAG----LRERLW 105
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDG-PIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGvehdLRTDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 106 KKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISeHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPL 185
Cdd:cd18543 80 AHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 186 GRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVI 265
Cdd:cd18543 159 RRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446376040 266 IVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18543 239 VLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
341-555 |
3.28e-47 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 164.12 E-value: 3.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNED-EKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIG 419
Cdd:cd03369 6 EIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 420 YVSQDSPLIDGTIRDNIcyGVEGEVTDAEIEKvaamayvdafihdlpngyATEVGERGVKLSGGQRQRIAIARALLRNPQ 499
Cdd:cd03369 86 IIPQDPTLFSGTIRSNL--DPFDEYSDEEIYG------------------ALRVSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNL 555
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
27-317 |
3.65e-46 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 164.16 E-value: 3.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 27 KGILVFALLMSLLSTGASLFIPMLTKGLVDNFsLSSISTGQI----VGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRE 102
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPLIVRYIIDDL-LPSKNLRLIliigAILLALYILRTLLNYFVTYWGHVMGARIETDMRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 103 RLWKKVLVLPVSYYDQNRTGDTISRMTNDTgvvkTLISE--H--LSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLS 178
Cdd:cd18549 80 DLFEHLQKLSFSFFDNNKTGQLMSRITNDL----FDISElaHhgPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 179 VLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFV 258
Cdd:cd18549 156 IIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFF 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 259 LMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATER 317
Cdd:cd18549 236 TNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
342-553 |
6.33e-46 |
|
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: 160.71 E-value: 6.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDE----KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKesitsyslqswrrQ 417
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 418 IGYVSQDSPLIDGTIRDNICYGVEgevTDAE-IEKVaamayVDA--FIHDL---PNGYATEVGERGVKLSGGQRQRIAIA 491
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP---FDEErYEKV-----IKAcaLEPDLeilPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446376040 492 RALLRNPQILMLDEATSSLDSK-SESVVQKALN-NLMKGRTTLVIAHRLSTVVDADKIIFIEKG 553
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHvGRHIFENCILgLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
30-318 |
8.51e-46 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 163.34 E-value: 8.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNFSLSS-----ISTGQIVGLVAFFvmQTIAAGLSIYLLNYIGQKIVAGLRERL 104
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGdlsyiLRTGLLMLLLALL--GLIAGILAGYFAAKASQGFGRDLRKDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 105 WKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVP 184
Cdd:cd18548 79 FEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 185 LGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLV 264
Cdd:cd18548 159 IMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446376040 265 IIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18548 239 AILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
342-557 |
9.97e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 160.98 E-value: 9.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDE---KVLNNIDFTIESGKVTAIVGPSGSGKTTLF---SLLERfyePTGGAIKLGKESITSYS---LQ 412
Cdd:COG1136 5 LELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLnilGGLDR---PTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 413 SWRRQ-IGYVSQDSPLIDG-TIRDNICY-----GVEGEVTDAEIEKVAAMAYVDAFIHDLPNgyatevgergvKLSGGQR 485
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPElTALENVALplllaGVSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446376040 486 QRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVDADKIIFIEKGNLTG 557
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
30-298 |
7.86e-45 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 160.12 E-value: 7.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNFS-LSSISTGQI----VGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERL 104
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpDGDPETQALnvysLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 105 WKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVP 184
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 185 LGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLV 264
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 446376040 265 IIVGYGGMRVSSGALTTGELVAFILYLVQIIMPM 298
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
342-580 |
1.08e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 158.30 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQsWRRQIGYV 421
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNI-----CYGVEGEVTDAEIEKVAAMAYVDAFIHDLpngyateVGergvKLSGGQRQRIAIARALL 495
Cdd:COG1131 79 PQEPALYPDlTVRENLrffarLYGLPRKEARERIDELLELFGLTDAADRK-------VG----TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 496 RNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIA-HRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRTH--DMY 571
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKARLleDVF 227
|
....*....
gi 446376040 572 REFATQQLK 580
Cdd:COG1131 228 LELTGEEAR 236
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
343-553 |
5.72e-44 |
|
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: 155.70 E-value: 5.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 343 VLENVHFEY-NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYV 421
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQ--DSPLIDGTIRDNICYGVEGE-VTDAEIEKVAAMAyvdafihdlpngyATEVGERGVK------LSGGQRQRIAIAR 492
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENLgLPEEEIEERVEEA-------------LELVGLEGLRdrspftLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 493 ALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIA-HRLSTVVD-ADKIIFIEKG 553
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDG 210
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
30-318 |
2.11e-43 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 156.88 E-value: 2.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNfSLSSISTGQIVGLVAFFVMQTIAAGL----SIYLLNYIGQKIVAGLRERLW 105
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDS-GVRAGDLGVLLLAAAAYLAVVLAGWVaqraQTRLTGRTGERLLYDLRLRVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 106 KKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPL 185
Cdd:cd18546 80 AHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 186 GRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVI 265
Cdd:cd18546 160 RRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446376040 266 IVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18546 240 VLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
342-565 |
2.76e-43 |
|
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: 155.20 E-value: 2.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYV 421
Cdd:COG1120 2 LEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNICYG------VEGEVTDAEIEKVA-AMAYVDafIHDLPNGYATEvgergvkLSGGQRQRIAIARA 493
Cdd:COG1120 81 PQEPPAPFGlTVRELVALGryphlgLFGRPSAEDREAVEeALERTG--LEHLADRPVDE-------LSGGERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 494 LLRNPQILMLDEATSSLDSKSESVVQKALNNL--MKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELL 565
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
358-508 |
3.69e-43 |
|
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: 151.26 E-value: 3.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDG-TIRDNI 436
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 437 -----CYGVEGEVTDAEIEKVAAMAyvdafihDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATS 508
Cdd:pfam00005 81 rlgllLKGLSKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
342-574 |
7.57e-43 |
|
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: 153.60 E-value: 7.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS---LQSWRRQI 418
Cdd:COG1127 6 IEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 GYVSQDSPLIDG-TIRDNICYGVE--GEVTDAEIEKVAAMAyvdafihdLpngyaTEVGERGVK------LSGGQRQRIA 489
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVAFPLRehTDLSEAEIRELVLEK--------L-----ELVGLPGAAdkmpseLSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSesvvQKALNNLMK------GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHD 562
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPIT----SAVIDELIRelrdelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPE 227
|
250
....*....|...
gi 446376040 563 ELLRTHDMY-REF 574
Cdd:COG1127 228 ELLASDDPWvRQF 240
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
342-564 |
7.90e-43 |
|
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: 153.11 E-value: 7.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYE-----PTGGAIKLGKESITS--YSLQSW 414
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 415 RRQIGYVSQDSPLIDGTIRDNICYGV------EGEVTDAEIEKVAAMAYVDAFIHDLPNGYAtevgergvkLSGGQRQRI 488
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGLrlhgikLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 489 AIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAH------RLstvvdADKIIFIEKGNLTGSGTHD 562
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFGPTE 225
|
..
gi 446376040 563 EL 564
Cdd:cd03260 226 QI 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
342-555 |
7.97e-43 |
|
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: 152.64 E-value: 7.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEK---VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSW---- 414
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 415 RRQIGYVSQDSPLIDG-TIRDNICY-----GVEGEVTDAEIEKVAAMAYVDAFIHDLPNgyatevgergvKLSGGQRQRI 488
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 489 AIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVDADKIIFIEKGNL 555
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-566 |
1.41e-42 |
|
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: 160.07 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDE----KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS---LQSW 414
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 415 RRQIGYVSQD-----SPLIdgTIRDNICYGVE--GEVTDAEI-EKVAAM--------AYVDAFIHDLpngyatevgergv 478
Cdd:COG1123 341 RRRVQMVFQDpysslNPRM--TVGDIIAEPLRlhGLLSRAERrERVAELlervglppDLADRYPHEL------------- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 479 klSGGQRQRIAIARALLRNPQILMLDEATSSLDskseSVVQKALNNLMK------GRTTLVIAHRLSTVVD-ADKIIFIE 551
Cdd:COG1123 406 --SGGQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQILNLLRdlqrelGLTYLFISHDLAVVRYiADRVAVMY 479
|
250
....*....|....*
gi 446376040 552 KGNLTGSGTHDELLR 566
Cdd:COG1123 480 DGRIVEDGPTEEVFA 494
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
27-318 |
2.23e-42 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 154.14 E-value: 2.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 27 KGILVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQIVGLVAFFVMQTIAAGLSI---YLLNYIGQKIVAGLRER 103
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYirsYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 104 LWKKVLVLPVSYYDQNRTGDTISRMtNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILV 183
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 184 PLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALL 263
Cdd:cd18570 160 LFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGS 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 264 VIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18570 240 LLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
30-318 |
4.36e-42 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 153.40 E-value: 4.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLStGASL-FIPMLTKGLVDNFS------------LSSISTgQIVGLVAFFVMQTIAAGLSIYLLNYIGQKI 96
Cdd:cd18577 1 LIIGLLAAIAA-GAALpLMTIVFGDLFDAFTdfgsgesspdefLDDVNK-YALYFVYLGIGSFVLSYIQTACWTITGERQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 97 VAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIP 176
Cdd:cd18577 79 ARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 177 LSVLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMS 256
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446376040 257 FVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
342-574 |
5.58e-42 |
|
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: 151.12 E-value: 5.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS---LQSWRRQI 418
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 GYVSQDSPLIDG-TIRDNICYGV--EGEVTDAEIEKVAAMAYvdafihdlpngyaTEVGERGVK------LSGGQRQRIA 489
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFPLreHTRLSEEEIREIVLEKL-------------EAVGLRGAEdlypaeLSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKALNNL--MKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLR 566
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
....*....
gi 446376040 567 -THDMYREF 574
Cdd:cd03261 227 sDDPLVRQF 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
342-565 |
2.09e-41 |
|
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: 149.62 E-value: 2.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQsWRRQIGYV 421
Cdd:COG4555 2 IEVENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNICY-----GVEGEVTDAEIEKVAAMAYVDAFIHdlpngyatevgERGVKLSGGQRQRIAIARALL 495
Cdd:COG4555 80 PDERGLYDRlTVRENIRYfaelyGLFDEELKKRIEELIELLGLEEFLD-----------RRVGELSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446376040 496 RNPQILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELL 565
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
344-559 |
3.56e-41 |
|
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: 146.81 E-value: 3.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVSQ 423
Cdd:cd03214 2 VENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 424 dsplidgtirdnicygvegevtdaeiekvaAMAYVDafIHDLPNGYATEvgergvkLSGGQRQRIAIARALLRNPQILML 503
Cdd:cd03214 81 ------------------------------ALELLG--LAHLADRPFNE-------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 504 DEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSG 559
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-574 |
5.70e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 148.70 E-value: 5.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYslqswRRQIGYV 421
Cdd:COG1121 7 IELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQ------DSPLidgTIRDNICYGVEGEV------TDAEIEKV-AAMAYVDAFihdlpnGYATE-VGErgvkLSGGQRQR 487
Cdd:COG1121 81 PQraevdwDFPI---TVRDVVLMGRYGRRglfrrpSRADREAVdEALERVGLE------DLADRpIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 488 IAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNL-MKGRTTLVIAHRLSTVVD-ADKIIFIEKGnLTGSGTHDELL 565
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRG-LVAHGPPEEVL 226
|
....*....
gi 446376040 566 RTHDMYREF 574
Cdd:COG1121 227 TPENLSRAY 235
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
16-505 |
9.80e-41 |
|
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: 155.34 E-value: 9.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 16 FLRLIRDTNPPkgILVFALLMSLLSTGAS-LFIPMLTKGLVDNFSLSSISTGQIVGLVAFFVmqtIAAGLSIYLLNYIGQ 94
Cdd:COG4615 3 LLRLLLRESRW--LLLLALLLGLLSGLANaGLIALINQALNATGAALARLLLLFAGLLVLLL---LSRLASQLLLTRLGQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 95 KIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVkTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTV 174
Cdd:COG4615 78 HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 175 IPLSVLILVPLGRKMYK-ISKALQDETASFTSV--LTQVLSEIRLvkssNTEKR------EYETGNTGIQKLLQFGLKEG 245
Cdd:COG4615 157 LGLGVAGYRLLVRRARRhLRRAREAEDRLFKHFraLLEGFKELKL----NRRRRraffdeDLQPTAERYRDLRIRADTIF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 246 KVQALISPVMSFVLMALLVIIVgyggmrVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINAI--LE 323
Cdd:COG4615 233 ALANNWGNLLFFALIGLILFLL------PALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELelAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 324 YEVEDHETGVKVSNAK---QSIVLENVHFEY-NEDEK---VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTG 396
Cdd:COG4615 307 AAAEPAAADAAAPPAPadfQTLELRGVTYRYpGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPES 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 397 GAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTirdnicYGVEGEVTDAEiekvaamayVDAFIHDLpnGYATEVGER 476
Cdd:COG4615 387 GEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEADPAR---------ARELLERL--ELDHKVSVE 449
|
490 500 510
....*....|....*....|....*....|....
gi 446376040 477 G-----VKLSGGQRQRIAIARALLRNPQILMLDE 505
Cdd:COG4615 450 DgrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
344-553 |
2.34e-40 |
|
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: 143.92 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYNEDeKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVSQ 423
Cdd:cd00267 2 IENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 424 dsplidgtirdnicygvegevtdaeiekvaamayvdafihdlpngyatevgergvkLSGGQRQRIAIARALLRNPQILML 503
Cdd:cd00267 81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446376040 504 DEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVDA-DKIIFIEKG 553
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
342-559 |
2.40e-40 |
|
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: 144.76 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEY-NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSlQSWRRQIGY 420
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDGTIRDNIcygvegevtdaeiekvaamayvdafihdlpngyatevgerGVKLSGGQRQRIAIARALLRNPQI 500
Cdd:cd03247 80 LNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 501 LMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSG 559
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
30-318 |
2.64e-40 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 148.40 E-value: 2.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVD------NFSLSSISTGQIVGLVAffvmqtIAAGLSI---YLLNYIGQKIVAGL 100
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDdalpqgDLGLLVLLALGMVAVAV------ASALLGVvqtYLSARIGQGVMYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 101 RERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVL 180
Cdd:cd18550 75 RVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 181 ILVPLGRKMYKISKALQDETASFTSVLTQVLSE--IRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFV 258
Cdd:cd18550 155 PTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLF 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 259 LMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18550 235 TAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
342-564 |
3.14e-39 |
|
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: 143.86 E-value: 3.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS---LQSWRRQI 418
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 GYVSQDSPLIDG-TIRDNICYGVEGEVTD--------AEIEKVAAMAYVDAFihdlpnGYATEVGERGVKLSGGQRQRIA 489
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRRSTwrslfglfPKEEKQRALAALERV------GLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKAL--NNLMKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDEL 564
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
66-583 |
9.31e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 152.82 E-value: 9.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 66 GQIVGLVAFFVMQTIAAGLSIYLLNY--IGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKtLISEHL 143
Cdd:PLN03232 340 GYVYAFLIFFGVTFGVLCESQYFQNVgrVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQ-QIAEQL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 144 SNLLTGGISIVGSLIVLF----VLDWKMTALLLTVIPLSVLILvplgRKMYKISKALQDETASFTSVLTQVLSEIRLVKS 219
Cdd:PLN03232 419 HGLWSAPFRIIVSMVLLYqqlgVASLFGSLILFLLIPLQTLIV----RKMRKLTKEGLQWTDKRVGIINEILASMDTVKC 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 220 SNTEKreyeTGNTGIQKLLQFGLKEGKVQALISPVMSFVL--MALLVIIVGYGGMRVSSGALTTGElvAFI-LYLVQII- 295
Cdd:PLN03232 495 YAWEK----SFESRIQGIRNEELSWFRKAQLLSAFNSFILnsIPVVVTLVSFGVFVLLGGDLTPAR--AFTsLSLFAVLr 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 296 MPMSQLSMFFTQFQKAIGATERINAILEYEVEDHETGVKVSNAKQSIVLENVHFEYNE--DEKVLNNIDFTIESGKVTAI 373
Cdd:PLN03232 569 SPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFSWDSktSKPTLSDINLEIPVGSLVAI 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 374 VGPSGSGKTTLFSLLerfyeptggaikLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNICYGvegevTDAEIEKVA 453
Cdd:PLN03232 649 VGGTGEGKTSLISAM------------LGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFG-----SDFESERYW 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 454 AMAYVDAFIHDL---PNGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSK-SESVVQKALNNLMKGR 529
Cdd:PLN03232 712 RAIDVTALQHDLdllPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGK 791
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446376040 530 TTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHDMYREFATQQLKIKE 583
Cdd:PLN03232 792 TRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDA 845
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
342-553 |
1.06e-38 |
|
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: 140.01 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEdEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQS--WRRQIG 419
Cdd:cd03229 1 LELKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 420 YVSQDSPLIDG-TIRDNICYGvegevtdaeiekvaamayvdafihdlpngyatevgergvkLSGGQRQRIAIARALLRNP 498
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG----------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 499 QILMLDEATSSLDSKSESVVQKALNNL--MKGRTTLVIAHRLSTVVD-ADKIIFIEKG 553
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
337-565 |
1.59e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 142.82 E-value: 1.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 337 NAKQSIVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWR 415
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 416 RQIGYVSQ--DSPLIDGTIRDNICYGVEG-----EVTDAEIEKVAAMAYVDAFIHDLPNgyatevgergvKLSGGQRQRI 488
Cdd:PRK13632 83 KKIGIIFQnpDNQFIGATVEDDIAFGLENkkvppKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 489 AIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRT-TLV-IAHRLSTVVDADKIIFIEKGNLTGSGTHDELL 565
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
100-575 |
1.70e-38 |
|
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: 152.02 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 100 LRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLfvldwkmtallLTVIPLSV 179
Cdd:TIGR00957 1040 LHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVI-----------LLATPIAA 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 180 LILVPLG------RKMYKIS----KALQDETAS-FTSVLTQVLSEIRLVKSSNtEKREYEtgntgiqklLQFGLKEGKVQ 248
Cdd:TIGR00957 1109 VIIPPLGllyffvQRFYVASsrqlKRLESVSRSpVYSHFNETLLGVSVIRAFE-EQERFI---------HQSDLKVDENQ 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 249 ALISP-VMSFVLMALLVIIVG-----YGGM--RVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERINA 320
Cdd:TIGR00957 1179 KAYYPsIVANRWLAVRLECVGncivlFAALfaVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 321 ILEYEVED----HETGVKVSNAKQSIV-LENVHFEYNED-EKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEP 394
Cdd:TIGR00957 1259 YSETEKEApwqiQETAPPSGWPPRGRVeFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINES 1338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 395 TGGAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNIcyGVEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVG 474
Cdd:TIGR00957 1339 AEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL--DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECA 1416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 475 ERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGN 554
Cdd:TIGR00957 1417 EGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGE 1496
|
490 500
....*....|....*....|.
gi 446376040 555 LTGSGTHDELLRTHDMYREFA 575
Cdd:TIGR00957 1497 VAEFGAPSNLLQQRGIFYSMA 1517
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
342-548 |
1.94e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 141.73 E-value: 1.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS---LQSWRRQI 418
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 GYVSQDSPLIDG-TIRDNICYGVEGEV----------TDAEIEKvaAMAYVDAFihdlpnGYATEVGERGVKLSGGQRQR 487
Cdd:COG3638 83 GMIFQQFNLVPRlSVLTNVLAGRLGRTstwrsllglfPPEDRER--ALEALERV------GLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446376040 488 IAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKII 548
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRII 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
346-555 |
3.51e-38 |
|
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: 140.33 E-value: 3.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 346 NVHF-EYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS---LQSWRRQIGYV 421
Cdd:cd03257 8 SVSFpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDS-----PLIdgTIRDNIC---YGVEGEVTDAEIEKVAAMAYV-----DAFIHDLPNgyatevgergvKLSGGQRQRI 488
Cdd:cd03257 88 FQDPmsslnPRM--TIGEQIAeplRIHGKLSKKEARKEAVLLLLVgvglpEEVLNRYPH-----------ELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446376040 489 AIARALLRNPQILMLDEATSSLDskseSVVQKALNNLMK------GRTTLVIAHRLSTVVD-ADKIIFIEKGNL 555
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALD----VSVQAQILDLLKklqeelGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
342-555 |
3.64e-38 |
|
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: 139.96 E-value: 3.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDeKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITsySLQSWRRQIGYV 421
Cdd:cd03259 1 LELKGLSKTYGSV-RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNICYGVE-GEVTDAEIEKVAAMAYVDAFIHDLPNGYATEvgergvkLSGGQRQRIAIARALLRNPQ 499
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGLKlRGVPKAEIRARVRELLELVGLEGLLNRYPHE-------LSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNL 555
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRI 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
342-579 |
7.06e-38 |
|
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: 140.32 E-value: 7.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEY---NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQI 418
Cdd:COG1124 2 LEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 GYVSQDS-----PLidGTIRDNI-----CYGVegevTDAEIEKVAAMAYVDafihdLPNGYATEvgeRGVKLSGGQRQRI 488
Cdd:COG1124 82 QMVFQDPyaslhPR--HTVDRILaeplrIHGL----PDREERIAELLEQVG-----LPPSFLDR---YPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 489 AIARALLRNPQILMLDEATSSLDskseSVVQKALNNLMK------GRTTLVIAHRLStVVD--ADKIIFIEKGNLTGSGT 560
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALD----VSVQAEILNLLKdlreerGLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELT 222
|
250
....*....|....*....
gi 446376040 561 HDELLRTHdmyREFATQQL 579
Cdd:COG1124 223 VADLLAGP---KHPYTREL 238
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-318 |
1.18e-37 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 141.08 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 27 KGILVFALLMSLLSTGASLFIPMLTKGLVDNF----SLSSIsTGQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRE 102
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFitpgTLDGL-TGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 103 RLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLIL 182
Cdd:cd18540 80 KAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 183 VPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMAL 262
Cdd:cd18540 160 IYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 263 LVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18540 240 TALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
342-574 |
1.24e-37 |
|
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: 139.36 E-value: 1.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYV 421
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNICY--GVEGEVTDAEIEKVA-AMAYVDAFIHDLPNGYATEvgergvkLSGGQRQRIAIARALLRN 497
Cdd:cd03295 81 IQQIGLFPHmTVEENIALvpKLLKWPKEKIRERADeLLALVGLDPAEFADRYPHE-------LSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 498 PQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRL-STVVDADKIIFIEKGNLTGSGTHDELLRT--HDMYR 572
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSpaNDFVA 233
|
..
gi 446376040 573 EF 574
Cdd:cd03295 234 EF 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
342-555 |
2.12e-37 |
|
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: 136.37 E-value: 2.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQsWRRQIGYV 421
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNIcygvegevtdaeiekvaamayvdafihdlpngyatevgergvKLSGGQRQRIAIARALLRNPQI 500
Cdd:cd03230 79 PEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 501 LMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKIIFIEKGNL 555
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
341-566 |
2.73e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.77 E-value: 2.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSysLQSWRRQIGY 420
Cdd:COG3842 5 ALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG--LPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLid-gTIRDNICYGVEGE-VTDAEI-EKVAAM-------AYVDAFIHDLpngyatevgergvklSGGQRQRIAI 490
Cdd:COG3842 82 VFQDYALfphlTVAENVAFGLRMRgVPKAEIrARVAELlelvgleGLADRYPHQL---------------SGGQQQRVAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 491 ARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHrlstvvD-------ADKIIFIEKGNLTGSGTH 561
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTH------DqeealalADRIAVMNDGRIEQVGTP 220
|
....*
gi 446376040 562 DELLR 566
Cdd:COG3842 221 EEIYE 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
100-565 |
2.79e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 148.59 E-value: 2.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 100 LRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVvktlISEHLSNLLTGGISIVGSLIVLFVLDWKMTAL-LLTVIPLS 178
Cdd:PLN03232 985 LHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGD----IDRNVANLMNMFMNQLWQLLSTFALIGTVSTIsLWAIMPLL 1060
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 179 VLILVPL------GRKMYKISKALQDET-ASFTSVLTQvLSEIRLVKSSNtekREYETGNTGIQKLLQFGL---KEGKVQ 248
Cdd:PLN03232 1061 ILFYAAYlyyqstSREVRRLDSVTRSPIyAQFGEALNG-LSSIRAYKAYD---RMAKINGKSMDNNIRFTLantSSNRWL 1136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 249 ALISPVMSFVLMALLVI--IVGYGGMRVSSG-ALTTGELVAFILYLVQIimpmsqLSMFFTQFQKA---IGATERINAIL 322
Cdd:PLN03232 1137 TIRLETLGGVMIWLTATfaVLRNGNAENQAGfASTMGLLLSYTLNITTL------LSGVLRQASKAensLNSVERVGNYI 1210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 323 EYEVEdhETGVKVSN-------AKQSIVLENVHFEYN-EDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEP 394
Cdd:PLN03232 1211 DLPSE--ATAIIENNrpvsgwpSRGSIKFEDVHLRYRpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVEL 1288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 395 TGGAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNIcyGVEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVG 474
Cdd:PLN03232 1289 EKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI--DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVS 1366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 475 ERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGN 554
Cdd:PLN03232 1367 EGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQ 1446
|
490
....*....|.
gi 446376040 555 LTGSGTHDELL 565
Cdd:PLN03232 1447 VLEYDSPQELL 1457
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
344-553 |
4.72e-37 |
|
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: 136.89 E-value: 4.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITsyslQSWRRqIGYVSQ 423
Cdd:cd03235 2 VEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE----KERKR-IGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 424 ------DSPLidgTIRDNICYGVEGE------VTDAEIEKV-AAMAYVDAfihdlpngyaTEVGERGV-KLSGGQRQRIA 489
Cdd:cd03235 76 rrsidrDFPI---SVRDVVLMGLYGHkglfrrLSKADKAKVdEALERVGL----------SELADRQIgELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKALNNL-MKGRTTLVIAHRLSTVVD-ADKIIFIEKG 553
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-570 |
3.56e-36 |
|
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: 141.96 E-value: 3.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTG---GAIKLGKESITSYSLQSWRRQ 417
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 418 IGYVSQD--SPLIDGTIRDNICYGVE-GEVTDAEIEKVAAMAYVDAFIHDLPNGYATEvgergvkLSGGQRQRIAIARAL 494
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEALEnLGLSRAEARARVLELLEAVGLERRLDRYPHQ-------LSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 495 LRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRTHDM 570
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
33-318 |
7.10e-36 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 136.14 E-value: 7.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 33 ALLMSLLSTGASLFIPMLTKGLVDNFSLS-SISTGQIVG--------LVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRER 103
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNVISRSlKETNGDFIEdlkkpalkLLGLYLLQSLLTFAYISLLSVVGERVAARLRND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 104 LWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILV 183
Cdd:cd18574 81 LFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 184 PLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQ----FGLKEGKVQALispvMSFVL 259
Cdd:cd18574 161 LYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKlnekLGLGIGIFQGL----SNLAL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 260 MALLVIIVGYGGMRVSSGALTTGELVAFILYlVQIIM-PMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18574 237 NGIVLGVLYYGGSLVSRGELTAGDLMSFLVA-TQTIQrSLAQLSVLFGQYVKGKSAGARV 295
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
342-565 |
1.49e-35 |
|
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: 133.48 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEY---NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTL---FSLLERfyePTGGAIKLGKESITSYS---LQ 412
Cdd:cd03258 2 IELKNVSKVFgdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 413 SWRRQIGYVSQDSPLIDG-TIRDNICYGVEgevtdaeIEKVAaMAYVDAFIHDLPN--GYATEVGERGVKLSGGQRQRIA 489
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALPLE-------IAGVP-KAEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELL 565
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
342-548 |
1.82e-35 |
|
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: 132.60 E-value: 1.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEY---NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSlqswrRQI 418
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 GYVSQDSPLID-GTIRDNICYGVEGEVTDAEIEKVAAMAYVDA-----FIHDLPNgyatevgergvKLSGGQRQRIAIAR 492
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEELLELvglsgFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 493 ALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKII 548
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDEAVFlADRVV 203
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
336-536 |
1.84e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 134.06 E-value: 1.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 336 SNAKQSIVLENVHFEYNEDEK---VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSlq 412
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGgvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 413 swrRQIGYVSQDspliDG-----TIRDNICYGVEGE-VTDAEIEKvAAMAYVD-----AFIHDLPNgyatevgergvKLS 481
Cdd:COG1116 80 ---PDRGVVFQE----PAllpwlTVLDNVALGLELRgVPKAERRE-RARELLElvglaGFEDAYPH-----------QLS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 482 GGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAH 536
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTH 197
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
342-574 |
4.77e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 132.04 E-value: 4.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTL---FSLLErfyEPTGGAIKLGKESIT--SYSLQSWRR 416
Cdd:COG1126 2 IEIENLHKSFG-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLE---EPDSGTITVDGEDLTdsKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 417 QIGYVSQDSPLI-DGTIRDNICYG---VEGeVTDAEIEKVAaMAYVDAF-IHDLPNGYATEvgergvkLSGGQRQRIAIA 491
Cdd:COG1126 78 KVGMVFQQFNLFpHLTVLENVTLApikVKK-MSKAEAEERA-MELLERVgLADKADAYPAQ-------LSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 492 RALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLS---TVvdADKIIFIEKGNLTGSGTHDELLR- 566
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKeGMTMVVVTHEMGfarEV--ADRVVFMDGGRIVEEGPPEEFFEn 226
|
....*....
gi 446376040 567 -THDMYREF 574
Cdd:COG1126 227 pQHERTRAF 235
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
341-566 |
1.02e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 134.12 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSL---LERfyePTGGAIKLGKESITSySLQSWRRQ 417
Cdd:COG1118 2 SIEVRNISKRFG-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFT-NLPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 418 IGYVSQDSPLI-DGTIRDNICYGVE-GEVTDAEIEKVAaMAYVDAF-IHDLPNGYATEvgergvkLSGGQRQRIAIARAL 494
Cdd:COG1118 77 VGFVFQHYALFpHMTVAENIAFGLRvRPPSKAEIRARV-EELLELVqLEGLADRYPSQ-------LSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 495 LRNPQILMLDEATSSLDSKsesvVQKAL-NNLMK-----GRTTLVIAH------RLstvvdADKIIFIEKGNLTGSGTHD 562
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAK----VRKELrRWLRRlhdelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPD 219
|
....
gi 446376040 563 ELLR 566
Cdd:COG1118 220 EVYD 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
337-573 |
1.73e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.68 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 337 NAKQSIVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWR 415
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 416 RQIGYVSQ--DSPLIDGTIRDNICYGVE--GEVTDAEIEKV-AAMAYV--DAFIHDLPNgyatevgergvKLSGGQRQRI 488
Cdd:PRK13635 81 RQVGMVFQnpDNQFVGATVQDDVAFGLEniGVPREEMVERVdQALRQVgmEDFLNREPH-----------RLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 489 AIARALLRNPQILMLDEATSSLDSKSESVVQKALNNL--MKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLR 566
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
....*..
gi 446376040 567 THDMYRE 573
Cdd:PRK13635 230 SGHMLQE 236
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
27-318 |
2.37e-34 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 131.86 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 27 KGILVFALLMSLLSTGASLFIPMLTKGLVDNfslssISTGQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWK 106
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDN-----VIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 107 --------KVLVLPVSYYDQNRTGDTISRMtNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLS 178
Cdd:cd18555 76 slmsdffeHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 179 VLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFV 258
Cdd:cd18555 155 VLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSI 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 259 LMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18555 235 QFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
342-559 |
3.43e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.40 E-value: 3.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS---LQSWRRQI 418
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 GYVSQDSPLIDG-TIRDNICYG--VEGeVTDAEIEK--VAAMAYVD--AFIHDLPNgyatevgergvKLSGGQRQRIAIA 491
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALPlrVTG-KSRKEIRRrvREVLDLVGlsDKAKALPH-----------ELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 492 RALLRNPQILMLDEATSSLDSK-SESVVQ--KALNNLmkGrTTLVIA-HRLSTVVDADK-IIFIEKGNLTGSG 559
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPEtSWEIMEllEEINRR--G-TTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
341-513 |
3.59e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.19 E-value: 3.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSysLQSWRRQIGY 420
Cdd:COG3839 3 SLELENVSKSYGGVE-ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD--LPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDG-TIRDNICYG-----VEGEVTDAEIEKVAAMAYVDAFIHDLPNGyatevgergvkLSGGQRQRIAIARAL 494
Cdd:COG3839 80 VFQSYALYPHmTVYENIAFPlklrkVPKAEIDRRVREAAELLGLEDLLDRKPKQ-----------LSGGQRQRVALGRAL 148
|
170
....*....|....*....
gi 446376040 495 LRNPQILMLDEATSSLDSK 513
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAK 167
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
342-574 |
4.29e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 129.43 E-value: 4.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEY---NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTL---FSLLERfyePTGGAIKLGKESITSYS---LQ 412
Cdd:COG1135 2 IELENLSKTFptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLircINLLER---PTSGSVLVDGVDLTALSereLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 413 SWRRQIGYVSQDSPLIDG-TIRDNICYGVEGE-VTDAEI-EKVAAM-AYVD--AFIHDLPNgyatevgergvKLSGGQRQ 486
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVALPLEIAgVPKAEIrKRVAELlELVGlsDKADAYPS-----------QLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 487 RIAIARALLRNPQILMLDEATSSLDSKS-ESVVQ--KALNNLMkGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHD 562
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETtRSILDllKDINREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVL 226
|
250
....*....|....
gi 446376040 563 ELLRT--HDMYREF 574
Cdd:COG1135 227 DVFANpqSELTRRF 240
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
341-567 |
4.45e-33 |
|
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: 126.68 E-value: 4.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQswRRQIGY 420
Cdd:cd03296 2 SIEVRNVSKRFG-DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDG-TIRDNICYGVE-----GEVTDAEI-EKVAA---MAYVDAFIHDLPNgyatevgergvKLSGGQRQRIAI 490
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAFGLRvkprsERPPEAEIrAKVHEllkLVQLDWLADRYPA-----------QLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 491 ARALLRNPQILMLDEATSSLDSKsesvVQKALNNLMK------GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDE 563
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAK----VRKELRRWLRrlhdelHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDE 223
|
....
gi 446376040 564 LLRT 567
Cdd:cd03296 224 VYDH 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
341-565 |
7.58e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 134.87 E-value: 7.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNED-EKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIG 419
Cdd:PLN03130 1237 SIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 420 YVSQDSPLIDGTIRDNIcyGVEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQ 499
Cdd:PLN03130 1317 IIPQAPVLFSGTVRFNL--DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELL 565
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
336-555 |
1.11e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.92 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 336 SNAKQSIVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGA-----IKLGKESI--TS 408
Cdd:COG1117 6 STLEPKIEVRNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 409 YSLQSWRRQIGYVSQDS---PLidgTIRDNICYGVE--GEVTDAEIEKVAAMAYVDAFIHDlpngyatEVGER----GVK 479
Cdd:COG1117 85 VDVVELRRRVGMVFQKPnpfPK---SIYDNVAYGLRlhGIKSKSELDEIVEESLRKAALWD-------EVKDRlkksALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 480 LSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLmKGRTTLVI-------AHRLStvvdaDKIIFIEK 552
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIvthnmqqAARVS-----DYTAFFYL 228
|
...
gi 446376040 553 GNL 555
Cdd:COG1117 229 GEL 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
342-569 |
1.25e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 125.25 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKvlnNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSlqSWRRQIGYV 421
Cdd:COG3840 2 LRLDDLTYRYGDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP--PAERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNICYGVE--GEVTDAEIEKVAAMAY---VDAFIHDLPNgyatevgergvKLSGGQRQRIAIARALL 495
Cdd:COG3840 77 FQENNLFPHlTVAQNIGLGLRpgLKLTAEQRAQVEQALErvgLAGLLDRLPG-----------QLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 496 RNPQILMLDEATSSLDSksesvvqkALNNLM----------KGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDEL 564
Cdd:COG3840 146 RKRPILLLDEPFSALDP--------ALRQEMldlvdelcreRGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
....*
gi 446376040 565 LRTHD 569
Cdd:COG3840 218 LDGEP 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
342-553 |
2.06e-32 |
|
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: 124.18 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESIT--SYSLQSWRRQIG 419
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 420 YVSQDSPLIDG-TIRDNICYG---VEGEVTDAEIEKvaAMAYVD-----AFIHDLPNgyatevgergvKLSGGQRQRIAI 490
Cdd:cd03262 80 MVFQQFNLFPHlTVLENITLApikVKGMSKAEAEER--ALELLEkvglaDKADAYPA-----------QLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 491 ARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKIIFIEKG 553
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
342-574 |
3.28e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 124.48 E-value: 3.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESI-TSYSL-------QS 413
Cdd:PRK11264 4 IEVKNLVKKFH-GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLsqqkgliRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 414 WRRQIGYVSQDSPLI-DGTIRDNIcygVEGEVTDAEIEKVAAMAYVDAFIHDLpnGYATEVGERGVKLSGGQRQRIAIAR 492
Cdd:PRK11264 83 LRQHVGFVFQNFNLFpHRTVLENI---IEGPVIVKGEPKEEATARARELLAKV--GLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 493 ALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVI-AHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLR--TH 568
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIvTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAdpQQ 237
|
....*.
gi 446376040 569 DMYREF 574
Cdd:PRK11264 238 PRTRQF 243
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
38-318 |
9.09e-32 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 124.35 E-value: 9.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 38 LLSTGASLFIPMLT----KGLVDNFSLSSISTGQI-VGLVAFfvMQTIAAGLSIYLLNYIGQKIVAGLRERLWKKVLVLP 112
Cdd:cd18784 6 LAAAVGEIFIPYYTgqviDGIVIEKSQDKFSRAIIiMGLLAI--ASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 113 VSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLsVLILVPLGRKMY-K 191
Cdd:cd18784 84 IGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPL-IAIVSKVYGDYYkK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 192 ISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVIIVGYGG 271
Cdd:cd18784 163 LSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446376040 272 MRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18784 243 HLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
342-564 |
3.08e-31 |
|
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: 121.19 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSysLQSWRRQIGYV 421
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNICYG-----VEGEVTDAEIEKVAAMAYVDAFIHDLPNgyatevgergvKLSGGQRQRIAIARALL 495
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlrlkkLPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446376040 496 RNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLS-TVVDADKIIFIEKGNLTGSGTHDEL 564
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
30-318 |
3.49e-31 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 123.45 E-value: 3.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLfIPMLTKGL-VDNFSLSSIS--------------TGQIVGLVAF----FVMQTIAAGLSIYLLN 90
Cdd:cd18565 1 LVLGLLASILNRLFDL-APPLLIGVaIDAVFNGEASflplvpaslgpadpRGQLWLLGGLtvaaFLLESLFQYLSGVLWR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 91 YIGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTAL 170
Cdd:cd18565 80 RFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 171 LLTVIPLSVLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQAL 250
Cdd:cd18565 160 ALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446376040 251 ISPVMSFVLMALLVIIVGYGGMRV------SSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18565 240 FFPVIRLVAGAGFVATFVVGGYWVldgpplFTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
121-564 |
4.62e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 129.47 E-value: 4.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 121 TGDTISRMTNDTGVVKTlISEHLSNLLTGGISIVGSLIVLF----VLDWKMTALLLTVIPLSVLILvplgRKMYKISKAL 196
Cdd:PLN03130 397 SGKITNLMTTDAEALQQ-ICQQLHTLWSAPFRIIIAMVLLYqqlgVASLIGSLMLVLMFPIQTFII----SKMQKLTKEG 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 197 QDETASFTSVLTQVLSEIRLVKSSNTEKreyeTGNTGIQKLLQFGLKEGKVQALISPVMSFVL--MALLVIIVGYGGMRV 274
Cdd:PLN03130 472 LQRTDKRIGLMNEVLAAMDTVKCYAWEN----SFQSKVQTVRDDELSWFRKAQLLSAFNSFILnsIPVLVTVVSFGVFTL 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 275 SSGALTTGElvAFI-LYLVQII-MPMSQLSMFFTQFQKAIGATERINAILEYEVEDHETGVKVSNAKQSIVLENVHFEYN 352
Cdd:PLN03130 548 LGGDLTPAR--AFTsLSLFAVLrFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGLPAISIKNGYFSWD 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 353 E--DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLerfyeptggaikLGKESITSYSLQSWRRQIGYVSQDSPLIDG 430
Cdd:PLN03130 626 SkaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM------------LGELPPRSDASVVIRGTVAYVPQVSWIFNA 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 TIRDNICYGvegevTDAEIEKVAAMAYVDAFIHDL---PNGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEAT 507
Cdd:PLN03130 694 TVRDNILFG-----SPFDPERYERAIDVTALQHDLdllPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 508 SSLDSK-SESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDEL 564
Cdd:PLN03130 769 SALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-574 |
7.71e-31 |
|
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: 128.91 E-value: 7.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 21 RDTNPpkgilvfALLMSLLST-GASLFIPMLTKGLVDnfsLSSISTGQIVGLVAFFVMQTIA--------AGL------- 84
Cdd:TIGR00957 301 KPRKP-------SLFKVLYKTfGPYFLMSFCFKAIHD---LMMFIGPQILSLLIRFVNDPMApdwqgyfyTGLlfvcacl 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 85 -SIYLLNYIGQKIVAGLRER------LWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLiSEHLSNLLTGGISIVgsl 157
Cdd:TIGR00957 371 qTLILHQYFHICFVSGMRIKtavmgaVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDL-ATYINMIWSAPLQVI--- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 158 IVLFVLDWKMTALLLTVIPLSVLiLVPLGRKMYKISKALQ----DETASFTSVLTQVLSEIRLVKSSNTEKrEYETGNTG 233
Cdd:TIGR00957 447 LALYFLWLNLGPSVLAGVAVMVL-MVPLNAVMAMKTKTYQvahmKSKDNRIKLMNEILNGIKVLKLYAWEL-AFLDKVEG 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 234 IQkllQFGLKEGKVQALISPVMSFVLMA---LLVIIVGYGGMRVSSGALTTGELVAFILYLVQII-MPMSQLSMFFTQFQ 309
Cdd:TIGR00957 525 IR---QEELKVLKKSAYLHAVGTFTWVCtpfLVALITFAVYVTVDENNILDAEKAFVSLALFNILrFPLNILPMVISSIV 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 310 KAIGATERINAIL---EYEVEDHETGVKVSNAKQSIVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLF 385
Cdd:TIGR00957 602 QASVSLKRLRIFLsheELEPDSIERRTIKPGEGNSITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLL 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 386 SLLERFYEPTGGAIKLgkesitsyslqswRRQIGYVSQDSPLIDGTIRDNICYG--VEGEVTDAEIEKVAAMAYVDAfih 463
Cdd:TIGR00957 682 SALLAEMDKVEGHVHM-------------KGSVAYVPQQAWIQNDSLRENILFGkaLNEKYYQQVLEACALLPDLEI--- 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 464 dLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSK-SESVVQKALN--NLMKGRTTLVIAHRLST 540
Cdd:TIGR00957 746 -LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGpeGVLKNKTRILVTHGISY 824
|
570 580 590
....*....|....*....|....*....|....
gi 446376040 541 VVDADKIIFIEKGNLTGSGTHDELLRTHDMYREF 574
Cdd:TIGR00957 825 LPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
361-586 |
1.11e-30 |
|
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: 122.91 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 361 IDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS----LQSWRRQIGYVSQDSPLIDG-TIRDN 435
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgifLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 436 ICYGV---EGEVTDAEIEKVAAMAYVDAFIHDLPNgyatevgergvKLSGGQRQRIAIARALLRNPQILMLDEATSSLDS 512
Cdd:TIGR02142 96 LRYGMkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 513 KSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRTHDMYREFATQQLKIKEGAL 586
Cdd:TIGR02142 165 PRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSLIEGVV 241
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
10-537 |
1.44e-30 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 126.08 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 10 KGSWRQFLRLIR------DTNPPKGILVFALLMSLLSTGASLFIPMLTKGLVDnfSLSSISTGQIVGLVA-FFVMQTIAA 82
Cdd:COG4178 1 RSLLRQFWRLARpywrseEKWKAWGLLALLLLLTLASVGLNVLLNFWNRDFYD--ALQARDAAAFWQQLGvFALLAAISI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 83 GLSIYLLnYIGQKIVAGLRERLWKKVLVL---PVSYYDQNRTGDTIS----RMTNDtgvVKTLISEHLSnLLTGGISIVG 155
Cdd:COG4178 79 LLAVYQT-YLRQRLQIRWREWLTERLLDRwlsNRAYYRLQLSGGEIDnpdqRIAED---IRLFTETTLS-LSLGLLSSVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 156 SLI---------------VLFVLDWK----MTALLLTVIPLSVLILVPLGRKMYKISKALQDETASFTSVLTQVL--SE- 213
Cdd:COG4178 154 TLIsfigilwslsgsltfTLGGYSITipgyMVWAALIYAIIGTLLTHLIGRPLIRLNFEQQRREADFRFALVRVRenAEs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 214 IRLVKSSNTEKREYET------GN----TGIQKLLQFglkegkVQA---LISPVMSFVLMALLVIivgyggmrvsSGALT 280
Cdd:COG4178 234 IALYRGEAAERRRLRRrfdaviANwrrlIRRQRNLTF------FTTgygQLAVIFPILVAAPRYF----------AGEIT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 281 TGELVafilylvqiimpmsQLSMFFTQFQKAIG-------------AT-ERI----NAILEYEVEDHETGVKVSNAKQSI 342
Cdd:COG4178 298 LGGLM--------------QAASAFGQVQGALSwfvdnyqslaewrATvDRLagfeEALEAADALPEAASRIETSEDGAL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 343 VLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKL--GKESItsyslqswrrqigY 420
Cdd:COG4178 364 ALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVL-------------F 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDGTIRDNICY-GVEGEVTDAEIEKVAAMAYVDAFIHDLpngyaTEVGERGVKLSGGQRQRIAIARALLRNPQ 499
Cdd:COG4178 431 LPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPD 505
|
570 580 590
....*....|....*....|....*....|....*...
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHR 537
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
342-567 |
2.06e-30 |
|
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: 118.98 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEkvLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSysLQSWRRQIGYV 421
Cdd:cd03299 1 LKVENLSKDWKEFK--LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNICYG-----VEGEVTDAEIEKVAAMAYVDAFIHDLPNgyatevgergvKLSGGQRQRIAIARALL 495
Cdd:cd03299 77 PQNYALFPHmTVYKNIAYGlkkrkVDKKEIERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 496 RNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTV-VDADKIIFIEKGNLTGSGTHDELLRT 567
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
342-555 |
2.95e-30 |
|
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: 117.89 E-value: 2.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSY---SLQSWRRQI 418
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 GYVSQDSPLI-DGTIRDNICYGVEgeVTDA---EIEK--VAAMAYVD--AFIHDLPNGyatevgergvkLSGGQRQRIAI 490
Cdd:cd03292 81 GVVFQDFRLLpDRNVYENVAFALE--VTGVpprEIRKrvPAALELVGlsHKHRALPAE-----------LSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 491 ARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADK--IIFIEKGNL 555
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
356-541 |
3.19e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 120.99 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS---LQSWRRQIGYVSQDS-----PL 427
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPyaslnPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 428 IdgTIRDNICYGVE--GEVTDAEI-EKVAAM--------AYVDAFIHDLpngyatevgergvklSGGQRQRIAIARALLR 496
Cdd:COG4608 112 M--TVGDIIAEPLRihGLASKAERrERVAELlelvglrpEHADRYPHEF---------------SGGQRQRIGIARALAL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446376040 497 NPQILMLDEATSSLDsKSesvVQKALNNLMK------GRTTLVIAHRLSTV 541
Cdd:COG4608 175 NPKLIVCDEPVSALD-VS---IQAQVLNLLEdlqdelGLTYLFISHDLSVV 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
342-573 |
8.44e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.32 E-value: 8.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGY 420
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQ--DSPLIDGTIRDNICYGVEG---------EVTDAEIEKVAAMAYVDafihDLPNGyatevgergvkLSGGQRQRIA 489
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGLENhavpydemhRRVSEALKQVDMLERAD----YEPNA-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKALNNLM--KGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRT 567
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
....*.
gi 446376040 568 HDMYRE 573
Cdd:PRK13648 233 AEELTR 238
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
355-559 |
1.25e-29 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 115.73 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 355 EKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLL--ERFYEPTGGAIKLGKESItsySLQSWRRQIGYVSQDSPLIDG-T 431
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 432 IRDNICYgvegevtdaeiekVAAMayvdafihdlpngyatevgeRGvkLSGGQRQRIAIARALLRNPQILMLDEATSSLD 511
Cdd:cd03213 99 VRETLMF-------------AAKL--------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446376040 512 SKSESVVQKALNNLMK-GRTTLVIAHRLSTVV--DADKIIFIEKGNLTGSG 559
Cdd:cd03213 144 SSSALQVMSLLRRLADtGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
342-559 |
1.50e-29 |
|
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: 115.75 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGkVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSlQSWRRQIGYV 421
Cdd:cd03264 1 LQLENLTKRYG-KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNICY-GVEGEVTDAEIEkvaamAYVDAFIHDLpnGYATEVGERGVKLSGGQRQRIAIARALLRNPQ 499
Cdd:cd03264 78 PQEFGVYPNfTVREFLDYiAWLKGIPSKEVK-----ARVDEVLELV--NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSG 559
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
344-553 |
1.97e-29 |
|
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: 115.43 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESItsySLQSWRRQIGYVSQ 423
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 424 DS--PLIDGTIRDNICYGVEGevTDAEIEKVAAM-------AYVDAFIHDLpngyatevgergvklSGGQRQRIAIARAL 494
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKE--LDAGNEQAETVlkdldlyALKERHPLSL---------------SGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 495 LRNPQILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHR---LSTVvdADKIIFIEKG 553
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDyefLAKV--CDRVLLLANG 202
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
360-559 |
2.17e-29 |
|
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: 115.47 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 360 NIDFTIeSGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGK----ESITSYSLQSWRRQIGYVSQDSPLIDG-TIRD 434
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfDSRKKINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 435 NICYGV----EGEVTDAEIEKVAAMAYvdafihdlpngyaTEVGERGV-KLSGGQRQRIAIARALLRNPQILMLDEATSS 509
Cdd:cd03297 95 NLAFGLkrkrNREDRISVDELLDLLGL-------------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446376040 510 LDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSG 559
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
342-547 |
2.47e-29 |
|
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: 115.27 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSySLQSWRRQIGYV 421
Cdd:COG4133 3 LEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNIC-----YGVEgeVTDAEIEKVAAMAYVDAFIhDLPNGYatevgergvkLSGGQRQRIAIARALL 495
Cdd:COG4133 81 GHADGLKPElTVRENLRfwaalYGLR--ADREAIDEALEAVGLAGLA-DLPVRQ----------LSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446376040 496 RNPQILMLDEATSSLDSKSESVVQKALNN-LMKGRTTLVIAHRLSTVVDADKI 547
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
342-567 |
2.67e-29 |
|
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: 116.34 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGA------IKLGKESItsyslqsW- 414
Cdd:COG1119 4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRGGEDV-------We 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 415 -RRQIGYVS---QDSPLIDGTIRDNIC---YGVEG---EVTDAEIEKV-AAMAYVDAfihdlpngyaTEVGERGVK-LSG 482
Cdd:COG1119 76 lRKRIGLVSpalQLRFPRDETVLDVVLsgfFDSIGlyrEPTDEQRERArELLELLGL----------AHLADRPFGtLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 483 GQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLV-IAHRLSTVVDA-DKIIFIEKGNLTGSG 559
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAG 225
|
....*...
gi 446376040 560 THDELLRT 567
Cdd:COG1119 226 PKEEVLTS 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
342-553 |
4.06e-29 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 115.12 E-value: 4.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAI----KLGKESITSYSLQSWRRQ 417
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 418 IGYVSQDSPLIDGTIRDNICYGvegevtdAEIEKVAAMAYVDAF-----IHDLPNGYATEVGERGVKLSGGQRQRIAIAR 492
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFG-------SPFNKQRYKAVTDACslqpdIDLLPFGDQTEIGERGINLSGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446376040 493 ALLRNPQILMLDEATSSLDSK-SESVVQKALNNLMKG--RTTLVIAHRLSTVVDADKIIFIEKG 553
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
360-570 |
4.56e-29 |
|
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: 118.28 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 360 NIDFTIESGKVTAIVGPSGSGKTTLFSL---LERfyePTGGAIKLGKE----SITSYSLQSWRRQIGYVSQDSPLIDG-T 431
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEARLFPHlS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 432 IRDNICYG---VEGEVTDAEIEKVAAMayvdafihdlpngyaTEVG---ERGV-KLSGGQRQRIAIARALLRNPQILMLD 504
Cdd:COG4148 94 VRGNLLYGrkrAPRAERRISFDEVVEL---------------LGIGhllDRRPaTLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 505 EATSSLD--SKSE-----SVVQKALNNLMkgrttLVIAH------RLstvvdADKIIFIEKGNLTGSGTHDELLRTHDM 570
Cdd:COG4148 159 EPLAALDlaRKAEilpylERLRDELDIPI-----LYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSRPDL 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
342-536 |
1.18e-28 |
|
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: 113.50 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSysLQSWRRQIGYV 421
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD--LPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLI-DGTIRDNICYGVE-----GEVTDAEIEKVAAMAYVDAFIHDLPNgyatevgergvKLSGGQRQRIAIARALL 495
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGLKlrkvpKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446376040 496 RNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAH 536
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTH 189
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
346-573 |
1.40e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.17 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 346 NVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESItSY---SLQSWRRQIGYVS 422
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYdkkSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 423 Q--DSPLIDGTIRDNICYG----------VEGEVTDAeIEKVAAMAYVDAFIHdlpngyatevgergvKLSGGQRQRIAI 490
Cdd:PRK13639 85 QnpDDQLFAPTVEEDVAFGplnlglskeeVEKRVKEA-LKAVGMEGFENKPPH---------------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 491 ARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIA-HRLSTV-VDADKIIFIEKGNLTGSGTHDELLRTH 568
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
....*
gi 446376040 569 DMYRE 573
Cdd:PRK13639 229 ETIRK 233
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
342-569 |
1.56e-28 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 114.62 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGY 420
Cdd:cd03288 20 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDGTIRDNIcyGVEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQI 500
Cdd:cd03288 100 ILQDPILFSGSIRFNL--DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 501 LMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHD 569
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQED 246
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
346-548 |
1.83e-28 |
|
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: 115.92 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 346 NVHFEYNEDE-KVLNNIDFTIESGKVTAIVGPSGSGKTTL-FSLLeRFYEP---TGGAIKLGKESITSYSLQSWR----R 416
Cdd:COG0444 8 KVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAIL-GLLPPpgiTSGEILFDGEDLLKLSEKELRkirgR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 417 QIGYVSQDS-----PLIdgTIRDNICYGVE--GEVTDAEI-EKVAAM----------AYVDAFIHDLpngyatevgergv 478
Cdd:COG0444 87 EIQMIFQDPmtslnPVM--TVGDQIAEPLRihGGLSKAEArERAIELlervglpdpeRRLDRYPHEL------------- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 479 klSGGQRQRIAIARALLRNPQILMLDEATSSLDsksesV-VQKALNNLMK------GRTTLVIAHRLSTVVD-ADKII 548
Cdd:COG0444 152 --SGGMRQRVMIARALALEPKLLIADEPTTALD-----VtIQAQILNLLKdlqrelGLAILFITHDLGVVAEiADRVA 222
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
27-318 |
2.24e-28 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 114.96 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 27 KGILVFALLMSLLSTGASLFIPMLTKGLVD------NFSLSSIStgqIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGL 100
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDrvlvhkNISLLNLI---LIGLLIVGIFQILLSAVRQYLLDYFANRIDLSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 101 RERLWKKVLVLPVSYYDQNRTGDTISRMtNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVL 180
Cdd:cd18568 78 LSDFYKHLLSLPLSFFASRKVGDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 181 ILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLM 260
Cdd:cd18568 157 LTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINH 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 261 ALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18568 237 LGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
342-555 |
2.47e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 114.00 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGkesitSYSLQSWRRQIGYV 421
Cdd:PRK11247 13 LLLNAVSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLID-GTIRDNICYGVEGEVTDAEIEKVAAMayvdafihdlpnGYATEVGERGVKLSGGQRQRIAIARALLRNPQI 500
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAV------------GLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 501 LMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNL 555
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
358-574 |
2.91e-28 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 113.89 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS---LQSWRRQ-IGYVSQDSPLI-DGTI 432
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 433 RDNICYGVEGEVTDAEIEKVAAMAYVDA-----FIHDLPNgyatevgergvKLSGGQRQRIAIARALLRNPQILMLDEAT 507
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELvglegWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446376040 508 SSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRT--HDMYREF 574
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAelQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNpaNDYVREF 260
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
341-564 |
3.71e-28 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 120.27 E-value: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNED-EKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIG 419
Cdd:PTZ00243 1308 SLVFEGVQMRYREGlPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 420 YVSQDSPLIDGTIRDNICYGVEGevTDAEI----------EKVAAMAyvdafihdlpNGYATEVGERGVKLSGGQRQRIA 489
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNVDPFLEA--SSAEVwaalelvglrERVASES----------EGIDSRVLEGGSNYSVGQRQLMC 1455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 490 IARALLRNPQ--ILMlDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDEL 564
Cdd:PTZ00243 1456 MARALLKKGSgfILM-DEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
342-566 |
5.99e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.58 E-value: 5.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNE----DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS----LQS 413
Cdd:PRK13634 3 ITFQKVEHRYQYktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkkLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 414 WRRQIGYVSQ--DSPLIDGTIRDNICYG-VEGEVTDAEIEKVA--AMAYVdafihdlpnGYATEVGERG-VKLSGGQRQR 487
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGpMNFGVSEEDAKQKAreMIELV---------GLPEELLARSpFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 488 IAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLM--KGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDEL 564
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
..
gi 446376040 565 LR 566
Cdd:PRK13634 234 FA 235
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
341-565 |
6.85e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.41 E-value: 6.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGY 420
Cdd:PRK11231 2 TLRTENLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDG-TIRDNICYGVE------GEVTDAEIEKVA-AMAyvDAFIHDLPNGYATEvgergvkLSGGQRQRIAIAR 492
Cdd:PRK11231 81 LPQHHLTPEGiTVRELVAYGRSpwlslwGRLSAEDNARVNqAME--QTRINHLADRRLTD-------LSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 493 ALLRNPQILMLDEATSSLDSKSesvvQKALNNLM-----KGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELL 565
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINH----QVELMRLMrelntQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
344-565 |
1.83e-27 |
|
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: 110.22 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYNEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQS-WRRQIGYVS 422
Cdd:cd03224 3 VENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 423 QDSPLIDG-TIRDNI---CYGVEGEVTDAEIEKVAAMayvdafihdLPNgyateVGER----GVKLSGGQRQRIAIARAL 494
Cdd:cd03224 82 EGRRIFPElTVEENLllgAYARRRAKRKARLERVYEL---------FPR-----LKERrkqlAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 495 LRNPQILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELL 565
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDeGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
69-564 |
1.99e-27 |
|
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: 118.09 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 69 VGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWKKVLVLpvsyydQNRTGDTISrmtndTGVVKTLISEHLsNLLT 148
Cdd:TIGR01271 126 LGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKL------SSRVLDKIS-----TGQLVSLLSNNL-NKFD 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 149 GGISIVG-------SLIVLFVLDWKmtalLLTV---IPLSVLILVP-----LGRKMYKISKALQDETASFTSVLTQVLSE 213
Cdd:TIGR01271 194 EGLALAHfvwiaplQVILLMGLIWE----LLEVngfCGLGFLILLAlfqacLGQKMMPYRDKRAGKISERLAITSEIIEN 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 214 IRLVKSSNTEkreyETGNTGIQKLLQFGLKEGKVQALISPVMS--FVLMALLVIIvgyggMRVSSGALTTGELVAFILYL 291
Cdd:TIGR01271 270 IQSVKAYCWE----EAMEKIIKNIRQDELKLTRKIAYLRYFYSsaFFFSGFFVVF-----LSVVPYALIKGIILRRIFTT 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 292 VQ--IIMPMSQLSMFFTQFQKAIGATERINAILEYEVEDHETGVKVSNAKQSIVLENVHFEYNED-----EK-------- 356
Cdd:TIGR01271 341 ISycIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNVTASWDEGigelfEKikqnnkar 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 --------------------VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKlgkesitsyslQSWRr 416
Cdd:TIGR01271 421 kqpngddglffsnfslyvtpVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-----------HSGR- 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 417 qIGYVSQDSPLIDGTIRDNICYGVEGEvtDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLR 496
Cdd:TIGR01271 489 -ISFSPQTSWIMPGTIKDNIIFGLSYD--EYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYK 565
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 497 NPQILMLDEATSSLDSKSE-SVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDEL 564
Cdd:TIGR01271 566 DADLYLLDSPFTHLDVVTEkEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
342-564 |
2.55e-27 |
|
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: 109.90 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITsYSLQSWRRQIGY 420
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDG-TIRDNICY-----GVEGEVTDAEIEKVAAM----AYVDAFIHDlpngyatevgergvkLSGGQRQRIAI 490
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLRVlgltDKANKRART---------------LSGGMKRKLSL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 491 ARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTV-VDADKIIFIEKGNLTGSGTHDEL 564
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
344-548 |
3.05e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.80 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVSQ 423
Cdd:PRK10247 10 LQNVGYLAG-DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 424 DSPLIDGTIRDNIC--YGVEGEVTDAeiekvaamayvDAFIHDLPN-GYATEVGERGV-KLSGGQRQRIAIARALLRNPQ 499
Cdd:PRK10247 89 TPTLFGDTVYDNLIfpWQIRNQQPDP-----------AIFLDDLERfALPDTILTKNIaELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLM--KGRTTLVIAHRLSTVVDADKII 548
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVI 208
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
79-318 |
3.89e-27 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 111.41 E-value: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 79 TIAAGLSIYL----LNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIV 154
Cdd:cd18589 46 TIASAVSEFVcdliYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 155 GSLIVLFVLDWKMTalLLTVIPLSVLILVP--LGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNT 232
Cdd:cd18589 126 FLFIFMLWLSPKLA--LLTALGLPLLLLVPkfVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 233 GIQKLLQFGLKEGKVQALISPVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAI 312
Cdd:cd18589 204 RLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAV 283
|
....*.
gi 446376040 313 GATERI 318
Cdd:cd18589 284 GSSEKI 289
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
342-572 |
6.63e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 110.59 E-value: 6.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDE----KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQS---- 413
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 414 WRRQIGYVSQ--DSPLIDGTIRDNICYGVEG-EVTDAEIEKVAAMAYVDAfihdlpnGYATEVGERG-VKLSGGQRQRIA 489
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNfGIPKEKAEKIAAEKLEMV-------GLADEFWEKSpFELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRT 567
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
....*
gi 446376040 568 HDMYR 572
Cdd:PRK13643 235 VDFLK 239
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
356-574 |
7.05e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.41 E-value: 7.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQ--SWRRQIGYVSQDSPLIDG-TI 432
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerLIRQEAGMVFQQFYLFPHlTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 433 RDNICYG---VEGeVTDAEIEKVAAMAYVDAFIHDLPNGYATEvgergvkLSGGQRQRIAIARALLRNPQILMLDEATSS 509
Cdd:PRK09493 95 LENVMFGplrVRG-ASKEEAEKQARELLAKVGLAERAHHYPSE-------LSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 510 LDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRT--HDMYREF 574
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNppSQRLQEF 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
342-564 |
8.40e-27 |
|
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: 108.61 E-value: 8.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVlNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSwRRQIGYV 421
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV-RRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNI-----CYGVEGEVTDAEIEKVaaMAYVDAfihdlpngyaTEVGERGVK-LSGGQRQRIAIARAL 494
Cdd:cd03265 79 FQDLSVDDElTGWENLyiharLYGVPGAERRERIDEL--LDFVGL----------LEAADRLVKtYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 495 LRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDEL 564
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
342-559 |
2.06e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.67 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYV 421
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQ--DSPLIDGTIRDNICYG-VEGEVTDAEIEKVA--AMAYVD--AFIHDLPNgyatevgergvKLSGGQRQRIAIARAL 494
Cdd:PRK13647 85 FQdpDDQVFSSTVWDDVAFGpVNMGLDKDEVERRVeeALKAVRmwDFRDKPPY-----------HLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 495 LRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIA-HRLSTVVD-ADKIIFIEKGNLTGSG 559
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEG 220
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
342-582 |
2.91e-26 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 108.40 E-value: 2.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNED-EKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEpTGGAIKLGKESITSYSLQSWRRQIGY 420
Cdd:cd03289 3 MTVKDLTAKYTEGgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDGTIRDNIcyGVEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQI 500
Cdd:cd03289 82 IPQKVFIFSGTFRKNL--DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 501 LMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHDMYREFATQQLK 580
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDR 239
|
..
gi 446376040 581 IK 582
Cdd:cd03289 240 LK 241
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
344-569 |
4.62e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.87 E-value: 4.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYNEDEKV--LNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYV 421
Cdd:PRK13642 7 VENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQ--DSPLIDGTIRDNICYGVEGE-VTDAEIEKVAAMAYVDAFIHDLPNgyatevgERGVKLSGGQRQRIAIARALLRNP 498
Cdd:PRK13642 87 FQnpDNQFVGATVEDDVAFGMENQgIPREEMIKRVDEALLAVNMLDFKT-------REPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 499 QILMLDEATSSLDSKSESVVQKALNNLMKGR--TTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHD 569
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
356-566 |
4.73e-26 |
|
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: 106.75 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSL-QSWRRQIGYVSQD-SPLIDGTIR 433
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPhEIARLGIGRTFQIpRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 434 DNI---------CYGVEGEVTDAEIEKVA-AMAYVDAFihDLPNGYATEVGErgvkLSGGQRQRIAIARALLRNPQILML 503
Cdd:cd03219 94 ENVmvaaqartgSGLLLARARREEREARErAEELLERV--GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 504 DEATSSLDSK-SESVVQ--KALNNlmKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLR 566
Cdd:cd03219 168 DEPAAGLNPEeTEELAEliRELRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
328-584 |
4.99e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 113.72 E-value: 4.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 328 DHETGVKVSNAKQSIVLENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIklgkesit 407
Cdd:PTZ00243 647 HEATPTSERSAKTPKMKTDDFFEL-EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------- 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 408 syslqsW-RRQIGYVSQDSPLIDGTIRDNICYGVEGEVtdAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQ 486
Cdd:PTZ00243 718 ------WaERSIAYVPQQAWIMNATVRGNILFFDEEDA--ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKA 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 487 RIAIARALLRNPQILMLDEATSSLDSK-SESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELL 565
Cdd:PTZ00243 790 RVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM 869
|
250
....*....|....*....
gi 446376040 566 RThDMYREFATQQLKIKEG 584
Cdd:PTZ00243 870 RT-SLYATLAAELKENKDS 887
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
341-566 |
6.79e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.83 E-value: 6.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNE----DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESIT--SYSLQSW 414
Cdd:PRK13637 2 SIKIENLTHIYMEgtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 415 RRQIGYVSQ--DSPLIDGTIRDNICYG-VEGEVTDAEIEK--VAAMAYVDAFIHDLPNGYATEvgergvkLSGGQRQRIA 489
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIEKDIAFGpINLGLSEEEIENrvKRAMNIVGLDYEDYKDKSPFE-------LSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLR 566
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFK 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
356-579 |
6.90e-26 |
|
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: 111.70 E-value: 6.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTL-FSLLeRFyEPTGGAIKLGKESITSYS---LQSWRRQIGYVSQD-----SP 426
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDpfgslSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 427 LIdgTIRDNIcygVEG------EVTDAEIEK--VAAMAYV--DAfihDLPNGYATEvgergvkLSGGQRQRIAIARALLR 496
Cdd:COG4172 378 RM--TVGQII---AEGlrvhgpGLSAAERRArvAEALEEVglDP---AARHRYPHE-------FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 497 NPQILMLDEATSSLD-SksesvVQKALNNLMK------GRTTLVIAHRLStVVDA--DKIIFIEKGNLTGSGTHDELLR- 566
Cdd:COG4172 443 EPKLLVLDEPTSALDvS-----VQAQILDLLRdlqrehGLAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPTEQVFDa 516
|
250
....*....|....
gi 446376040 567 -THDmYrefaTQQL 579
Cdd:COG4172 517 pQHP-Y----TRAL 525
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
341-567 |
7.20e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.02 E-value: 7.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNEDeKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSysLQSWRRQIGY 420
Cdd:PRK10851 2 SIEIANIKKSFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDG-TIRDNICYGV----EGEVTDAEIEKVAAMAYVDAF-IHDLPNGYATEvgergvkLSGGQRQRIAIARAL 494
Cdd:PRK10851 79 VFQHYALFRHmTVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVqLAHLADRYPAQ-------LSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 495 LRNPQILMLDEATSSLDSKSESVVQKALNNL---MKgRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRT 567
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLheeLK-FTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWRE 227
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
29-318 |
8.54e-26 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 107.58 E-value: 8.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 29 ILVFALLMSLLStgasLFIPMLTKGLVD----NFSLSSISTgQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERL 104
Cdd:cd18588 7 VLLASLFLQLFA----LVTPLFFQVIIDkvlvHRSLSTLDV-LAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 105 WKKVLVLPVSYYDQNRTGDTISRmtndtgvVKTLisEHLSNLLTG--------GISIVGSLIVLFVLDWKMTALLLTVIP 176
Cdd:cd18588 82 FRHLLRLPLSYFESRQVGDTVAR-------VREL--ESIRQFLTGsaltlvldLVFSVVFLAVMFYYSPTLTLIVLASLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 177 LSVLI---LVPLGRKmyKISKALQDETASfTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISP 253
Cdd:cd18588 153 LYALLsllVTPILRR--RLEEKFQRGAEN-QSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQ 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 254 VMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18588 230 IVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
344-583 |
1.03e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.92 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKesitsyslqSWRrqIGYVSQ 423
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------GLR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 424 DSPLIDG-TIRDNICYGVeGEVTDAEIEK---VAAMAYVDAFIHDLP---------NGYA---------------TEVGE 475
Cdd:COG0488 69 EPPLDDDlTVLDTVLDGD-AELRALEAELeelEAKLAEPDEDLERLAelqeefealGGWEaearaeeilsglgfpEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 476 RGVK-LSGGQRQRIAIARALLRNPQILMLDEATSSLDskSESVV--QKALNNLmKGrTTLVIAH-R--LSTVVdaDKIIF 549
Cdd:COG0488 148 RPVSeLSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LESIEwlEEFLKNY-PG-TVLVVSHdRyfLDRVA--TRILE 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446376040 550 IEKGNLT---GSGTHDELLRTHDMYRE---FATQQLKIKE 583
Cdd:COG0488 222 LDRGKLTlypGNYSAYLEQRAERLEQEaaaYAKQQKKIAK 261
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
357-564 |
1.72e-25 |
|
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: 106.48 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKlgkesitsyslQSWRrqIGYVSQDSPLIDGTIRDNI 436
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----------HSGR--ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 437 CYGVEGEvtDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSE- 515
Cdd:cd03291 119 IFGVSYD--EYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEk 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446376040 516 SVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDEL 564
Cdd:cd03291 197 EIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-573 |
2.03e-25 |
|
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: 111.93 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 12 SWRQFLRLIRDTNPPKGILVFALLMSLLSTGASLFIPMLTKGLVDN-FSLSSISTGQIVGLVAFFVMQTIAAGLSIYLLn 90
Cdd:TIGR01271 852 TWNTYLRYITTNRNLVFVLIFCLVIFLAEVAASLLGLWLITDNPSApNYVDQQHANASSPDVQKPVIITPTSAYYIFYI- 930
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 91 YIGQK--------------------IVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGG 150
Cdd:TIGR01271 931 YVGTAdsvlalgffrglplvhtlltVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLT 1010
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 151 ISIVGSLIVLFVLDwkmTALLLTVIPLSVLILVplgRKMYKIS-----KALQDETAS--FTSVLTQV--LSEIRLV-KSS 220
Cdd:TIGR01271 1011 LIVLGAIFVVSVLQ---PYIFIAAIPVAVIFIM---LRAYFLRtsqqlKQLESEARSpiFSHLITSLkgLWTIRAFgRQS 1084
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 221 NTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVIIVGYGGMRvssgaltTGElVAFILYLVQIIMPMSQ 300
Cdd:TIGR01271 1085 YFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDG-------EGE-VGIILTLAMNILSTLQ 1156
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 301 LSMFFT-QFQKAIGATERINAILEYEVEDHET--GVKVSNAKQSIVLENVHFE-----------------YNEDEK-VLN 359
Cdd:TIGR01271 1157 WAVNSSiDVDGLMRSVSRVFKFIDLPQEEPRPsgGGGKYQLSTVLVIENPHAQkcwpsggqmdvqgltakYTEAGRaVLQ 1236
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 360 NIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEpTGGAIKLGKESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNIcyG 439
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL--D 1313
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 440 VEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQ 519
Cdd:TIGR01271 1314 PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 446376040 520 KALNNLMKGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHDMYRE 573
Cdd:TIGR01271 1394 KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
341-560 |
2.33e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.98 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNE----DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS----LQ 412
Cdd:PRK13649 2 GINLQNVSYTYQAgtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 413 SWRRQIGYVSQ--DSPLIDGTIRDNICYGVEG-EVTDAEIEKVA--AMAYVdafihdlpnGYATEVGERG-VKLSGGQRQ 486
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfGVSQEEAEALAreKLALV---------GISESLFEKNpFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 487 RIAIARALLRNPQILMLDEATSSLDSKSesvvQKALNNLMK-----GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGT 560
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKG----RKELMTLFKklhqsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
339-564 |
3.55e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.58 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 339 KQSIVLENVHFEYNEDEK--VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRR 416
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 417 QIGYVSQ--DSPLIDGTIRDNICYGVEGEVTDAE--IEKV-AAMAYVD--AFIHDLPngyatevgergVKLSGGQRQRIA 489
Cdd:PRK13650 82 KIGMVFQnpDNQFVGATVEDDVAFGLENKGIPHEemKERVnEALELVGmqDFKEREP-----------ARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDEL 564
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
342-534 |
4.18e-25 |
|
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: 104.05 E-value: 4.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEK---VLNNIDFTIESGKVTAIVGPSGSGKTTLFSL---LERfyePTGGAIKLGKESITSYS---LQ 412
Cdd:COG4181 9 IELRGLTKTVGTGAGeltILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedaRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 413 SWRRQ-IGYVSQDSPLIDG-TIRDNICYGVE--GEvTDAEIEKVAAMAYV--DAFIHDLPNGyatevgergvkLSGGQRQ 486
Cdd:COG4181 86 RLRARhVGFVFQSFQLLPTlTALENVMLPLElaGR-RDARARARALLERVglGHRLDHYPAQ-----------LSGGEQQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446376040 487 RIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGR-TTLVI 534
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVL 202
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
342-573 |
4.99e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.88 E-value: 4.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGA---IKLGKESITSYSLQSWRRQ 417
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 418 IGYVSQ--DSPLIDGTIRDNICYGVEG-EVTDAEIEKVAAMAYVDAfihdlpnGYATEVGERGVKLSGGQRQRIAIARAL 494
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGLENrAVPRPEMIKIVRDVLADV-------GMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 495 LRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTHDMYR 572
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
.
gi 446376040 573 E 573
Cdd:PRK13640 239 E 239
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
350-559 |
6.94e-25 |
|
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: 103.12 E-value: 6.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 350 EYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEP---TGGAIKL-GKESitsySLQSWRRQIGYVSQDS 425
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFnGQPR----KPDQFQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 426 PLIDG-TIRDNICYGV----EGEVTDAEIEKVAAmayvDAFIHDLPNgyaTEVGERGVK-LSGGQRQRIAIARALLRNPQ 499
Cdd:cd03234 91 ILLPGlTVRETLTYTAilrlPRKSSDAIRKKRVE----DVLLRDLAL---TRIGGNLVKgISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHR-LSTVVDA-DKIIFIEKGNLTGSG 559
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHQpRSDLFRLfDRILLLSSGEIVYSG 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
330-513 |
7.53e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.57 E-value: 7.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 330 ETGVKVSNAKQSIV-LENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITS 408
Cdd:PRK09452 2 KKLNKQPSSLSPLVeLRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 409 YSLQswRRQIGYVSQDSPLIDG-TIRDNICYGVEGE-VTDAEIEK----VAAMAYVDAFihdlpngyatevGERGVK-LS 481
Cdd:PRK09452 81 VPAE--NRHVNTVFQSYALFPHmTVFENVAFGLRMQkTPAAEITPrvmeALRMVQLEEF------------AQRKPHqLS 146
|
170 180 190
....*....|....*....|....*....|..
gi 446376040 482 GGQRQRIAIARALLRNPQILMLDEATSSLDSK 513
Cdd:PRK09452 147 GGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
31-323 |
8.22e-25 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 105.23 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 31 VFALLMSLLSTGASLFIPMLTKGLVDNFSLSSIstgqIVGLVAFfvmqtIAAGLSIYLLNYIGQKIVAGLRERLWKKVLV 110
Cdd:cd18578 27 VFAILFSKLISVFSLPDDDELRSEANFWALMFL----VLAIVAG-----IAYFLQGYLFGIAGERLTRRLRKLAFRAILR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 111 LPVSYYDQ--NRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPLGRK 188
Cdd:cd18578 98 QDIAWFDDpeNSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 189 MYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQAL---ISPVMSFVLMALlvi 265
Cdd:cd18578 178 LSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLgfgLSQSLTFFAYAL--- 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 266 IVGYGGMRVSSGALTTGE-LVAFILyLVQIIMPMSQLSMFFTQFQKAIGATERINAILE 323
Cdd:cd18578 255 AFWYGGRLVANGEYTFEQfFIVFMA-LIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLD 312
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
344-578 |
9.77e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 103.32 E-value: 9.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYE-----PTGGAIKLGKESITSYSLQS--WRR 416
Cdd:PRK14239 8 VSDLSVYYN-KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 417 QIGYVSQDSPLIDGTIRDNICYGV------EGEVTDAEIEKvaamAYVDAFIHDlpngyatEVGER----GVKLSGGQRQ 486
Cdd:PRK14239 87 EIGMVFQQPNPFPMSIYENVVYGLrlkgikDKQVLDEAVEK----SLKGASIWD-------EVKDRlhdsALGLSGGQQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 487 RIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTgsgthdELL 565
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLI------EYN 229
|
250
....*....|...
gi 446376040 566 RTHDMYREFATQQ 578
Cdd:PRK14239 230 DTKQMFMNPKHKE 242
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
342-555 |
1.38e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 101.86 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYnedEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSysLQSWRRQIGYV 421
Cdd:TIGR01277 1 LALDKVRYEY---EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG--LAPYQRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNICYGVE-----GEVTDAEIEKVAAMAYVDAFIHDLPNgyatevgergvKLSGGQRQRIAIARALL 495
Cdd:TIGR01277 76 FQENNLFAHlTVRQNIGLGLHpglklNAEQQEKVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 496 RNPQILMLDEATSSLDSKSESVVQKALNNLM--KGRTTLVIAHRLSTVVD-ADKIIFIEKGNL 555
Cdd:TIGR01277 145 RPNPILLLDEPFSALDPLLREEMLALVKQLCseRQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
344-564 |
1.62e-24 |
|
urea ABC transporter, ATP-binding protein UrtE; 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: 274567 [Multi-domain] Cd Length: 230 Bit Score: 102.22 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYNEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSW-RRQIGYVS 422
Cdd:TIGR03410 3 VSNLNVYYGQSH-ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 423 QDS---PLIdgTIRDNICYGVEGevtdaeieKVAAMAYVDAFIHDL-PngYATEV-GERGVKLSGGQRQRIAIARALLRN 497
Cdd:TIGR03410 82 QGReifPRL--TVEENLLTGLAA--------LPRRSRKIPDEIYELfP--VLKEMlGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 498 PQILMLDEATSSLDSkseSVVQ---KALNNL--MKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDEL 564
Cdd:TIGR03410 150 PKLLLLDEPTEGIQP---SIIKdigRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-554 |
1.76e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 102.81 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTG-----GAIKLGKESITS--YSLQS 413
Cdd:PRK14258 7 AIKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 414 WRRQIGYVSQDSPLIDGTIRDNICYGVE--GEVTDAEIEKVAAMAYVDAfihDLPNGYATEVGERGVKLSGGQRQRIAIA 491
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGVKivGWRPKLEIDDIVESALKDA---DLWDEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 492 RALLRNPQILMLDEATSSLDSKSESVVQKALNNL-MKGRTTLVI-AHRLSTVVDADKIIFIEKGN 554
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIvSHNLHQVSRLSDFTAFFKGN 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
362-559 |
1.80e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 101.42 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 362 DFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSysLQSWRRQIGYVSQDSPLIDG-TIRDNICYGV 440
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLFQENNLFAHlTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 441 E-----GEVTDAEIEKVAAMAYVDAFIHDLPNgyatevgergvKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSE 515
Cdd:cd03298 96 SpglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446376040 516 SVVQKALNNL--MKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSG 559
Cdd:cd03298 165 AEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
342-565 |
2.02e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.14 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKL-GKESITSYSLQSWRRQIGY 420
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsGIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQ--DSPLIDGTIRDNICYGVEGE-VTDAEIEKVAAMAY----VDAFIHDLPNgyatevgergvKLSGGQRQRIAIARA 493
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLcLPPIEIRKRVDRALaeigLEKYRHRSPK-----------TLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 494 LLRNPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELL 565
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
356-559 |
3.04e-24 |
|
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: 100.91 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLgkESI-TSYSLQSWRRQIGYVSQDSPLIDG-TIR 433
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV--DGFdVVKEPAEARRRLGFVSDSTGLYDRlTAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 434 DNICY-----GVEGEVTDAEIEKVAAMAYVDAFIHdlpngyatevgERGVKLSGGQRQRIAIARALLRNPQILMLDEATS 508
Cdd:cd03266 97 ENLEYfaglyGLKGDELTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446376040 509 SLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSG 559
Cdd:cd03266 166 GLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-558 |
3.25e-24 |
|
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: 99.04 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS-LQSWRRQIGY 420
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQdsplidgtirdnicygvegevtdaeiekvaamayvdafihdlpngyatevgergvkLSGGQRQRIAIARALLRNPQI 500
Cdd:cd03216 80 VYQ--------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 501 LMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGS 558
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAqGVAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-556 |
3.38e-24 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 106.59 E-value: 3.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 28 GILVFALLMSLLSTGASLFIpmlTKGLVDNFSLSSISTGQIVGLVAFFVMQTIAAGLSIYLLnyiGQKIVAGLRERLWKK 107
Cdd:PRK10522 17 SVMALSLASAALGIGLIAFI---NQRLIETADTSLLVLPEFLGLLLLLMAVTLGSQLALTTL---GHHFVYRLRSEFIKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 108 VLVLPVSYYDQNRTGDTISRMTNDTGVVkTLISEHLSNLLTGGISIVGSLIVLFVLDWKMtaLLLTVIPLSVLILVP--L 185
Cdd:PRK10522 91 ILDTHVERIEQLGSASLLASLTSDVRNI-TIAFVRLPELVQGIILTLGSAAYLAWLSPKM--LLVTAIWMAVTIWGGfvL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 186 GRKMYK-ISKALQDETASFTSVltQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFglKEGKVQA----LISPVMSFVLM 260
Cdd:PRK10522 168 VARVYKhMATLRETEDKLYNDY--QTVLEGRKELTLNRERAEYVFENEYEPDAQEY--RHHIIRAdtfhLSAVNWSNIMM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 261 ALLVIIVGYggMRVSSGALTTGELVAFILYLVQIIMPMSQlsmfftqfqkAIGA-----TERI--NAILEYEVEDHETGV 333
Cdd:PRK10522 244 LGAIGLVFY--MANSLGWADTNVAATYSLTLLFLRTPLLS----------AVGAlptllSAQVafNKLNKLALAPYKAEF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 334 KVSNAK---QSIVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS 410
Cdd:PRK10522 312 PRPQAFpdwQTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 411 LQSWRRQIGYVSQDSPLIDGTIrdnicyGVEGEVTDAEIekvaamayVDAFIHDLPNGYATEVGE---RGVKLSGGQRQR 487
Cdd:PRK10522 392 PEDYRKLFSAVFTDFHLFDQLL------GPEGKPANPAL--------VEKWLERLKMAHKLELEDgriSNLKLSKGQKKR 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446376040 488 IAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVDADKIIFIEKGNLT 556
Cdd:PRK10522 458 LALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
341-575 |
3.51e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKES------ITSYSLQSW 414
Cdd:COG4161 2 SIQLKNINCFYGSHQ-ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 415 RRQIGYVSQDSPLIDG-TIRDNIcygVEGEVTDAEIEKVAAMAYVDAFIHDLPngyATEVGER-GVKLSGGQRQRIAIAR 492
Cdd:COG4161 81 RQKVGMVFQQYNLWPHlTVMENL---IEAPCKVLGLSKEQAREKAMKLLARLR---LTDKADRfPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 493 ALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRlstvVD-----ADKIIFIEKGNLTGSGTHDELlr 566
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHE----VEfarkvASQVVYMEKGRIIEQGDASHF-- 228
|
....*....
gi 446376040 567 THDMYREFA 575
Cdd:COG4161 229 TQPQTEAFA 237
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
360-511 |
4.44e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 100.25 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 360 NIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEP---TGGAIKLGKESITSysLQSWRRQIGYVSQDSPLIDG-TIRDN 435
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTA--LPAEQRRIGILFQDDLLFPHlSVGEN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 436 ICYGVEGEVTDAEIEKVAAMAYVDAFIHDLpngyatevGERGVK-LSGGQRQRIAIARALLRNPQILMLDEATSSLD 511
Cdd:COG4136 97 LAFALPPTIGRAQRRARVEQALEEAGLAGF--------ADRDPAtLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
316-556 |
4.49e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.92 E-value: 4.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 316 ERINAIlEYEVEDHETGVKVSNAKQS----IVLENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERF 391
Cdd:COG0488 287 EKLERE-EPPRRDKTVEIRFPPPERLgkkvLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 392 YEPTGGAIKLGKesitsyslqswRRQIGYVSQDSPLIDG--TIRDNICYGVEGevtDAEIEkvaAMAYVDAFihDLPNGY 469
Cdd:COG0488 365 LEPDSGTVKLGE-----------TVKIGYFDQHQEELDPdkTVLDELRDGAPG---GTEQE---VRGYLGRF--LFSGDD 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 470 A-TEVGergvKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLmKGrTTLVIAH-R--LSTVvdAD 545
Cdd:COG0488 426 AfKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdRyfLDRV--AT 497
|
250
....*....|.
gi 446376040 546 KIIFIEKGNLT 556
Cdd:COG0488 498 RILEFEDGGVR 508
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
342-567 |
5.77e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 103.65 E-value: 5.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQswRRQIGYV 421
Cdd:PRK11432 7 VVLKNITKRFG-SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG-TIRDNICYGVEGE-VTDAEI-EKVA-AMAYVDAfihdlpNGYatevGERGV-KLSGGQRQRIAIARALLR 496
Cdd:PRK11432 84 FQSYALFPHmSLGENVGYGLKMLgVPKEERkQRVKeALELVDL------AGF----EDRYVdQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446376040 497 NPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRT 567
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
341-555 |
6.11e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.21 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNE----DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESIT----SYSLQ 412
Cdd:PRK13641 2 SIKFENVDYIYSPgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 413 SWRRQIGYVSQ--DSPLIDGTIRDNICYGVEGEVTDAEIEKVAAMAYVDAFihdlpnGYATEVGERG-VKLSGGQRQRIA 489
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKV------GLSEDLISKSpFELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKIIFIEKGNL 555
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
342-567 |
7.97e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 100.93 E-value: 7.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYV 421
Cdd:COG4604 2 IEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQD----SPLidgTIRDNICYG----VEGEVTDAEIEKVA-AMAYVDafIHDLPNGYATEvgergvkLSGGQRQRIAIAR 492
Cdd:COG4604 81 RQEnhinSRL---TVRELVAFGrfpySKGRLTAEDREIIDeAIAYLD--LEDLADRYLDE-------LSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 493 ALLRNPQILMLDEATSSLDSKSESVVQKALNNLM--KGRTTLVIAHrlstvvD-------ADKIIFIEKGNLTGSGTHDE 563
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLH------DinfascyADHIVAMKDGRVVAQGTPEE 222
|
....
gi 446376040 564 LLRT 567
Cdd:COG4604 223 IITP 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
373-564 |
1.04e-23 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 102.19 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 373 IVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSysLQSWRRQIGYVSQDSPLIDG-TIRDNICYGVEGEVTD-AEI- 449
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN--VPPHLRHINMVFQSYALFPHmTVEENVAFGLKMRKVPrAEIk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 450 EKVAAMayvdafihdLPNGYATEVGERG-VKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK- 527
Cdd:TIGR01187 79 PRVLEA---------LRLVQLEEFADRKpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEq 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 446376040 528 -GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDEL 564
Cdd:TIGR01187 150 lGITFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEI 188
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
342-573 |
1.23e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.03 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYV 421
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQ--DSPLIDGTIRDNICY-----GVEGEVTDAEIEKVAAMAYVDAFIHDLPNgyatevgergvKLSGGQRQRIAIARAL 494
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFgpinlGLDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 495 LRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRTHDMY 571
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
..
gi 446376040 572 RE 573
Cdd:PRK13652 233 AR 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
342-560 |
2.09e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.80 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEK---VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS---LQSWR 415
Cdd:PRK11153 2 IELKNISKVFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 416 RQIGYVSQDSPLIDG-TIRDNICYGVEGEVTD-AEIEK-VAAM-AYVDafIHDLPNGYATEvgergvkLSGGQRQRIAIA 491
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALPLELAGTPkAEIKArVTELlELVG--LSDKADRYPAQ-------LSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 492 RALLRNPQILMLDEATSSLDSK-SESVVQ--KALNNLMkGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGT 560
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPAtTRSILEllKDINREL-GLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
342-565 |
3.63e-23 |
|
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: 98.38 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEdEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSL-QSWRRQIGY 420
Cdd:cd03218 1 LRAENLSKRYGK-RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPL-IDGTIRDNICYGVEG-EVTDAEIEKVAamayvDAFIHDLpnGYATEVGERGVKLSGGQRQRIAIARALLRNP 498
Cdd:cd03218 80 LPQEASIfRKLTVEENILAVLEIrGLSKKEREEKL-----EELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 499 QILMLDEATSSLDSKSESVVQKALNNLM-KG----------RTTLVIAHRLStvvdadkIIFieKGNLTGSGTHDELL 565
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKdRGigvlitdhnvRETLSITDRAY-------IIY--EGKVLAEGTPEEIA 221
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
344-553 |
3.84e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.60 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLL---ERfYEPTGGAIKLGKESITSYSL-QSWRRQIG 419
Cdd:COG0396 3 IKNLHVSV-EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPdERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 420 YVSQDSPLIDG-TIRD------NICYGVEGEVTDAEIEKVAAMAYVDafihdLPNGYAtevgERGV--KLSGGQRQRIAI 490
Cdd:COG0396 81 LAFQYPVEIPGvSVSNflrtalNARRGEELSAREFLKLLKEKMKELG-----LDEDFL----DRYVneGFSGGEKKRNEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 491 ARALLRNPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAH--RLSTVVDADKIIFIEKG 553
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDG 217
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
27-318 |
3.87e-23 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 99.86 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 27 KGILVFALLMSLLSTGASLFIPMLTKGLVDNF---SLSSISTGQIVGLVAFFVMQTIAAGLSIYLLNYIGQKI-VAGLRE 102
Cdd:cd18569 1 RSALLFVVLAGLLLVIPGLVIPVFSRIFIDDIlvgGLPDWLRPLLLGMALTALLQGLLTWLQQYYLLRLETKLaLSSSSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 103 RLWKkVLVLPVSYYDQNRTGDTISRM-TNDTgvVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLI 181
Cdd:cd18569 81 FFWH-VLRLPVEFFSQRYAGDIASRVqSNDR--VANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 182 LVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEkREYETGNTGIQ-KLLQFGLKEGKVQALISPVMSFVLM 260
Cdd:cd18569 158 LRLVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAE-SDFFSRWAGYQaKVLNAQQELGRTNQLLGALPTLLSA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 261 ALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18569 237 LTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
344-574 |
4.17e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 98.13 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYNEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSysLQSW---RRQIGY 420
Cdd:COG0410 6 VENLHAGYGGIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG--LPPHriaRLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQD----SPLidgTIRDNICYGVEGEVTDAEIEKVAAMAYvDAFihdlPNgyateVGER----GVKLSGGQRQRIAIAR 492
Cdd:COG0410 83 VPEGrrifPSL---TVEENLLLGAYARRDRAEVRADLERVY-ELF----PR-----LKERrrqrAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 493 ALLRNPQILMLDEATSSLdskSESVVQ------KALNNlmKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELL 565
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGL---APLIVEeifeiiRRLNR--EGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELL 224
|
....*....
gi 446376040 566 RTHDMYREF 574
Cdd:COG0410 225 ADPEVREAY 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
357-567 |
5.73e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.31 E-value: 5.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVSQDSPL-IDGTIRDN 435
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 436 ICYG----VEGEVTDAEIekV-AAMAYVDafihdlpngyATEVGERGV-KLSGGQRQRIAIARALLR------NPQILML 503
Cdd:PRK13548 97 VAMGraphGLSRAEDDAL--VaAALAQVD----------LAHLAGRDYpQLSGGEQQRVQLARVLAQlwepdgPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 504 DEATSSLDSKSESVVQKALNNLMKGRTTLVIA--HRLS-TVVDADKIIFIEKGNLTGSGTHDELLRT 567
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLAHERGLAVIVvlHDLNlAARYADRIVLLHQGRLVADGTPAEVLTP 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
341-566 |
6.16e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.08 E-value: 6.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNE----DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS----LQ 412
Cdd:PRK13646 2 TIRFDNVSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 413 SWRRQIGYVSQ--DSPLIDGTIRDNICYGVEGEVTDaeIEKVAAMAYvdAFIHDLpnGYATEVGERG-VKLSGGQRQRIA 489
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN--LDEVKNYAH--RLLMDL--GFSRDVMSQSpFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKALNNLM--KGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLR 566
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
352-571 |
8.74e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.54 E-value: 8.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 352 NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAI---------KLGKESITSYSLQS-------WR 415
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKNNHELITNPYSKkiknfkeLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 416 RQIGYVSQ--DSPLIDGTIRDNICYG-VEGEVTDAEIEKVAA-----MAYVDAFIHDLPNGyatevgergvkLSGGQRQR 487
Cdd:PRK13631 116 RRVSMVFQfpEYQLFKDTIEKDIMFGpVALGVKKSEAKKLAKfylnkMGLDDSYLERSPFG-----------LSGGQKRR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 488 IAIARALLRNPQILMLDEATSSLDSKSES-VVQKALNNLMKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELL 565
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIF 264
|
....*.
gi 446376040 566 RTHDMY 571
Cdd:PRK13631 265 TDQHII 270
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
356-541 |
9.40e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 99.27 E-value: 9.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSW---RRQIGYVSQD-------- 424
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQkllRQKIQIVFQNpygslnpr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 425 --------SPLIDGTirdnicygvegEVTDAE-IEKVAAM-AYVdafihdlpnGYATEVGERGVKL-SGGQRQRIAIARA 493
Cdd:PRK11308 109 kkvgqileEPLLINT-----------SLSAAErREKALAMmAKV---------GLRPEHYDRYPHMfSGGQRQRIAIARA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446376040 494 LLRNPQILMLDEATSSLDSkseSVVQKALNNLMK-----GRTTLVIAHRLSTV 541
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDV---SVQAQVLNLMMDlqqelGLSYVFISHDLSVV 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
358-565 |
1.14e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 102.43 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKTTLFSLLErFYEPTG----GAIKLGKESITSyslQSWRRQIGYVSQDSPLIDG-TI 432
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLNGMPIDA---KEMRAISAYVQQDDLFIPTlTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 433 RDNICYGVEGEVtDAEIEKVAAMAYVDAFIHDLPNGYA--TEVGERGVK--LSGGQRQRIAIARALLRNPQILMLDEATS 508
Cdd:TIGR00955 117 REHLMFQAHLRM-PRRVTKKEKRERVDEVLQALGLRKCanTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 509 SLDSKSESVVQKALNNL-MKGRTTLVIAHRLSTVVDA--DKIIFIEKGNLTGSGTHDELL 565
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
30-318 |
1.26e-22 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 98.65 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQ----------IVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAG 99
Cdd:cd18554 1 IIITIVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTLDekvyklftiiGIMFFIFLILRPPVEYYRQYFAQWIANKILYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 100 LRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSV 179
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 180 LILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVL 259
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTIT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 260 MALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18554 241 DLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
344-536 |
1.79e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.08 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSwrrqiGYVSQ 423
Cdd:PRK11248 4 ISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 424 DSPLID-GTIRDNICYGVE-GEVTDAEIEKVA--AMAYVDAfihdlpngyaTEVGERGV-KLSGGQRQRIAIARALLRNP 498
Cdd:PRK11248 78 NEGLLPwRNVQDNVAFGLQlAGVEKMQRLEIAhqMLKKVGL----------EGAEKRYIwQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446376040 499 QILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAH 536
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH 187
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
357-548 |
1.80e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.99 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKesitsyslqswRRQIGYVSQDSPLIDG---TIR 433
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVPDSlplTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 434 DNICYGVEGEVT-------DAEIEKVAAMAYVDafIHDLPNgyaTEVGErgvkLSGGQRQRIAIARALLRNPQILMLDEA 506
Cdd:NF040873 76 DLVAMGRWARRGlwrrltrDDRAAVDDALERVG--LADLAG---RQLGE----LSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446376040 507 TSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVDADKII 548
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCV 189
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
341-562 |
1.84e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLG------KESITSYSLQSW 414
Cdd:PRK11124 2 SIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAgnhfdfSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 415 RRQIGYVSQDSPLIDG-TIRDNIcygVEGEVTDAEIEKVAAMAYVDAFIHDLpngYATEVGER-GVKLSGGQRQRIAIAR 492
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHlTVQQNL---IEAPCRVLGLSKDQALARAEKLLERL---RLKPYADRfPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 493 ALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRlstvVD-----ADKIIFIEKGNLTGSGTHD 562
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHE----VEvarktASRVVYMENGHIVEQGDAS 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
342-512 |
2.29e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.85 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEY---NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSyslQSWRRqi 418
Cdd:COG4525 4 LTVRHVSVRYpggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG---PGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 GYVSQDSPLIDG-TIRDNICYGVE--GeVTDAEIEKVAA--MAYVDAfihdlpngyaTEVGERGV-KLSGGQRQRIAIAR 492
Cdd:COG4525 79 GVVFQKDALLPWlNVLDNVAFGLRlrG-VPKAERRARAEelLALVGL----------ADFARRRIwQLSGGMRQRVGIAR 147
|
170 180
....*....|....*....|
gi 446376040 493 ALLRNPQILMLDEATSSLDS 512
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDA 167
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
356-559 |
2.39e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 95.36 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITsySLQSWRRQIGyVSQDSPLIDG--TIR 433
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIG-ALIEAPGFYPnlTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 434 DNICY-GVEGEVTDAEIEKVAAMAyvdafihdlpnGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDS 512
Cdd:cd03268 91 ENLRLlARLLGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446376040 513 KSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSG 559
Cdd:cd03268 160 DGIKELRELILSLRDqGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
69-318 |
4.02e-22 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 96.64 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 69 VGLVAFFVM-QTIAAGLSIYLLNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLL 147
Cdd:cd18590 39 IGLMCLFSLgSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 148 TGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLIlvplgRKMY-----KISKALQDETASFTSVLTQVLSEIRLVKSSNT 222
Cdd:cd18590 119 RSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIA-----QKVYntyhqKLSQAVQDSIAKAGELAREAVSSIRTVRSFKA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 223 EKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLS 302
Cdd:cd18590 194 EEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLV 273
|
250
....*....|....*.
gi 446376040 303 MFFTQFQKAIGATERI 318
Cdd:cd18590 274 YIYGDMLSNVGAAAKV 289
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-567 |
4.14e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.88 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 349 FEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKL-GK-----ESITSYSLQSWRRQIGYV- 421
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdGKvlyfgKDIFQIDAIKLRKEVGMVf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDGTIRDNICYGVE--GEVTDAEIEKVA--AMAYVDAF--IHDLPNGYATEvgergvkLSGGQRQRIAIARALL 495
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAYPLKshGIKEKREIKKIVeeCLRKVGLWkeVYDRLNSPASQ-------LSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 496 RNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRT 567
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
356-566 |
6.28e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.32 E-value: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKL-GKE-SITSYsLQSWRRQIGYVSQDSPLIDG-TI 432
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPvRFRSP-RDAQAAGIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 433 RDNICYGVE----GEVTDAEIEKVAA--MAYVDAFIhDLpngyATEVGErgvkLSGGQRQRIAIARALLRNPQILMLDEA 506
Cdd:COG1129 97 AENIFLGREprrgGLIDWRAMRRRARelLARLGLDI-DP----DTPVGD----LSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446376040 507 TSSLdSKSESvvqKALNNLM-----KGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSG-----THDELLR 566
Cdd:COG1129 168 TASL-TEREV---ERLFRIIrrlkaQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVR 234
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
341-568 |
6.46e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.33 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITsyslQSWRRQIGY 420
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSplidG-----TIRDNICY-----GVegevTDAEIEKvAAMAYVDAFihdlpngyatEVGERGVK----LSGGQRQ 486
Cdd:COG4152 76 LPEER----GlypkmKVGEQLVYlarlkGL----SKAEAKR-RADEWLERL----------GLGDRANKkveeLSKGNQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 487 RIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDEL 564
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEI 216
|
....
gi 446376040 565 LRTH 568
Cdd:COG4152 217 RRQF 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
357-539 |
9.05e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.50 E-value: 9.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQS----WRRQIGYVSQDSPLI-DGT 431
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaelRNQKLGFIYQFHHLLpDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 432 IRDNICYGVE-GEVTDAEIEKVA--AMAYVdafihdlpnGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATS 508
Cdd:PRK11629 104 ALENVAMPLLiGKKKPAEINSRAleMLAAV---------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|...
gi 446376040 509 SLDSKSESVVQKALN--NLMKGRTTLVIAHRLS 539
Cdd:PRK11629 175 NLDARNADSIFQLLGelNRLQGTAFLVVTHDLQ 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
342-553 |
1.47e-21 |
|
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: 90.97 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKesitsyslqswRRQIGYV 421
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQdsplidgtirdnicygvegevtdaeiekvaamayvdafihdlpngyatevgergvkLSGGQRQRIAIARALLRNPQIL 501
Cdd:cd03221 69 EQ--------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 502 MLDEATSSLDSKSesvvQKALNNLMKG--RTTLVIAH-R--LSTVvdADKIIFIEKG 553
Cdd:cd03221 93 LLDEPTNHLDLES----IEALEEALKEypGTVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
342-572 |
1.56e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.91 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESItSYS---LQSWRRQI 418
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSrkgLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 GYVSQ--DSPLIDGTIRDNICYGVEG-EVTDAEIEKVAAMAYVDAFIHDLPNgyatevgERGVKLSGGQRQRIAIARALL 495
Cdd:PRK13636 85 GMVFQdpDNQLFSASVYQDVSFGAVNlKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 496 RNPQILMLDEATSSLDSKSESVVQKALNNLMKGR-TTLVIA-HRLSTV-VDADKIIFIEKGNLTGSGTHDELLRTHDMYR 572
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELgLTIIIAtHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
358-574 |
1.64e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.03 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS----LQSWRRQIGYVSQDSPLIDG-TI 432
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 433 RDNICYGVE-GEVTDAEIEKVAAMAYVDAFIHDLPNGYATEvgergvkLSGGQRQRIAIARALLRNPQILMLDEATSSLD 511
Cdd:PRK10070 124 LDNTAFGMElAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 512 SKSESVVQKALNNLMKG--RTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLR--THDMYREF 574
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKhqRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNnpANDYVRTF 264
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
354-567 |
2.64e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 354 DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVSQDSPL-IDGTI 432
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 433 RDNICYG---------VEGEVTDAEIEKVAAMAYVDAFIhdlpngyatevgERGV-KLSGGQRQRIAIARALLRNPQILM 502
Cdd:PRK09536 95 RQVVEMGrtphrsrfdTWTETDRAAVERAMERTGVAQFA------------DRPVtSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 503 LDEATSSLD----SKSESVVQKALNNlmkGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRT 567
Cdd:PRK09536 163 LDEPTASLDinhqVRTLELVRRLVDD---GKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTA 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
357-553 |
2.73e-21 |
|
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: 92.88 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKL----GKESITSYS----LQSWRRQIGYVSQ----- 423
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASpreiLALRRRTIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 424 ------D---SPLIDGtirdnicyGVEGEVTDAEIEKVAAMAYVDAFIHDLPNgyATevgergvkLSGGQRQRIAIARAL 494
Cdd:COG4778 106 prvsalDvvaEPLLER--------GVDREEARARARELLARLNLPERLWDLPP--AT--------FSGGEQQRVNIARGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446376040 495 LRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLV-IAHRLStVVD--ADKIIFIEKG 553
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEE-VREavADRVVDVTPF 228
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
353-556 |
2.94e-21 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 98.64 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 353 EDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLL-ERFyepTGGAIKLGKESITSYSLQ-SWRRQIGYVSQ-DSPLID 429
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERV---TTGVITGGDRLVNGRPLDsSFQRSIGYVQQqDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 430 GTIRDNICYGV----EGEVTDAEiekvaAMAYVDAFIHDLP-NGYATE-VGERGVKLSGGQRQRIAIARALLRNPQ-ILM 502
Cdd:TIGR00956 851 STVRESLRFSAylrqPKSVSKSE-----KMEYVEEVIKLLEmESYADAvVGVPGEGLNVEQRKRLTIGVELVAKPKlLLF 925
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 503 LDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVDA--DKIIFIEKGNLT 556
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAILFEefDRLLLLQKGGQT 982
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
334-566 |
3.60e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 93.31 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 334 KVSNAKQSIVLENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQS 413
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRV-PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 414 WRRQIGYVSQDSPLIDG-TIRDNIC------YGVEGEVTDAEIEKV-AAMAYVD--AFIHDLPNgyatevgergvKLSGG 483
Cdd:PRK10575 83 FARKVAYLPQQLPAAEGmTVRELVAigrypwHGALGRFGAADREKVeEAISLVGlkPLAHRLVD-----------SLSGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 484 QRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIA--HRLSTVVD-ADKIIFIEKGNLTGSGT 560
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINMAARyCDYLVALRGGEMIAQGT 231
|
....*.
gi 446376040 561 HDELLR 566
Cdd:PRK10575 232 PAELMR 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
342-567 |
4.14e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.10 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSwRRQIGYV 421
Cdd:PRK13537 8 IDFRNVEKRYG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQ-DSPLIDGTIRDNI-CYGVEGEVTDAEIEKVAAMAYVDAfihDLPNGYATEVGErgvkLSGGQRQRIAIARALLRNPQ 499
Cdd:PRK13537 86 PQfDNLDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEFA---KLENKADAKVGE----LSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAH------RLstvvdADKIIFIEKGNLTGSGTHDELLRT 567
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIES 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
357-555 |
4.43e-21 |
|
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: 93.33 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSY---SLQSWRRQIGYVSQDSPLI---DG 430
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDSPSAvnpRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 TIRDNICYGVEG-EVTDAEIEKVAAMAYVDAFihDLPNGYATEvgeRGVKLSGGQRQRIAIARALLRNPQILMLDEATSS 509
Cdd:TIGR02769 106 TVRQIIGEPLRHlTSLDESEQKARIAELLDMV--GLRSEDADK---LPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446376040 510 LDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNL 555
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQI 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
356-566 |
5.01e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 92.79 E-value: 5.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSL-QSWRRQIGYVSQDSPLIDG-TIR 433
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPhRIARLGIARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 434 DNI---CYGVEGEVTDAEI--------EKVAAMAYVDAFIHDLpnGYATEVGERGVKLSGGQRQRIAIARALLRNPQILM 502
Cdd:COG0411 98 ENVlvaAHARLGRGLLAALlrlprarrEEREARERAEELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 503 LDEATSSLDSK-SESVVQ--KALNNLMkGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLR 566
Cdd:COG0411 176 LDEPAAGLNPEeTEELAEliRRLRDER-GITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
342-553 |
6.02e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 91.56 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYE--PTGGAIKLGKESItsyslqswrrqi 418
Cdd:COG2401 29 IVLEAFGVELRVVERyVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQF------------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 gyvSQDSPLIDgtirdniCYGVEGEVTDAeIEKVAAMAYVDAFIhdlpngYATEVGErgvkLSGGQRQRIAIARALLRNP 498
Cdd:COG2401 97 ---GREASLID-------AIGRKGDFKDA-VELLNAVGLSDAVL------WLRRFKE----LSTGQKFRFRLALLLAERP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 499 QILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRlSTVVDA---DKIIFIEKG 553
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQKLARraGITLVVATHH-YDVIDDlqpDLLIFVGYG 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
342-564 |
7.22e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 92.84 E-value: 7.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEK-----VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESiTSYSLQSW-- 414
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLWdi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 415 RRQIGYVSQ--DSPLIDGTIRDNICYGVEG---------EVTDAEIEKVAAMAYVDAFIHdlpngyatevgergvKLSGG 483
Cdd:PRK13633 84 RNKAGMVFQnpDNQIVATIVEEDVAFGPENlgippeeirERVDESLKKVGMYEYRRHAPH---------------LLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 484 QRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTH 561
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
...
gi 446376040 562 DEL 564
Cdd:PRK13633 229 KEI 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
342-537 |
7.66e-21 |
|
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: 89.52 E-value: 7.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLerfyeptGGAIKLGKESITSYslqsWRRQIGYV 421
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-------AGLWPWGSGRIGMP----EGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDGTIRDNICYgvegevtdaeiekvaamayvdafihdlPngyatevgeRGVKLSGGQRQRIAIARALLRNPQIL 501
Cdd:cd03223 70 PQRPYLPLGTLREQLIY---------------------------P---------WDDVLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*..
gi 446376040 502 MLDEATSSLDSKSEsvvQKALNNLMKGRTTLV-IAHR 537
Cdd:cd03223 114 FLDEATSALDEESE---DRLYQLLKELGITVIsVGHR 147
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
362-565 |
9.24e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.57 E-value: 9.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 362 DFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQswRRQIGYVSQDSPLIDG-TIRDNICYGV 440
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 441 EG--EVTDAEIEKVAAMA---YVDAFIHDLPNgyatevgergvKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSkse 515
Cdd:PRK10771 97 NPglKLNAAQREKLHAIArqmGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDP--- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446376040 516 svvqkALNNLM----------KGRTTLVIAHRLStvvDADKI----IFIEKGNLTGSGTHDELL 565
Cdd:PRK10771 163 -----ALRQEMltlvsqvcqeRQLTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELL 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
344-555 |
1.90e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.56 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEY---NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESIT---SYSLQSWRRQ 417
Cdd:PRK10535 7 LKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtldADALAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 418 -IGYVSQDSPLIDG-TIRDNicygVEGEVTDAEIEKVAAMAYVDAFIHDLpnGYATEVGERGVKLSGGQRQRIAIARALL 495
Cdd:PRK10535 87 hFGFIFQRYHLLSHlTAAQN----VEVPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446376040 496 RNPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVDADKIIFIEKGNL 555
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
324-559 |
1.90e-20 |
|
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: 90.47 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 324 YEVEDHETGVKvsNAKQSIVlenvHFEYNEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGk 403
Cdd:cd03267 10 YRVYSKEPGLI--GSLKSLF----KRKYREVE-ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 404 esitsySLQSWRRQIGYVSQ-------------DSPLIDGTIRDNICYGVEGEVTDAEIEKVAAMAYVDAFIHdlpngya 470
Cdd:cd03267 82 ------GLVPWKRRKKFLRRigvvfgqktqlwwDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLD------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 471 TEVgeRgvKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVI--AHRLSTVVD-ADKI 547
Cdd:cd03267 149 TPV--R--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIEAlARRV 224
|
250
....*....|..
gi 446376040 548 IFIEKGNLTGSG 559
Cdd:cd03267 225 LVIDKGRLLYDG 236
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
27-318 |
2.95e-20 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 91.50 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 27 KGILVFALLMSLLSTGASLFIPMLTKGLVDNF-------SLSSIstgqIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAG 99
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVlvqqdlaTLYVI----GVVMLVAALLEAVLTALRTYLFTDTANRIDLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 100 LRERLWKKVLVLPVSYYDQNRTGDTISRmTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSV 179
Cdd:cd18782 77 LGGTIIDHLLRLPLGFFDKRPVGELSTR-ISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 180 LILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVL 259
Cdd:cd18782 156 LLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 260 MALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18782 236 KLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-567 |
3.12e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.93 E-value: 3.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 355 EKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGA-----IKLGKESITSY-SLQSWRRQIGYVSQDSPLI 428
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 429 DGTIRDNICYGVEGE--VTDAEIEKVAAMAYVDAFIHDlpnGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEA 506
Cdd:PRK14271 114 PMSIMDNVLAGVRAHklVPRKEFRGVAQARLTEVGLWD---AVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446376040 507 TSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRT 567
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-579 |
3.83e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.97 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 354 DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYE-----PTGGAIKLGKESITSYSLQSWRRQIGYVSQ-DSPL 427
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 428 IDGTIRDNICYGVEGE---VTDAEIEKVAAMAYVDAFIHDlpngyatEVGER----GVKLSGGQRQRIAIARALLRNPQI 500
Cdd:PRK14247 95 PNLSIFENVALGLKLNrlvKSKKELQERVRWALEKAQLWD-------EVKDRldapAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 501 LMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAH------RLStvvdaDKIIFIEKGNLTGSGTHDELLRT--HDMYR 572
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREVFTNprHELTE 242
|
....*..
gi 446376040 573 EFATQQL 579
Cdd:PRK14247 243 KYVTGRL 249
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
357-564 |
7.17e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.82 E-value: 7.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSysLQSWRRQIGYVSQDSPLIDG-TIRDN 435
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 436 ICYGVE------GEVTDaEIEKVAAMAYVDAFIHDLPNgyatevgergvKLSGGQRQRIAIARALLRNPQILMLDEATSS 509
Cdd:PRK11607 112 IAFGLKqdklpkAEIAS-RVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 510 LDSKSESVVQKALNNLMK--GRTTLVIAH-RLSTVVDADKIIFIEKGNLTGSGTHDEL 564
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
342-573 |
7.34e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.53 E-value: 7.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDE----KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAI-------------KLGKE 404
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 405 SITSYSLQ-----------SWRRQIGYVSQ--DSPLIDGTIRDNICYG-VEGEVTDAEIEKVAAmAYVDafIHDLPNGYA 470
Cdd:PRK13651 83 VLEKLVIQktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpVSMGVSKEEAKKRAA-KYIE--LVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 471 tevgERG-VKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKI 547
Cdd:PRK13651 160 ----QRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVLEwTKRT 235
|
250 260
....*....|....*....|....*.
gi 446376040 548 IFIEKGNLTGSGTHDELLRTHDMYRE 573
Cdd:PRK13651 236 IFFKDGKIIKDGDTYDILSDNKFLIE 261
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
360-511 |
1.21e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 90.70 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 360 NIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGK----ESITSYSLQSWRRQIGYVSQDSPLIDG-TIRD 434
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfDAEKGICLPPEKRRIGYVFQDARLFPHyKVRG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 435 NICYGVeGEVTDAEIEKVAAMAYVDAFIHDLPngyatevgergVKLSGGQRQRIAIARALLRNPQILMLDEATSSLD 511
Cdd:PRK11144 96 NLRYGM-AKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
341-568 |
1.48e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.28 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSlQSWRRQIGY 420
Cdd:PRK13536 41 AIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQ-DSPLIDGTIRDN-ICYGVEGEVTDAEIEkvAAMAYVDAFIHdLPNGYATEVGErgvkLSGGQRQRIAIARALLRNP 498
Cdd:PRK13536 119 VPQfDNLDLEFTVRENlLVFGRYFGMSTREIE--AVIPSLLEFAR-LESKADARVSD----LSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 499 QILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAH------RLstvvdADKIIFIEKGNLTGSGTHDELLRTH 568
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
342-559 |
1.48e-19 |
|
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: 87.20 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERF--YEPTGGAIKLGKESITSYSLQS-WRRQI 418
Cdd:cd03217 1 LEIKDLHVSV-GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEErARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 GYVSQDSPLIDGtirdnicygvegeVTDAEiekvaamayvdaFIHDLpngyatevgerGVKLSGGQRQRIAIARALLRNP 498
Cdd:cd03217 80 FLAFQYPPEIPG-------------VKNAD------------FLRYV-----------NEGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446376040 499 QILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAH--RLSTVVDADKIIFIEKGNLTGSG 559
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-579 |
1.97e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.98 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 339 KQSIVLENVHFEYNEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYE-----PTGGAIKLGKESITSYSLQS 413
Cdd:PRK14267 2 KFAIETVNLRVYYGSNH-VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 414 W--RRQIGYVSQ-DSPLIDGTIRDNICYGVE--GEV-TDAEIEKVAAMAYVDAFIHDlpngyatEVGER----GVKLSGG 483
Cdd:PRK14267 81 IevRREVGMVFQyPNPFPHLTIYDNVAIGVKlnGLVkSKKELDERVEWALKKAALWD-------EVKDRlndyPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 484 QRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHD 562
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTR 233
|
250
....*....|....*....
gi 446376040 563 ELLRT--HDMYREFATQQL 579
Cdd:PRK14267 234 KVFENpeHELTEKYVTGAL 252
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
358-566 |
2.43e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.24 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKL-GKE-SITSySLQSWRRQIGYVSQDSPLIDG-TIRD 434
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPvRIRS-PRDAIALGIGMVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 435 NICYGVEGEV-----TDAEIEKVAAMA--Y-----VDAFIHDLPngyateVGERgvklsggqrQRIAIARALLRNPQILM 502
Cdd:COG3845 100 NIVLGLEPTKggrldRKAARARIRELSerYgldvdPDAKVEDLS------VGEQ---------QRVEILKALYRGARILI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 503 LDEATSSLdSKSESvvqKALNNLMK-----GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSG-----THDELLR 566
Cdd:COG3845 165 LDEPTAVL-TPQEA---DELFEILRrlaaeGKSIIFITHKLREVMAiADRVTVLRRGKVVGTVdtaetSEEELAE 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
358-553 |
3.13e-19 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 86.75 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESIT-----------SYSLQSWRrqigyvsqdsp 426
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepgpdrmvvfqNYSLLPWL----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 427 lidgTIRDNICYGVEGEVTDAEieKVAAMAYVDAFIHDLPNGYATEvgERGVKLSGGQRQRIAIARALLRNPQILMLDEA 506
Cdd:TIGR01184 70 ----TVRENIALAVDRVLPDLS--KSERRAIVEEHIALVGLTEAAD--KRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446376040 507 TSSLDSKSESVVQKALNNLMK--GRTTLVIAHRL-STVVDADKIIFIEKG 553
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
342-570 |
4.00e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.14 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDE----KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITS-----YSLQ 412
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 413 SWRRQIGYVSQ--DSPLIDGTIRDNICYGVE--GEVTDAEIEKVAAMAYvdafIHDLPNGYATEvgeRGVKLSGGQRQRI 488
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQETIEKDIAFGPVnlGENKQEAYKKVPELLK----LVQLPEDYVKR---SPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 489 AIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELL 565
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIF 239
|
....*
gi 446376040 566 RTHDM 570
Cdd:PRK13645 240 SNQEL 244
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
341-564 |
5.05e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.93 E-value: 5.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSysLQSWRRQIGY 420
Cdd:PRK11000 3 SVTLRNVTKAYG-DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND--VPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDG-TIRDNICYGVE-GEVTDAEIEK-VAAMAYVDAFIHDLpngyatevgERGVK-LSGGQRQRIAIARALLR 496
Cdd:PRK11000 80 VFQSYALYPHlSVAENMSFGLKlAGAKKEEINQrVNQVAEVLQLAHLL---------DRKPKaLSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 497 NPQILMLDEATSSLDS------KSE-SVVQKALnnlmkGRTTLVIAH-RLSTVVDADKIIFIEKGNLTGSGTHDEL 564
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAalrvqmRIEiSRLHKRL-----GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
27-318 |
6.17e-19 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 87.60 E-value: 6.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 27 KGILVFALLMSLLSTGASLFIPMLTKGLVDN---FSLSSISTGQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRER 103
Cdd:cd18779 1 PGLLGQILLASLLLQLLGLALPLLTGVLVDRvipRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 104 LWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGIsIVGSLIVLFVLDWKMTALLLTVIPLSVLILV 183
Cdd:cd18779 81 FLEHLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALLDGTL-VLGYLALLFAQSPLLGLVVLGLAALQVALLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 184 PLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALL 263
Cdd:cd18779 160 ATRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 264 VIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18779 240 LVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
341-581 |
7.10e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.10 E-value: 7.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNEdEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQS-WRRQIG 419
Cdd:PRK10895 3 TLTAKNLAKAYKG-RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 420 YVSQDSPLIDG-TIRDNICYGVE-GEVTDAEIEKVAAMAYVDAF-IHDLPNGYatevgerGVKLSGGQRQRIAIARALLR 496
Cdd:PRK10895 82 YLPQEASIFRRlSVYDNLMAVLQiRDDLSAEQREDRANELMEEFhIEHLRDSM-------GQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 497 NPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVDA-DKIIFIEKGNLTGSGTHDELLRTHDMYREF 574
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
....*..
gi 446376040 575 ATQQLKI 581
Cdd:PRK10895 235 LGEDFRL 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
357-541 |
7.20e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 86.66 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSW---RRQIGYVSQDSPlidG--- 430
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkafRRDIQMVFQDSI---Savn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 ---TIRDNIcygveGE----VTDaeIEKVAAMAYVDAFIH--DLPNGYATEvgeRGVKLSGGQRQRIAIARALLRNPQIL 501
Cdd:PRK10419 104 prkTVREII-----REplrhLLS--LDKAERLARASEMLRavDLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446376040 502 MLDEATSSLDskseSVVQKALNNLMK------GRTTLVIAHRLSTV 541
Cdd:PRK10419 174 ILDEAVSNLD----LVLQAGVIRLLKklqqqfGTACLFITHDLRLV 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
356-572 |
7.26e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.61 E-value: 7.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLL----------ERFYEPTGGAIKlgKESITSYSLQSWRRQIGYVSQDS 425
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksaGSHIELLGRTVQ--REGRLARDIRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 426 PLIDG-TIRDNICYGVEGEV-----------TDAEIEKVAAMAYVdafihdlpnGYATEVGERGVKLSGGQRQRIAIARA 493
Cdd:PRK09984 96 NLVNRlSVLENVLIGALGSTpfwrtcfswftREQKQRALQALTRV---------GMVHFAHQRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 494 LLRNPQILMLDEATSSLDSKSESVVQKALN--NLMKGRTTLVIAHRLSTVVD-ADKIIFIEKGNL--TGSGTHDELLRTH 568
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRyCERIVALRQGHVfyDGSSQQFDNERFD 246
|
....
gi 446376040 569 DMYR 572
Cdd:PRK09984 247 HLYR 250
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
18-314 |
7.60e-19 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 87.19 E-value: 7.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 18 RLIRDtnppkgILVFALLMSLLStgasLFIPMLTKGLVDN-FSLSSISTGQIVGLVAFFVM--QTIAAGLSIYLLNYIGQ 94
Cdd:cd18783 2 RLFRD------VAIASLILHVLA----LAPPIFFQIVIDKvLVHQSYSTLYVLTIGVVIALlfEGILGYLRRYLLLVATT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 95 KIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMtNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLL-- 172
Cdd:cd18783 72 RIDARLALRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLaf 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 173 -TVIPLSVLILVPLGRKMYKiskALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALI 251
Cdd:cd18783 151 sALIALIILAFLPPFRRRLQ---ALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 252 SPVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGA 314
Cdd:cd18783 228 QTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLS 290
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
341-513 |
8.49e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.98 E-value: 8.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSL---LERFyepTGGAIKLGKESITSysLQSWRRQ 417
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNE--LEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 418 IGYVSQDSPLIDG-TIRDNICYG-----VEGEVTDAEIEKVAAMAYVDAFIHDLPNgyatevgergvKLSGGQRQRIAIA 491
Cdd:PRK11650 78 IAMVFQNYALYPHmSVRENMAYGlkirgMPKAEIEERVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMG 146
|
170 180
....*....|....*....|..
gi 446376040 492 RALLRNPQILMLDEATSSLDSK 513
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAK 168
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
352-529 |
8.51e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 8.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 352 NEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITsysLQSWRRQIGYVSQDSPLIDG- 430
Cdd:PRK13539 13 GGRV-LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYLGHRNAMKPAl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 TIRDNI-----CYGveGEVTDAEiekvAAMAYVD-AFIHDLPNGYatevgergvkLSGGQRQRIAIARALLRNPQILMLD 504
Cdd:PRK13539 89 TVAENLefwaaFLG--GEELDIA----AALEAVGlAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILD 152
|
170 180
....*....|....*....|....*
gi 446376040 505 EATSSLDSKSesvvQKALNNLMKGR 529
Cdd:PRK13539 153 EPTAALDAAA----VALFAELIRAH 173
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
342-564 |
1.65e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 88.71 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERF--YEPTGGAI-----------------KLG 402
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpsKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 403 K------ESITSYSLQSW----------RRQIGYVSQDSPLI--DGTIRDNICYGVEgevtDAEIEKVAAMAYVDAFIHD 464
Cdd:TIGR03269 80 EpcpvcgGTLEPEEVDFWnlsdklrrriRKRIAIMLQRTFALygDDTVLDNVLEALE----EIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 465 lpngyaTEVGER----GVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRL 538
Cdd:TIGR03269 156 ------VQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWP 229
|
250 260
....*....|....*....|....*..
gi 446376040 539 STVVD-ADKIIFIEKGNLTGSGTHDEL 564
Cdd:TIGR03269 230 EVIEDlSDKAIWLENGEIKEEGTPDEV 256
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
357-578 |
2.05e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKlgkesitsyslqswRRqiGYVsqdSPLID-GTI--- 432
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE--------------VN--GRV---SALLElGAGfhp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 433 ----RDNI-----CYGVEGEVTDAEIEKVAAMAYVDAFIhDLPngyatevgergVK-LSGGQRQRIAIARALLRNPQILM 502
Cdd:COG1134 102 eltgRENIylngrLLGLSRKEIDEKFDEIVEFAELGDFI-DQP-----------VKtYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 503 LDEATSSLDS----KSesvvQKALNNLMKGRTTLVIA-HRLSTVVD-ADKIIFIEKGNLTGSGTHDELLrthDMYREFAT 576
Cdd:COG1134 170 VDEVLAVGDAafqkKC----LARIRELRESGRTVIFVsHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVI---AAYEALLA 242
|
..
gi 446376040 577 QQ 578
Cdd:COG1134 243 GR 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
337-564 |
2.48e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 86.30 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 337 NAKQSIVLE----NVHFEYNEDE----------KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIK-L 401
Cdd:PRK15079 2 TEGKKVLLEvadlKVHFDIKDGKqwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 402 GKEsITSYSLQSW---RRQIGYVSQDsPLID----GTIRDNICYGVEG---EVTDAEI-EKVAAMAYVDAFIHDLPNGYA 470
Cdd:PRK15079 82 GKD-LLGMKDDEWravRSDIQMIFQD-PLASlnprMTIGEIIAEPLRTyhpKLSRQEVkDRVKAMMLKVGLLPNLINRYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 471 TEvgergvkLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKI 547
Cdd:PRK15079 160 HE-------FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRV 232
|
250
....*....|....*..
gi 446376040 548 IFIEKGNLTGSGTHDEL 564
Cdd:PRK15079 233 LVMYLGHAVELGTYDEV 249
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
356-505 |
3.65e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.93 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSL-QSWRRQIGYVSQDSPLIDG-TIR 433
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhKRARLGIGYLPQEASIFRKlTVE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 434 DNIcYGV--EGEVTDAEIEKVAAmAYVDAF-IHDLPNgyatevgERGVKLSGGQRQRIAIARALLRNPQILMLDE 505
Cdd:COG1137 97 DNI-LAVleLRKLSKKEREERLE-ELLEEFgITHLRK-------SKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
359-564 |
3.72e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 84.27 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 359 NNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQigyvsqdsplidGTIR--DNI 436
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM------------GVVRtfQHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 437 cyGVEGEVTDAEIEKVAAMAYVDA-FIHDLPNGYA---------------------TEVGERGV-KLSGGQRQRIAIARA 493
Cdd:PRK11300 90 --RLFREMTVIENLLVAQHQQLKTgLFSGLLKTPAfrraesealdraatwlervglLEHANRQAgNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446376040 494 LLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDEL 564
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
354-553 |
4.52e-18 |
|
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: 83.10 E-value: 4.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 354 DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSyslqSWRRQIGYVSQDSPLI-DGTI 432
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYLPEERGLYpKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 433 RDNICY-----GVEGEVTDAEI----EKVAAMAYVDafihdlpngyatevgERGVKLSGGQRQRIAIARALLRNPQILML 503
Cdd:cd03269 88 IDQLVYlaqlkGLKKEEARRRIdewlERLELSEYAN---------------KRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446376040 504 DEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVD-ADKIIFIEKG 553
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
338-575 |
5.83e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.16 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 338 AKQSIVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIklgkeSITSYSLQSWRRQ 417
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 418 --IGYVSQdSPLIDGT----IRDNICYGVEGEVTDAEIEKVAAMAYVDAFIH--DLPNGYATEVGErgvkLSGGQRQRIA 489
Cdd:PRK15056 78 nlVAYVPQ-SEEVDWSfpvlVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALArvDMVEFRHRQIGE----LSGGQKKRVF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGTHDELLRTH 568
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAE 232
|
....*..
gi 446376040 569 DMYREFA 575
Cdd:PRK15056 233 NLELAFS 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
342-563 |
6.97e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.00 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESIT---SYSLQSWRRQI 418
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlkNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 GYVSQDSPLI-DGTIRDN-----ICYGVEGE----VTDAEIEKVAAMAYVDAFihdlpngyatevgerGVKLSGGQRQRI 488
Cdd:PRK10908 82 GMIFQDHHLLmDRTVYDNvaiplIIAGASGDdirrRVSAALDKVGLLDKAKNF---------------PIQLSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 489 AIARALLRNPQILMLDEATSSLDSK-SESVVQ--KALNNLmkGRTTLVIAHRLSTVVDAD-KIIFIEKGNLTGsGTHDE 563
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDAlSEGILRlfEEFNRV--GVTVLMATHDIGLISRRSyRMLTLSDGHLHG-GVGGE 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-538 |
7.27e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.60 E-value: 7.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNE---DEK-VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSysLQSWRR- 416
Cdd:COG1101 2 LELKNLSKTFNPgtvNEKrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK--LPEYKRa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 417 -QIGYVSQDsPLI----DGTIRDN--ICY----------GVEGEVTDAEIEKVAAMAYvdafihDLPNGYATEVGergvK 479
Cdd:COG1101 80 kYIGRVFQD-PMMgtapSMTIEENlaLAYrrgkrrglrrGLTKKRRELFRELLATLGL------GLENRLDTKVG----L 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446376040 480 LSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGR--TTLVIAHRL 538
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNM 209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
337-565 |
8.47e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.48 E-value: 8.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 337 NAKQSIVLENVHFEYNEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESIT--------- 407
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHE-VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 408 ----SYSLQSWRRQIGYVSQDSPLIDG-TIRDNIcygVEGEVTDAEIEKVAAMAYVDAFIHDLPNGYATEvGERGVKLSG 482
Cdd:PRK10619 80 kvadKNQLRLLRTRLTMVFQHFNLWSHmTVLENV---MEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ-GKYPVHLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 483 GQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGT 560
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGA 235
|
....*
gi 446376040 561 HDELL 565
Cdd:PRK10619 236 PEQLF 240
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
354-574 |
1.38e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.89 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 354 DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS---LQSWRRQIGYVSQDSPLI-D 429
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRMSMLFQSGALFtD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 430 GTIRDNICYGV-EGEVTDAEIEKVAAMAYVDAfihdlpngyateVGERGV------KLSGGQRQRIAIARALLRNPQILM 502
Cdd:PRK11831 99 MNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEA------------VGLRGAaklmpsELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 503 LDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRTHDM-YREF 574
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANPDPrVRQF 242
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
357-559 |
1.49e-17 |
|
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: 81.81 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLgkesitsyslqswRRQIgyvsqdSPLIDG------ 430
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-------------RGRV------SSLLGLgggfnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 --TIRDNI-----CYGVEGEVTDAEIEKVAAMAYVDAFIhDLPngyatevgergVK-LSGGQRQRIAIARALLRNPQILM 502
Cdd:cd03220 98 elTGRENIylngrLLGLSRKEIDEKIDEIIEFSELGDFI-DLP-----------VKtYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 503 LDEATSSLDSKSESVVQKALNNLMKGRTTLVIA-HRLSTVVD-ADKIIFIEKGNLTGSG 559
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
358-538 |
2.54e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.14 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQS-------WRRQIGYVSQDSPLIDG 430
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYApdvdpveVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 TIRDNICYGVEGEVTDAEIEKVAAMAYVDAFIHDlpngyatEVGER----GVKLSGGQRQRIAIARALLRNPQILMLDEA 506
Cdd:PRK14243 106 SIYDNIAYGARINGYKGDMDELVERSLRQAALWD-------EVKDKlkqsGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|..
gi 446376040 507 TSSLDSKSESVVQKALNNLMKGRTTLVIAHRL 538
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
346-537 |
3.80e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 79.99 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 346 NVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSySLQSWRRQIGYVSQDS 425
Cdd:PRK13540 6 ELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 426 ---PLIdgTIRDNICYGVEGEVTDAEIEKVAAMAYVDAFIhDLPNGYatevgergvkLSGGQRQRIAIARALLRNPQILM 502
Cdd:PRK13540 84 ginPYL--TLRENCLYDIHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 446376040 503 LDEATSSLDSKS-ESVVQKALNNLMKGRTTLVIAHR 537
Cdd:PRK13540 151 LDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
32-318 |
9.28e-17 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 80.99 E-value: 9.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 32 FALLMSLLSTGASLFIPMLTKGLVDNF-SLSSISTGQ----IVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWK 106
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLsSYPDEPLSEgyllALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 107 KVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLIsEHLSNLLTGGISIVGSLIVLF-VLDWkmtallLTVIPLSVLIL-VP 184
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLYrLLGW------AALAGLGVLLLlIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 185 LGRKMYKISKALQDETASFT----SVLTQVLSEIRLVKSSN---------TEKREYEtgntgIQKLLQFGLkegkVQALI 251
Cdd:cd18579 154 LQAFLAKLISKLRKKLMKATdervKLTNEILSGIKVIKLYAwekpflkriEELRKKE-----LKALRKFGY----LRALN 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 252 SpvMSFVLMALLVIIVGYGGMRVSSGALTTGelVAF-ILYLVQII-MPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18579 225 S--FLFFSTPVLVSLATFATYVLLGNPLTAA--KVFtALSLFNLLrFPLLMLPQAISSLIEALVSLKRI 289
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
357-565 |
1.25e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 80.27 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVSQDS-----P----- 426
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDPntslnPrlnig 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 427 -LIDGTIRDNICYGVEG--EVTDAEIEKVAAMA-YVDAFIHDLpngyatevgergvklSGGQRQRIAIARALLRNPQILM 502
Cdd:COG4167 108 qILEEPLRLNTDLTAEEreERIFATLRLVGLLPeHANFYPHML---------------SSGQKQRVALARALILQPKIII 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 503 LDEATSSLDSKsesvVQKALNNLM------KGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELL 565
Cdd:COG4167 173 ADEALAALDMS----VRSQIINLMlelqekLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVF 238
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
357-565 |
1.47e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.03 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVSQDSPlidgtirdni 436
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAT---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 437 cygVEGEVTDAEIekVAAMAY-------------VDAFIHDLPNGYATEVGERGV-KLSGGQRQRIAIARALLRNPQILM 502
Cdd:PRK10253 92 ---TPGDITVQEL--VARGRYphqplftrwrkedEEAVTKAMQATGITHLADQSVdTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 503 LDEATSSLDSKSESVVQKALNNL--MKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELL 565
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
31-318 |
2.63e-16 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 79.63 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 31 VFALLMSLLSTGASLFIPMLTKGLVDNFSLSSIsTGQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWKKVLV 110
Cdd:cd18561 3 LLGLLITALYIAQAWLLARALARIFAGGPWEDI-MPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 111 LPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILVPLGRKMY 190
Cdd:cd18561 82 LGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 191 KISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVIIVGYG 270
Cdd:cd18561 162 DTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446376040 271 GMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18561 242 ALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
352-553 |
3.37e-16 |
|
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: 77.28 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 352 NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLL-ERfyePTGGAIKlGKESITSYSL-QSWRRQIGYVSQDSPLID 429
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR---KTAGVIT-GEILINGRPLdKNFQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 430 G-TIRDNICYGvegevtdaeiekvaamAYVdafihdlpngyatevgeRGvkLSGGQRQRIAIARALLRNPQILMLDEATS 508
Cdd:cd03232 93 NlTVREALRFS----------------ALL-----------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446376040 509 SLDSKSESVVQKALNNL-MKGRTTLVIAHRLSTVVDA--DKIIFIEKG 553
Cdd:cd03232 138 GLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
357-539 |
5.99e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.90 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGK--ESITSYSLQSWRRQIGYVSQD-----SPLID 429
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQplHNLNRRQLLPVRHRIQVVFQDpnsslNPRLN 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 430 gtIRDNICYGVE---GEVTDAEIEK--VAAMAYV--DAfihDLPNGYATEvgergvkLSGGQRQRIAIARALLRNPQILM 502
Cdd:PRK15134 381 --VLQIIEEGLRvhqPTLSAAQREQqvIAVMEEVglDP---ETRHRYPAE-------FSGGQRQRIAIARALILKPSLII 448
|
170 180 190
....*....|....*....|....*....|....*..
gi 446376040 503 LDEATSSLDskseSVVQKALNNLMKgrtTLVIAHRLS 539
Cdd:PRK15134 449 LDEPTSSLD----KTVQAQILALLK---SLQQKHQLA 478
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
27-309 |
6.85e-16 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 78.27 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 27 KGILVFALLMSLLSTGASLFIPMLTKGLVDNFslssISTGQI-------VGLVAFFVMQTIAAGLSIYLLNYIGQKIVAG 99
Cdd:cd18567 1 KRALLQILLLSLALELFALASPLYLQLVIDEV----IVSGDRdlltvlaIGFGLLLLLQALLSALRSWLVLYLSTSLNLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 100 LRERLWKKVLVLPVSYYDQNRTGDTISRMtNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSV 179
Cdd:cd18567 77 WTSNLFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 180 LI-LVplgrkMYKISKALQDET----ASFTSVLTQVLSEIRLVKSSNtekREYETGNTGIQKLLQF---GLKEGKVQALI 251
Cdd:cd18567 156 LLrLA-----LYPPLRRATEEQivasAKEQSHFLETIRGIQTIKLFG---REAEREARWLNLLVDAinaDIRLQRLQILF 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 252 SPVMSFVLMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQ 309
Cdd:cd18567 228 SAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKLFELR 285
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
342-581 |
1.17e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEdEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKlgkesitsyslQSWRRQIGYV 421
Cdd:PRK09544 5 VSLENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLiDGTIRDNIC--YGVEGEVTDAEIekVAAMAYVDA-FIHDLPNGyatevgergvKLSGGQRQRIAIARALLRNP 498
Cdd:PRK09544 73 PQKLYL-DTTLPLTVNrfLRLRPGTKKEDI--LPALKRVQAgHLIDAPMQ----------KLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 499 QILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVDADKIIFIEKGNLTGSGThDELLRTH----DMYR 572
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGT-PEVVSLHpefiSMFG 218
|
....*....
gi 446376040 573 EFATQQLKI 581
Cdd:PRK09544 219 PRGAEQLGI 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
310-566 |
1.39e-15 |
|
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: 79.85 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 310 KAIGATERINAILEYEVEDHETGVKVSNAKQSIVLENVHFEYNEDE----KVLNNIDFTIESGKVTAIVGPSGSGKTTLF 385
Cdd:TIGR03269 248 KEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYISVDrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 386 SLLERFYEPTGGA--IKLGKESITSYSLQSW-----RRQIGYVSQDSPLI-DGTIRDNICYGVEGEVTDaEIEKVAAMAY 457
Cdd:TIGR03269 328 KIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDgrgraKRYIGILHQEYDLYpHRTVLDNLTEAIGLELPD-ELARMKAVIT 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 458 VDAFIHDlpNGYATEVGER-GVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVI 534
Cdd:TIGR03269 407 LKMVGFD--EEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIV 484
|
250 260 270
....*....|....*....|....*....|...
gi 446376040 535 AHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLR 566
Cdd:TIGR03269 485 SHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
27-318 |
5.86e-15 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 75.70 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 27 KGILVFALLMSLLSTGASLFIPMLTKGLVDN-FSLSSISTGQ--IVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRER 103
Cdd:cd18566 1 RPLLPQVLLASLFINILALATPLFILQVYDRvIPNESIPTLQvlVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 104 LWKKVLVLPVSYYDQNRTGDTISRMtNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSVLILV 183
Cdd:cd18566 81 AFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 184 PLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEK---REYE--TGNTGIQkllqfGLKEGKVQALISPVMSFV 258
Cdd:cd18566 160 LLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPqmlRRYErlQANAAYA-----GFKVAKINAVAQTLGQLF 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 259 LMALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18566 235 SQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
364-536 |
6.35e-15 |
|
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: 74.75 E-value: 6.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 364 TIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESItSYSLQswrrqigYVSQDSPlidGTIRDNIcygvege 443
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQ-------YIKADYE---GTVRDLL------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 444 vtdaeIEKVAAMAYVDAFIHDLPNGYATE-VGERGV-KLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKA 521
Cdd:cd03237 83 -----SSITKDFYTHPYFKTEIAKPLQIEqILDREVpELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170
....*....|....*..
gi 446376040 522 LNNLM--KGRTTLVIAH 536
Cdd:cd03237 158 IRRFAenNEKTAFVVEH 174
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
349-548 |
6.39e-15 |
|
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: 77.90 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 349 FEYNEDEKVLNNIDFTIESGK-----VTAIVGPSGSGKTTLFSLLERFYEPTGGAIKlGKESItSYSLQswrrqigYVSQ 423
Cdd:COG1245 342 VEYPDLTKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKI-SYKPQ-------YISP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 424 DsplIDGTIRDNIcygvegevtdaeiEKVAAMAYVDAFihdlpngYATEVG---------ERGVK-LSGGQRQRIAIARA 493
Cdd:COG1245 413 D---YDGTVEEFL-------------RSANTDDFGSSY-------YKTEIIkplglekllDKNVKdLSGGELQRVAIAAC 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 494 LLRNPQILMLDEATSSLDSKSESVVQKALNNLM--KGRTTLVIAHRLsTVVD--ADKII 548
Cdd:COG1245 470 LSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAenRGKTAMVVDHDI-YLIDyiSDRLM 527
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
356-539 |
1.74e-14 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 77.19 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERfyEPTGGAIKlGKESITSY--SLQSWRRQIGYVSQD---SPLIdg 430
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFpkKQETFARISGYCEQNdihSPQV-- 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 TIRDNICYGVEGEVTdAEIEKVAAMAYVDAFIH--DLPNGYATEVGERGVK-LSGGQRQRIAIARALLRNPQILMLDEAT 507
Cdd:PLN03140 969 TVRESLIYSAFLRLP-KEVSKEEKMMFVDEVMElvELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
170 180 190
....*....|....*....|....*....|...
gi 446376040 508 SSLDSKSESVVQKALNNLM-KGRTTLVIAHRLS 539
Cdd:PLN03140 1048 SGLDARAAAIVMRTVRNTVdTGRTVVCTIHQPS 1080
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
358-560 |
1.79e-14 |
|
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: 77.36 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSySLQSWRRQIGYVSQDSPLIDG-TIRDNI 436
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 437 CY--GVEGEVTD-AEIEKVAAMAyvDAFIHDLPNgyatevgERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSK 513
Cdd:TIGR01257 1025 LFyaQLKGRSWEeAQLEMEAMLE--DTGLHHKRN-------EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446376040 514 SESVVQKALNNLMKGRTTLVIAHRLSTV-VDADKIIFIEKGNLTGSGT 560
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
360-541 |
1.79e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.43 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 360 NIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESI---TSYSLQSWRRQIGYVSQDsPLIDGTIRDNI 436
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQD-PYASLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 437 CYGV-EGEVTDAEIEKVAAMAYVDAFIHDLpnGYATEVGER-GVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKS 514
Cdd:PRK10261 421 GDSImEPLRVHGLLPGKAAAARVAWLLERV--GLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180
....*....|....*....|....*....
gi 446376040 515 ESVVQKALNNLMK--GRTTLVIAHRLSTV 541
Cdd:PRK10261 499 RGQIINLLLDLQRdfGIAYLFISHDMAVV 527
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
342-540 |
1.98e-14 |
|
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: 76.13 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGkESItsyslqswrrQIGYV 421
Cdd:TIGR03719 323 IEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG-ETV----------KLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLIDG--TIRDNICYGVEG-EVTDAEIekvAAMAYVDAFihdlpNGYATEVGERGVKLSGGQRQRIAIARALLRNP 498
Cdd:TIGR03719 391 DQSRDALDPnkTVWEEISGGLDIiKLGKREI---PSRAYVGRF-----NFKGSDQQKKVGQLSGGERNRVHLAKTLKSGG 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446376040 499 QILMLDEATSSLDSKSESVVQKALNNLmkGRTTLVIAH------RLST 540
Cdd:TIGR03719 463 NVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
356-538 |
2.36e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESI----TSYSLQSwrrQIGYVSQDSPLI-DG 430
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALAA---GVAIIYQELHLVpEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 TIRDNICYG---VEGEVTDAEIEKVAAMAYVDAFIHDL-PNgyaTEVGErgvkLSGGQRQRIAIARALLRNPQILMLDEA 506
Cdd:PRK11288 95 TVAENLYLGqlpHKGGIVNRRLLNYEAREQLEHLGVDIdPD---TPLKY----LSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190
....*....|....*....|....*....|...
gi 446376040 507 TSSLDSKSESVVQKALNNLM-KGRTTLVIAHRL 538
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRaEGRVILYVSHRM 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
357-579 |
2.50e-14 |
|
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: 75.88 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKT----TLFSLLERFYEPTGGAIKLGKESITSYSLQSWRR----QIGYVSQD---- 424
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEpmts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 425 -SPLIdgTIRDNIcygveGEV---------TDAEIEKVAAMAYV---------DAFIHdlpngyatevgergvKLSGGQR 485
Cdd:COG4172 105 lNPLH--TIGKQI-----AEVlrlhrglsgAAARARALELLERVgipdperrlDAYPH---------------QLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 486 QRIAIARALLRNPQILMLDEATSSLDsksesV-VQKALNNLMK------GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTG 557
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALD-----VtVQAQILDLLKdlqrelGMALLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
250 260
....*....|....*....|....
gi 446376040 558 SGTHDELLR--THDmYrefaTQQL 579
Cdd:COG4172 238 QGPTAELFAapQHP-Y----TRKL 256
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
349-582 |
3.30e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.12 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 349 FEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIkLGKESITSYS---LQSWRRQIGYVSQD- 424
Cdd:PRK13638 9 FRY-QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDYSkrgLLALRQQVATVFQDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 425 -SPLIDGTIRDNICYGVEG-EVTDAEIEKVA--AMAYVDA--FIHDLPNGyatevgergvkLSGGQRQRIAIARALLRNP 498
Cdd:PRK13638 87 eQQIFYTDIDSDIAFSLRNlGVPEAEITRRVdeALTLVDAqhFRHQPIQC-----------LSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 499 QILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELL-RTHDMYREFA 575
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFaCTEAMEQAGL 235
|
....*..
gi 446376040 576 TQQLKIK 582
Cdd:PRK13638 236 TQPWLVK 242
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
356-555 |
3.93e-14 |
|
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: 70.92 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQ-IGYVSQDsPLIDG---- 430
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPED-RKREGlvld 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 -TIRDNIcygvegevtdaeiekvaamayvdaFIHDLpngyatevgergvkLSGGQRQRIAIARALLRNPQILMLDEATSS 509
Cdd:cd03215 93 lSVAENI------------------------ALSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446376040 510 LDSKSESVVQKALNNL-MKGRTTLVIAHRLSTVVD-ADKIIFIEKGNL 555
Cdd:cd03215 135 VDVGAKAEIYRLIRELaDAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
342-545 |
5.03e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 74.67 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYePTGGAIKL---GK-----ESItsyslqs 413
Cdd:PRK10938 261 IVLNNGVVSYN-DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQGYSNDLtlfGRrrgsgETI------- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 414 W--RRQIGYVSQDSPL---IDGTIRDNI------CYGVEGEVTDAeiEKVAAMAYVDAFihdlpnGYATEVGERGVK-LS 481
Cdd:PRK10938 332 WdiKKHIGYVSSSLHLdyrVSTSVRNVIlsgffdSIGIYQAVSDR--QQKLAQQWLDIL------GIDKRTADAPFHsLS 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 482 GGQrQRIA-IARALLRNPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLV------------IAHRLSTVVDAD 545
Cdd:PRK10938 404 WGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQLLfvshhaedapacITHRLEFVPDGD 480
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
363-577 |
7.24e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.50 E-value: 7.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 363 FTIESGKVTAIVGPSGSGKTTLFS----LLerfyePTGGAIKLGKESITSYSLQSWRRQIGYVSQ-DSPLI--------- 428
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAELARHRAYLSQqQTPPFampvfqylt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 429 ----DGTirdnicygVEGEVTDAeIEKVAAMAYVDAFIHdlpngyatevgeRGV-KLSGGQRQRIAIARALLR-----NP 498
Cdd:PRK03695 92 lhqpDKT--------RTEAVASA-LNEVAEALGLDDKLG------------RSVnQLSGGEWQRVRLAAVVLQvwpdiNP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 499 --QILMLDEATSSLDsksesVVQK-ALNNLMK-----GRTTLVIAHRLS-TVVDADKIIFIEKGNLTGSGTHDELLRTHD 569
Cdd:PRK03695 151 agQLLLLDEPMNSLD-----VAQQaALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
....*...
gi 446376040 570 MYREFATQ 577
Cdd:PRK03695 226 LAQVFGVN 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
347-573 |
9.47e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.43 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 347 VHFEYNEDEKVlNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIK-LG----KESITsyslqsWRRQIGYV 421
Cdd:COG4586 28 FRREYREVEAV-DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGyvpfKRRKE------FARRIGVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 ----SQ---DSPLID-----GTIrdnicYGVEGEVTDAEIEKVAAMAYVDAFIHdlpngyaTEVgeRgvKLSGGQRQRIA 489
Cdd:COG4586 101 fgqrSQlwwDLPAIDsfrllKAI-----YRIPDAEYKKRLDELVELLDLGELLD-------TPV--R--QLSLGQRMRCE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 490 IARALLRNPQILMLDEATSSLDskseSVVQKALNNLMK------GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHD 562
Cdd:COG4586 165 LAAALLHRPKILFLDEPTIGLD----VVSKEAIREFLKeynrerGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLE 240
|
250
....*....|.
gi 446376040 563 ELLRTHDMYRE 573
Cdd:COG4586 241 ELKERFGPYKT 251
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
358-566 |
1.74e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKL-GKESITSYSLQSWRRQIGYVSQDSPLIDG-TIRDN 435
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITInNINYNKLDHKLAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 436 ICYG------VEG-EVTD-AEIEKVAAMAYVDAFIHDLPNgyaTEVGErgvkLSGGQRQRIAIARALLRNPQILMLDEAT 507
Cdd:PRK09700 101 LYIGrhltkkVCGvNIIDwREMRVRAAMMLLRVGLKVDLD---EKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 508 SSLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSG-----THDELLR 566
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGmvsdvSNDDIVR 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
357-514 |
2.00e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 69.31 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESItSYSLQSWRRQIGYVSQDSplidgtirdni 436
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENILYLGHLP----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 437 cyGVEGEVTDAE-IEKVAAM-AYVDAFIHDLpngyATEVGERGVK------LSGGQRQRIAIARALLRNPQILMLDEATS 508
Cdd:TIGR01189 83 --GLKPELSALEnLHFWAAIhGGAQRTIEDA----LAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
....*.
gi 446376040 509 SLDSKS 514
Cdd:TIGR01189 157 ALDKAG 162
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
356-534 |
2.24e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKL-GKE-SITSYSlQSWRRQIGYVSQD---SPLI-D 429
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdGKPvRIRSPR-DAIRAGIAYVPEDrkgEGLVlD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 430 GTIRDNICYGVEGEVTDAE-IEKVAAMAYVDAFIHDL---PNGYATEVGErgvkLSGGQRQRIAIARALLRNPQILMLDE 505
Cdd:COG1129 345 LSIRENITLASLDRLSRGGlLDRRRERALAEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190
....*....|....*....|....*....|..
gi 446376040 506 ATSSLD--SKSEsvVQKALNNL-MKGRTTLVI 534
Cdd:COG1129 421 PTRGIDvgAKAE--IYRLIRELaAEGKAVIVI 450
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
334-539 |
4.18e-13 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 72.09 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 334 KVSNAKQSIVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGaiKLGKESitsyslqs 413
Cdd:TIGR00954 444 IVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG--RLTKPA-------- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 414 wRRQIGYVSQDSPLIDGTIRDNICYGVEGE------VTDAEIEKVAAMAyvdafihDLPNGYATEVGERGVK-----LSG 482
Cdd:TIGR00954 514 -KGKLFYVPQRPYMTLGTLRDQIIYPDSSEdmkrrgLSDKDLEQILDNV-------QLTHILEREGGWSAVQdwmdvLSG 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 483 GQRQRIAIARALLRNPQILMLDEATSSLdskSESVVQKALNNLMKGRTTLV-IAHRLS 539
Cdd:TIGR00954 586 GEKQRIAMARLFYHKPQFAILDECTSAV---SVDVEGYMYRLCREFGITLFsVSHRKS 640
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
355-515 |
5.99e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 67.90 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 355 EKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESItSYSLQSWRRQIGYVSQdSPLIDGTI-- 432
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGH-APGIKTTLsv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 433 RDNICYgVEGEVTDAEIEKVAAMAYVDAFiHDLPNGYatevgergvkLSGGQRQRIAIARALLRNPQILMLDEATSSLDS 512
Cdd:cd03231 91 LENLRF-WHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
...
gi 446376040 513 KSE 515
Cdd:cd03231 159 AGV 161
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
360-542 |
6.43e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.80 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 360 NIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQS---------WRRQIGYVSQDsPLiDG 430
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYAlseaerrrlLRTEWGFVHQH-PR-DG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 tIRDNICYG--------VEGEVTDAEIEKVAA--MAYVD---AFIHDLPNGYatevgergvklSGGQRQRIAIARALLRN 497
Cdd:PRK11701 102 -LRMQVSAGgnigerlmAVGARHYGDIRATAGdwLERVEidaARIDDLPTTF-----------SGGMQQRLQIARNLVTH 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446376040 498 PQILMLDEATSSLDSKsesvVQKALNNLMKGrttLVIAHRLSTVV 542
Cdd:PRK11701 170 PRLVFMDEPTGGLDVS----VQARLLDLLRG---LVRELGLAVVI 207
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
350-536 |
8.26e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.99 E-value: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 350 EYNEDEKVLNNIDFTIESGK-----VTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLgKESItSYSLQswrrqigYVSQD 424
Cdd:PRK13409 342 EYPDLTKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKI-SYKPQ-------YIKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 425 SpliDGTIRDNIcygvegevtdaeiEKVAAMAYVDAFIHDLPNGYA-TEVGERGVK-LSGGQRQRIAIARALLRNPQILM 502
Cdd:PRK13409 413 Y---DGTVEDLL-------------RSITDDLGSSYYKSEIIKPLQlERLLDKNVKdLSGGELQRVAIAACLSRDADLYL 476
|
170 180 190
....*....|....*....|....*....|....*.
gi 446376040 503 LDEATSSLDSKSESVVQKALNNLMKGR--TTLVIAH 536
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
353-542 |
1.32e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.68 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 353 EDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTG--GAIKLGKESITSYSLqswrRQIGYVSQDSPLIDG 430
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQIL----KRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 -TIRDNI--CYGVEGEVTDAEIEKVAAMAYVDAFIhDLPNGYATEVGE---RGVklSGGQRQRIAIARALLRNPQILMLD 504
Cdd:PLN03211 155 lTVRETLvfCSLLRLPKSLTKQEKILVAESVISEL-GLTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190
....*....|....*....|....*....|....*....
gi 446376040 505 EATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVV 542
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQPSSRV 270
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
33-312 |
1.77e-12 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 68.29 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 33 ALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQ-IVGLVAFF----VMQTIAAGLSIYLLNYIGQKIVAGLRERLWKK 107
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAvPLLLLLAYglarILSSLFNELRDALFARVSQRAVRRLALRVFRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 108 VLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVL-DWKMTALLLTVIPLSVLILVPLG 186
Cdd:cd18582 81 LHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLyGWSYALITLVTVALYVAFTIKVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 187 RKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMALLVII 266
Cdd:cd18582 161 EWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTAI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446376040 267 VGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAI 312
Cdd:cd18582 241 MLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSL 286
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
356-553 |
1.78e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYePTG---GAIKLGKESITSYSLQ-SWRRQIGYVSQDSPLIDG- 430
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRdTERAGIAIIHQELALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 TIRDNICYGvegevtdAEIEKVAAMAYvDAFIHD---------LPNGYATEVGErgvkLSGGQRQRIAIARALLRNPQIL 501
Cdd:PRK13549 98 SVLENIFLG-------NEITPGGIMDY-DAMYLRaqkllaqlkLDINPATPVGN----LGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446376040 502 MLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVD-ADKIIFIEKG 553
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLKaHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
360-572 |
1.90e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 360 NIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITsYSLQSWRRQ-IGYVSQD-----------SPL 427
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSQrIRMIFQDpstslnprqriSQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 428 IDGTIRDNIcygvegEVTDAEIEK--VAAMAYVdAFIHDLPNGYATevgergvKLSGGQRQRIAIARALLRNPQILMLDE 505
Cdd:PRK15112 110 LDFPLRLNT------DLEPEQREKqiIETLRQV-GLLPDHASYYPH-------MLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 506 ATSSLDSKSESvvqkALNNLM------KGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLRT--HDMYR 572
Cdd:PRK15112 176 ALASLDMSMRS----QLINLMlelqekQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASplHELTK 247
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
356-558 |
3.69e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.70 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYePTG---GAIKLGKESITSYSLQSWRRQ-IGYVSQDSPLI-DG 430
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 TIRDNICYGVE-----GEVTDAEIEKVAAMAYVDAFIHDLPNgyATEVGERGvklsGGQRQRIAIARALLRNPQILMLDE 505
Cdd:TIGR02633 94 SVAENIFLGNEitlpgGRMAYNAMYLRAKNLLRELQLDADNV--TRPVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 506 ATSSLDSKSESVVQKALNNL-MKGRTTLVIAHRLSTV-VDADKIIFIEKGNLTGS 558
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLkAHGVACVYISHKLNEVkAVCDTICVIRDGQHVAT 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
324-564 |
5.88e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.31 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 324 YEVEDHETGVKVSNAkqsivlENV--HFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPT-GGAIK 400
Cdd:TIGR02633 246 YPHEPHEIGDVILEA------RNLtcWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVF 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 401 L-GKESITSYSLQSWRRQIGYVSQDSPLiDGTIRDnicYGVEGEVTDAEIEKVAAMAYVDA------------------F 461
Cdd:TIGR02633 320 InGKPVDIRNPAQAIRAGIAMVPEDRKR-HGIVPI---LGVGKNITLSVLKSFCFKMRIDAaaelqiigsaiqrlkvktA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 462 IHDLPNGyatevgergvKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLST 540
Cdd:TIGR02633 396 SPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAE 465
|
250 260
....*....|....*....|....*
gi 446376040 541 VVD-ADKIIFIEKGNLTGSGTHDEL 564
Cdd:TIGR02633 466 VLGlSDRVLVIGEGKLKGDFVNHAL 490
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
27-318 |
6.41e-12 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 66.70 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 27 KGILVFALLMSLLSTGASLFIPMLTKGLVD------NFSL-SSISTGQIVglvaFFVMQTIAAGLSIYLLNYIGQKIVAG 99
Cdd:cd18571 1 KKLILQLLLGLLLGSLLQLIFPFLTQSIVDkginnkDLNFiYLILIAQLV----LFLGSTSIEFIRSWILLHISSRINIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 100 LRERLWKKVLVLPVSYYDQNRTGDTISRMtNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWKMTALLLTVIPLSV 179
Cdd:cd18571 77 IISDFLIKLMRLPISFFDTKMTGDILQRI-NDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGSVLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 180 L-ILVPLGRKMyKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKR---EYEtgntGIQ-KLLQFGLKEGKVQALISPV 254
Cdd:cd18571 156 LwILLFLKKRK-KLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQkrwEWE----RIQaKLFKINIKSLKLDQYQQIG 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 255 MSFVLMALLVIIVGYGGMRVSSGALTTGELVAfILYLV-QIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18571 231 ALFINQLKNILITFLAAKLVIDGEITLGMMLA-IQYIIgQLNSPIEQLIGFIQSLQDAKISLERL 294
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
334-511 |
9.90e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 334 KVSNAKQS--IV--LENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKesitsy 409
Cdd:PRK11147 308 QVEEASRSgkIVfeMENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGT------ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 410 slqswRRQIGYVSQDSPLID--GTIRDNICYGVEgEVTDAEIEKvAAMAYVDAFIHDlPNGYATEVGergvKLSGGQRQR 487
Cdd:PRK11147 381 -----KLEVAYFDQHRAELDpeKTVMDNLAEGKQ-EVMVNGRPR-HVLGYLQDFLFH-PKRAMTPVK----ALSGGERNR 448
|
170 180
....*....|....*....|....
gi 446376040 488 IAIARALLRNPQILMLDEATSSLD 511
Cdd:PRK11147 449 LLLARLFLKPSNLLILDEPTNDLD 472
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
16-318 |
1.03e-11 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 66.15 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 16 FLRLIRDTNPPKGILVFALLMSLLSTGASLFIPMLTKGLVDN-------------FSLSSISTGQIVgLVAFFVmQTIAA 82
Cdd:cd18558 6 LCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLNSSagpfekleeemtlYAYYYLIIGAIV-LITAYI-QGSFW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 83 GLSiyllnyiGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFV 162
Cdd:cd18558 84 GLA-------AGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 163 LDWKMTALLLTVIPLSVLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGL 242
Cdd:cd18558 157 RGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGI 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 243 KEGKVqALISPVMSFVLM-ALLVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18558 237 KKAIT-FNISMGAAFLLIyASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
357-564 |
1.65e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS-LQSWRRQIGYVSQDsPLI--DGTIR 433
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQE-PLLfpNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 434 DNICYGVEGEVTDAE--IEKVAAMAyvdafIH---DLPNGyATEVGErgvklsggqRQRIAIARALLRNPQILMLDEATS 508
Cdd:PRK15439 105 ENILFGLPKRQASMQkmKQLLAALG-----CQldlDSSAG-SLEVAD---------RQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 509 SLD-SKSESVVQKALNNLMKGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDEL 564
Cdd:PRK15439 170 SLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
366-543 |
1.82e-11 |
|
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: 64.70 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 366 ESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGaiKLGKEsitsyslQSWRRQIGYVS----QD--SPLIDGTIR------ 433
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDP-------PDWDEILDEFRgselQNyfTKLLEGDVKvivkpq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 434 --DNICYGVEGEVTDAeIEKVAAMAYVDAFIHDLPngyATEVGERGV-KLSGGQRQRIAIARALLRNPQILMLDEATSSL 510
Cdd:cd03236 95 yvDLIPKAVKGKVGEL-LKKKDERGKLDELVDQLE---LRHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|....
gi 446376040 511 DSKSESVVQKALNNLMK-GRTTLVIAHRLStVVD 543
Cdd:cd03236 171 DIKQRLNAARLIRELAEdDNYVLVVEHDLA-VLD 203
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
342-511 |
1.90e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.68 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYneDEKVL-NNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGkESItsyslqswrrQIGY 420
Cdd:PRK11819 325 IEAENLSKSF--GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG-ETV----------KLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 421 VSQDSPLIDG--TIRDNICYGVEG-EVTDAEiekVAAMAYVDAFihdlpNGYATE----VGErgvkLSGGQRQRIAIARA 493
Cdd:PRK11819 392 VDQSRDALDPnkTVWEEISGGLDIiKVGNRE---IPSRAYVGRF-----NFKGGDqqkkVGV----LSGGERNRLHLAKT 459
|
170
....*....|....*...
gi 446376040 494 LLRNPQILMLDEATSSLD 511
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLD 477
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
354-514 |
3.01e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.90 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 354 DEKVL-NNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESItsyslqswRRQigyvsqdspliDGTI 432
Cdd:PRK13538 12 DERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--------RRQ-----------RDEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 433 RDNICY-----GVEGEVTDAE----IEKVAAMAYVDAFIHDLpngyaTEVGERGVK------LSGGQRQRIAIARALLRN 497
Cdd:PRK13538 73 HQDLLYlghqpGIKTELTALEnlrfYQRLHGPGDDEALWEAL-----AQVGLAGFEdvpvrqLSAGQQRRVALARLWLTR 147
|
170
....*....|....*..
gi 446376040 498 PQILMLDEATSSLDSKS 514
Cdd:PRK13538 148 APLWILDEPFTAIDKQG 164
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
353-553 |
5.24e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 353 EDEKVLNNIDFTIESGKVTAIVGPSGSGKT-TLFSLLERFYEP----TGGAIKLGKESITSYSLQSWRR----QIGYVSQ 423
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 424 D-----SPLidGTIRDNIC------YGVEGEVTDAEI----EKVA---AMAYVDAFIHdlpngyatevgergvKLSGGQR 485
Cdd:PRK15134 100 EpmvslNPL--HTLEKQLYevlslhRGMRREAARGEIlnclDRVGirqAAKRLTDYPH---------------QLSGGER 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446376040 486 QRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMK--GRTTLVIAHRLSTVVD-ADKIIFIEKG 553
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
351-536 |
5.51e-11 |
|
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: 65.34 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 351 YNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGkESITsyslqswrrqIGYVSQDsPLIDG 430
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK----------VGYLPQE-PQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 --TIRDNICYGVE---------GEVT------DAEIEKVAA-MAYVDAFI-----HDLPNgyATEV---------GERGV 478
Cdd:TIGR03719 82 tkTVRENVEEGVAeikdaldrfNEISakyaepDADFDKLAAeQAELQEIIdaadaWDLDS--QLEIamdalrcppWDADV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 479 -KLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLmKGrTTLVIAH 536
Cdd:TIGR03719 160 tKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
364-547 |
6.99e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 364 TIESGKVTAIVGPSGSGKTTLFSLLerfyeptGGAIK--LGK--------ESITSYS---LQSWRRQ-----------IG 419
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKIL-------SGELIpnLGDyeeepswdEVLKRFRgteLQNYFKKlyngeikvvhkPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 420 YVSQDSPLIDGTIRDNIcygvegEVTDaeiEKVAAMAYVDAFihDLpngyaTEVGERGVK-LSGGQRQRIAIARALLRNP 498
Cdd:PRK13409 168 YVDLIPKVFKGKVRELL------KKVD---ERGKLDEVVERL--GL-----ENILDRDISeLSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446376040 499 QILMLDEATSSLDSKSESVVQKALNNLMKGRTTLVIAHRLsTVVD--ADKI 547
Cdd:PRK13409 232 DFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL-AVLDylADNV 281
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
29-318 |
7.24e-11 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 63.23 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 29 ILVFALLMSLLSTGASLFIPMLTKGLVDNFSLSS---ISTGQIVGLVAFFVMQTIAAglsiYLLNYIGQKIVAGLRERLW 105
Cdd:cd18587 7 VLLAALLINLFALASPLFVMNVYDRVVPNNAIETlwvLAIGVLIALLFDFILKLLRA----YFIDVAGKRADVILSSRLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 106 KKVLVLPVSYyDQNRTGDTISRMtNDTGVVKTLISehlSNLLTGGIS---IVGSLIVLFVLDWKMTALLLTVIPLSVLIL 182
Cdd:cd18587 83 ERVLGLRLEA-RPASVGSFANNL-REFESVRDFFT---SATLTALIDlpfVLLFLAVIALIGGPLALVPLVAIPLVLLYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 183 VPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMAL 262
Cdd:cd18587 158 LLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 263 LVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18587 238 TVAIVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQQARTALKSL 293
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
352-564 |
1.43e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 352 NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEptG---GAIKL-GKESITSYSLQSWRRQIGYVSQDS-- 425
Cdd:PRK13549 272 NPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIdGKPVKIRNPQQAIAQGIAMVPEDRkr 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 426 ----PLIDgtIRDNICYGVEGEVTDAE-IEKVAAMAYVDAFIHDLPNGYAT---EVGergvKLSGGQRQRIAIARALLRN 497
Cdd:PRK13549 350 dgivPVMG--VGKNITLAALDRFTGGSrIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 498 PQILMLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDEL 564
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQLVQqGVAIIVISSELPEVLGlSDRVLVMHEGKLKGDLINHNL 492
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
364-540 |
1.60e-10 |
|
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: 63.65 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 364 TIESGKVTAIVGPSGSGKTTLFSLLerfyeptGGAIK--LGKesitsYSLQ-SWRRQIGYVS----QD--SPLIDGTIR- 433
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKIL-------SGELKpnLGD-----YDEEpSWDEVLKRFRgtelQDyfKKLANGEIKv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 434 -------DNICYGVEGEVTDAeIEKV----AAMAYVDAFihDLpngyaTEVGERGVK-LSGGQRQRIAIARALLRNPQIL 501
Cdd:COG1245 163 ahkpqyvDLIPKVFKGTVREL-LEKVdergKLDELAEKL--GL-----ENILDRDISeLSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446376040 502 MLDEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLST 540
Cdd:COG1245 235 FFDEPSSYLDIYQRLNVARLIRELAEeGKYVLVVEHDLAI 274
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
351-517 |
1.84e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 351 YNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGkESITsyslqswrrqIGYVSQDSPLIDG 430
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK----------VGYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 -TIRDNICYGVeGEVTDA--EIEKVAA-----MAYVDAFI---------------HDL-------------PNGYAtEVG 474
Cdd:PRK11819 85 kTVRENVEEGV-AEVKAAldRFNEIYAayaepDADFDALAaeqgelqeiidaadaWDLdsqleiamdalrcPPWDA-KVT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446376040 475 ergvKLSGGQRQRIAIARALLRNPQILMLDEATSSLDskSESV 517
Cdd:PRK11819 163 ----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD--AESV 199
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
339-566 |
2.06e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.37 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 339 KQSIVLENVHFEYnEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESitsyslqswrrQI 418
Cdd:PRK15064 317 RNALEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA-----------NI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 419 GYVSQDSP---LIDGTIRDNIC-YGVEGEvtdaEIEKVAAMAYVDAFIHDlpngyatEVGERGVKLSGGQRQRIAIARAL 494
Cdd:PRK15064 385 GYYAQDHAydfENDLTLFDWMSqWRQEGD----DEQAVRGTLGRLLFSQD-------DIKKSVKVLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 495 LRNPQILMLDEATSSLDskSESVvqKALNN-LMKGRTTLV-IAHRLSTVVD-ADKIIFIEKGNLTG-SGTHDELLR 566
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMD--MESI--ESLNMaLEKYEGTLIfVSHDREFVSSlATRIIEITPDGVVDfSGTYEEYLR 525
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
356-559 |
4.35e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.58 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLF----SLLERFYEPTGgAIKLG----KESITSYslqswRRQIGYVSQDS-- 425
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLkalaNRTEGNVSVEG-DIHYNgipyKEFAEKY-----PGEIIYVSEEDvh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 426 -PLIdgTIRDNIcygvegevtdaeieKVAAMAYVDAFIhdlpngyatevgeRGVklSGGQRQRIAIARALLRNPQILMLD 504
Cdd:cd03233 95 fPTL--TVRETL--------------DFALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 505 EATSSLDSKSesvvqkALNNLMKGRTtlvIAH--RLSTVVDA-----------DKIIFIEKGNLTGSG 559
Cdd:cd03233 144 NSTRGLDSST------ALEILKCIRT---MADvlKTTTFVSLyqasdeiydlfDKVLVLYEGRQIYYG 202
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
357-581 |
6.97e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.72 E-value: 6.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGkesitsyslQSWrrQIGYVSQDSPLIDGTIRDNI 436
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFP---------GNW--QLAWVNQETPALPQPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 437 CYG------VEGEVTDA-EIEKVAAMAYV----DA------------FIHDLpnGYATEVGERGVK-LSGGQRQRIAIAR 492
Cdd:PRK10636 85 IDGdreyrqLEAQLHDAnERNDGHAIATIhgklDAidawtirsraasLLHGL--GFSNEQLERPVSdFSGGWRMRLNLAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 493 ALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKgrTTLVIAHR---LSTVVdaDKIIFIEKGNL---TGSGTHDELLR 566
Cdd:PRK10636 163 ALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG--TLILISHDrdfLDPIV--DKIIHIEQQSLfeyTGNYSSFEVQR 238
|
250
....*....|....*...
gi 446376040 567 THDMYRE---FATQQLKI 581
Cdd:PRK10636 239 ATRLAQQqamYESQQERV 256
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
29-324 |
1.01e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 59.83 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 29 ILVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSisTGQIVGLVAFFVMQTIAAGLSIYLLNY-IGQKIVAGLRERLWKK 107
Cdd:cd18580 4 LLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSS--GYYLGVYAALLVLASVLLVLLRWLLFVlAGLRASRRLHDKLLRS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 108 VLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLdwkmTALLLTVIPLSVLILVPLGR 187
Cdd:cd18580 82 VLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIV----SPYFLIVLPPLLVVYYLLQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 188 KMYKISKALQD-ETASFTSVLTQV------LSEIRlvkSSNTEKReYETGNTGIQKLLQ------------FGLkegkVQ 248
Cdd:cd18580 158 YYLRTSRQLRRlESESRSPLYSHFsetlsgLSTIR---AFGWQER-FIEENLRLLDASQrafylllavqrwLGL----RL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 249 ALISPVMSFVLMALLVIIVGYggmrVSSGalttgeLVAFIL-YLVQIIMPMSQLSMFFTQFQKAIGATERinaILEY 324
Cdd:cd18580 230 DLLGALLALVVALLAVLLRSS----ISAG------LVGLALtYALSLTGSLQWLVRQWTELETSMVSVER---ILEY 293
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
339-560 |
1.12e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 339 KQSIVLE--NVHFEYNEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERF--YEPTGGAIKLGKESITSYSLQSw 414
Cdd:CHL00131 3 KNKPILEikNLHASVNENE-ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 415 RRQIG-YVSQDSPL-IDGTirDNI------CYGVEGEVTDAEIEKVAAMAYVDAFIhDLPNGYATEVgERGVK--LSGGQ 484
Cdd:CHL00131 81 RAHLGiFLAFQYPIeIPGV--SNAdflrlaYNSKRKFQGLPELDPLEFLEIINEKL-KLVGMDPSFL-SRNVNegFSGGE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 485 RQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAH--RLSTVVDADKIIFIEKGNLTGSGT 560
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
367-554 |
2.68e-09 |
|
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: 56.23 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 367 SGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGyvsqdsplidgtirdnicygvegevtd 446
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 447 aeiekvaamayvdafihdlpngyateVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKA----- 521
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446376040 522 -LNNLMKGRTTLVIAHRLSTVVD-------ADKIIFIEKGN 554
Cdd:smart00382 108 lLLLKSEKNLTVILTTNDEKDLGpallrrrFDRRIVLLLIL 148
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
344-510 |
3.49e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.58 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 344 LENVHFEYNEDEkVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSY-SLQSWRRQIGYVS 422
Cdd:PRK11614 8 FDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVAIVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 423 QDSPLIDG-TIRDNICYG---VEGEVTDAEIEKVAAMayvdafihdLPNGYATEVgERGVKLSGGQRQRIAIARALLRNP 498
Cdd:PRK11614 87 EGRRVFSRmTVEENLAMGgffAERDQFQERIKWVYEL---------FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQP 156
|
170
....*....|..
gi 446376040 499 QILMLDEATSSL 510
Cdd:PRK11614 157 RLLLLDEPSLGL 168
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
340-567 |
3.82e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.79 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 340 QSIVLENVHFEynEDEKVLNNIDFTIESGKVTAIVGPSGSGKT----TLFSLLERFYEPTGGAIKLGKESITSYSLQSwr 415
Cdd:PRK10418 3 QQIELRNIALQ--AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 416 RQIGYVSQD-----SPLIdgTIRDN---ICYGVEGEVTDAEIekVAAMAYV---DAfiHDLPNGYATEvgergvkLSGGQ 484
Cdd:PRK10418 79 RKIATIMQNprsafNPLH--TMHTHareTCLALGKPADDATL--TAALEAVgleNA--ARVLKLYPFE-------MSGGM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 485 RQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRT--TLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTH 561
Cdd:PRK10418 146 LQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDV 225
|
....*.
gi 446376040 562 DELLRT 567
Cdd:PRK10418 226 ETLFNA 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
358-511 |
4.14e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQSWRRQ-IGYVSQDSP---LIDG-TI 432
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgIVYISEDRKrdgLVLGmSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 433 RDNICYGVEGEVTDA--EIEKVAAMAYVDAFIhDLPNGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSL 510
Cdd:PRK10762 348 KENMSLTALRYFSRAggSLKHADEQQAVSDFI-RLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
.
gi 446376040 511 D 511
Cdd:PRK10762 427 D 427
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
346-566 |
6.05e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 346 NVHFEYNEDE-KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGK-------ESITSYSLQSWRRQ 417
Cdd:PRK10261 19 NIAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 418 IGYVSQDSPLI--DGTIRDNICYGVEGEVTDA-----EIEKVAAMAYVDAFIHDLPNGYATEVGER-GVKLSGGQRQRIA 489
Cdd:PRK10261 99 RHVRGADMAMIfqEPMTSLNPVFTVGEQIAESirlhqGASREEAMVEAKRMLDQVRIPEAQTILSRyPHQLSGGMRQRVM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTTLV--IAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLR 566
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFH 258
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
356-538 |
7.30e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIK-LGKESITSYSLQSWRRQIGYVSQDSPLIDG-TIR 433
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKSSQEAGIGIIHQELNLIPQlTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 434 DNICYGVEGEVTDAEIEKVAAMAYVDAFIHDL--PNGYATEVGErgvkLSGGQRQRIAIARALLRNPQILMLDEATSSL- 510
Cdd:PRK10762 98 ENIFLGREFVNRFGRIDWKKMYAEADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALt 173
|
170 180
....*....|....*....|....*....
gi 446376040 511 DSKSESVVqKALNNLM-KGRTTLVIAHRL 538
Cdd:PRK10762 174 DTETESLF-RVIRELKsQGRGIVYISHRL 201
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
346-511 |
7.68e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.26 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 346 NVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTL-FSLLERFY--EPTGGAIKLGKESITSYSLQSWRRQIGYVS 422
Cdd:NF040905 264 TVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYgrNISGTVFKDGKEVDVSTVSDAIDAGLAYVT 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 423 QDSP-----LIDgTIRDNICY----GV-EGEVTDAEIEKVAAMAYVDAFihdlpNGYATEVGERGVKLSGGQRQRIAIAR 492
Cdd:NF040905 344 EDRKgyglnLID-DIKRNITLanlgKVsRRGVIDENEEIKVAEEYRKKM-----NIKTPSVFQKVGNLSGGNQQKVVLSK 417
|
170
....*....|....*....
gi 446376040 493 ALLRNPQILMLDEATSSLD 511
Cdd:NF040905 418 WLFTDPDVLILDEPTRGID 436
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
343-564 |
1.08e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.73 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 343 VLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLL--ERfyEPTGGAIKLGKESITSYSLQSWRRQ-IG 419
Cdd:COG3845 259 EVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 420 YVSQDsPLIDG-----TIRDNIC---YGVEGEVTDAEIEKVAAMAYVDAFIHDL---PNGYATEVGergvKLSGGQRQRI 488
Cdd:COG3845 337 YIPED-RLGRGlvpdmSVAENLIlgrYRRPPFSRGGFLDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 489 AIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIahrlSTVVD-----ADKIIFIEKGNLTGSGTHD 562
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLI----SEDLDeilalSDRIAVMYEGRIVGEVPAA 487
|
..
gi 446376040 563 EL 564
Cdd:COG3845 488 EA 489
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
357-514 |
1.09e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.94 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS----LQSWRRQIGYVSQDSPLIDgTI 432
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearAKLRAKHVGFVFQSFMLIP-TL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 433 rdNICYGVE------GEvTDAEIEKVAAmayvdAFIHDLpnGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEA 506
Cdd:PRK10584 104 --NALENVElpallrGE-SSRQSRNGAK-----ALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
....*...
gi 446376040 507 TSSLDSKS 514
Cdd:PRK10584 174 TGNLDRQT 181
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
30-180 |
1.24e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 56.71 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLSTGASLFIpmltkglvdNFSLS-------SISTGQIVGL-VAFFVMQTIAAGLSIYLLNYIGQKIVAGLR 101
Cdd:cd18606 1 LPLLLLLLILSQFAQVFT---------NLWLSfwtedffGLSQGFYIGIyAGLGVLQAIFLFLFGLLLAYLGIRASKRLH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 102 ERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFV-LDWkmtaLLLTVIPLSVL 180
Cdd:cd18606 72 NKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIyLPW----FAIALPPLLVL 147
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
359-511 |
1.33e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 359 NNIDFTIESGKVTAIVGPSGSGKTT----LFSLLErfyePTGGAIKLGKESITSYSLQSwRRQIGYVSQD----SPLidg 430
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTtmkmLTGLLP----ASEGEAWLFGQPVDAGDIAT-RRRVGYMSQAfslyGEL--- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 TIRDNI-----CYGVEGEVTDAEIEKVAA----MAYVDAFIHDLPngyatevgergvkLsgGQRQRIAIARALLRNPQIL 501
Cdd:NF033858 355 TVRQNLelharLFHLPAAEIAARVAEMLErfdlADVADALPDSLP-------------L--GIRQRLSLAVAVIHKPELL 419
|
170
....*....|
gi 446376040 502 MLDEATSSLD 511
Cdd:NF033858 420 ILDEPTSGVD 429
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
357-512 |
1.38e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLF----SLLERFyeptggaiKLGKESITSYS-------LQSWRRQIGYVSQ-D 424
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLktiaSNTDGF--------HIGVEGVITYDgitpeeiKKHYRGDVVYNAEtD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 425 SPLIDGTIRDNI-----CYGVEGEVTD-AEIEKVAAMAYVDAFIHDLPNGYATEVGE---RGVklSGGQRQRIAIARALL 495
Cdd:TIGR00956 148 VHFPHLTVGETLdfaarCKTPQNRPDGvSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASL 225
|
170
....*....|....*..
gi 446376040 496 RNPQILMLDEATSSLDS 512
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDS 242
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
33-312 |
1.51e-08 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 56.46 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 33 ALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQIVG--LVAFFVMQTIAAGLS-----IYLlnYIGQKIVAGLRERLW 105
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLESAVtlILLYALLRFSSKLLKelrslLYR--RVQQNAYRELSLKTF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 106 KKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLL-TGGISIVGSLIVLFVLDWKMTALLLT--VIPLSVLIL 182
Cdd:cd18560 79 AHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVpTLLELIVVSVVFAFHFGAWLALIVFLsvLLYGVFTIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 183 VPLGRKmyKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKEGKVQALISPVMSFVLMAL 262
Cdd:cd18560 159 VTEWRT--KFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446376040 263 LVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAI 312
Cdd:cd18560 237 LTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
358-574 |
1.60e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLgKESITSYSLQSwrrqiGYVSQDSPLIDGTIRdNIC 437
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-KGSAALIAISS-----GLNGQLTGIENIELK-GLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 438 YGVEGEVTDAEIEKVAAMAYVDAFIHDLPNGYatevgergvklSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESV 517
Cdd:PRK13545 113 MGLTKEKIKEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 518 VQKALNNLM-KGRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLrthDMYREF 574
Cdd:PRK13545 182 CLDKMNEFKeQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVV---DHYDEF 237
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
358-560 |
2.58e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 55.31 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKTTLfsLLERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVSQ-DSPLIDGT----- 431
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSL--INDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIViDQSPIGRTprsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 432 ---------IRDNICYGVEG--------EVT--DAEIEKVAAMAYVDA--FIHDLPN-------------GYATeVGERG 477
Cdd:cd03271 89 atytgvfdeIRELFCEVCKGkrynretlEVRykGKSIADVLDMTVEEAleFFENIPKiarklqtlcdvglGYIK-LGQPA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 478 VKLSGGQRQRIAIARALLR---NPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVDADKIIFI--- 550
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKCADWIIDLgpe 247
|
250
....*....|...
gi 446376040 551 ---EKGNLTGSGT 560
Cdd:cd03271 248 ggdGGGQVVASGT 260
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
358-553 |
2.80e-08 |
|
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: 53.87 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKTTLfsLLERFYEPtggAIKLGKESITSYSlqswRRQIGYVSQDSPLIDGTIrdnic 437
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYAS---GKARLISFLPKFS----RNKLIFIDQLQFLIDVGL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 438 ygvegevtdaeiekvaamayvdafihdlpnGYATeVGERGVKLSGGQRQRIAIARALLRNPQ--ILMLDEATSSLDSKSE 515
Cdd:cd03238 77 ------------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 446376040 516 SVVQKALNNLM-KGRTTLVIAHRLSTVVDADKIIFIEKG 553
Cdd:cd03238 126 NQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
360-558 |
3.49e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 360 NIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS-LQSWRRQIGYVSQD---SPL-IDGTIRD 434
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPEDrqsSGLyLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 435 NIC---YGVEGEVTDAEIEKvaamAYVDAFIHDLpnGYATEVGERGVK-LSGGQRQRIAIARALLRNPQILMLDEATSSL 510
Cdd:PRK15439 361 NVCaltHNRRGFWIKPAREN----AVLERYRRAL--NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446376040 511 DSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGS 558
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAqNVAVLFISSDLEEIEQmADRVLVMHQGEISGA 484
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
365-551 |
3.82e-08 |
|
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: 53.34 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 365 IESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESItSYSLQSwrrqigyvsqdsplidgtirdnicygvegev 444
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-VYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 445 tdaeiekvaamayvdafihdlpngyatevgergVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNN 524
Cdd:cd03222 70 ---------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190
....*....|....*....|....*....|.
gi 446376040 525 L-MKG-RTTLVIAHRLsTVVD--ADKIIFIE 551
Cdd:cd03222 117 LsEEGkKTALVVEHDL-AVLDylSDRIHVFE 146
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
359-541 |
4.59e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.12 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 359 NNIDFTIESGKVTAIVGPSGSGKT-TLFS---LLERFYEPTGGAIKLGKE--SITSYSLQSWR-RQIGYVSQDsPL--ID 429
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSqTAFAlmgLLAANGRIGGSATFNGREilNLPEKELNKLRaEQISMIFQD-PMtsLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 430 GTIRdnicygvegeVTDAEIEKV---AAMAYVDAFIHDLPNGYATEVGERGVKL-------SGGQRQRIAIARALLRNPQ 499
Cdd:PRK09473 112 PYMR----------VGEQLMEVLmlhKGMSKAEAFEESVRMLDAVKMPEARKRMkmyphefSGGMRQRVMIAMALLCRPK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLMKGRTT--LVIAHRLSTV 541
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVV 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
356-553 |
4.69e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYePTG---GAIKL-GKESITSYSLQSWRRQIGYVSQDSPLIDG- 430
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFdGEVCRFKDIRDSEALGIVIIHQELALIPYl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 431 TIRDNICYGVE---GEVTD---AEIEKVAAMAYVDafIHDLPNgyaTEVGERGVklsgGQRQRIAIARALLRNPQILMLD 504
Cdd:NF040905 94 SIAENIFLGNErakRGVIDwneTNRRARELLAKVG--LDESPD---TLVTDIGV----GKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 505 EATSSL-DSKSEsvvqkALNNLM-----KGRTTLVIAHRLSTVVD-ADKIIFIEKG 553
Cdd:NF040905 165 EPTAALnEEDSA-----ALLDLLlelkaQGITSIIISHKLNEIRRvADSITVLRDG 215
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
354-511 |
4.88e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 354 DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSyslqswRRQigyvsQDSPlidgtiR 433
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVA------RLQ-----QDPP------R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 434 DnicygVEGEVTDAEIEKVAAMA-YVDAFiHDLPNGYATEVGERGVK--------------------------------- 479
Cdd:PRK11147 78 N-----VEGTVYDFVAEGIEEQAeYLKRY-HDISHLVETDPSEKNLNelaklqeqldhhnlwqlenrinevlaqlgldpd 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 446376040 480 -----LSGGQRQRIAIARALLRNPQILMLDEATSSLD 511
Cdd:PRK11147 152 aalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
106-317 |
6.24e-08 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 54.46 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 106 KKVLVLPVSYYDQNRTGDTISRMTNDTGVvKTLISEHLSNLLTGGISIVGSLIVLFVL-DWKMTALLLTVIPLSVLILVP 184
Cdd:cd18583 78 NHVMNLSMDFHDSKKSGEVLKAIEQGSSI-NDLLEQILFQIVPMIIDLVIAIVYLYYLfDPYMGLIVAVVMVLYVWSTIK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 185 LGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLK-------EGKVQALIspvMSF 257
Cdd:cd18583 157 LTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKylfslnlLNAVQSLI---LTL 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 258 VLMALLVIIVgYggmRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKAIGATER 317
Cdd:cd18583 234 GLLAGCFLAA-Y---QVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAER 289
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
354-536 |
9.84e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 354 DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSLQswrRQIGYVSQDSPL-IDGTI 432
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLkADLST 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 433 RDNICY--GVEG----EVTDAEIEKVAAMAYVDAFIHdlpngyatevgergvKLSGGQRQRIAIARALLRNPQILMLDEA 506
Cdd:PRK13543 100 LENLHFlcGLHGrrakQMPGSALAIVGLAGYEDTLVR---------------QLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 446376040 507 TSSLDSKSESVVQKALN-NLMKGRTTLVIAH 536
Cdd:PRK13543 165 YANLDLEGITLVNRMISaHLRGGGAALVTTH 195
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
347-567 |
9.93e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.98 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 347 VHF-EYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKT----TLFSLLERFYEPTGGAIKLGKESITSYSlQSWRRQIgyV 421
Cdd:PRK11022 11 VHFgDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRIS-EKERRNL--V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSPLI--DGTIRDNICYGVEGEVTDA-EIEKVAAMAYVDAFIHDLpngyATEVG------ERGV---KLSGGQRQRIA 489
Cdd:PRK11022 88 GAEVAMIfqDPMTSLNPCYTVGFQIMEAiKVHQGGNKKTRRQRAIDL----LNQVGipdpasRLDVyphQLSGGMSQRVM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 490 IARALLRNPQILMLDEATSSLDSKSESVVQKALNNLMKGRTT--LVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELLR 566
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIFR 243
|
.
gi 446376040 567 T 567
Cdd:PRK11022 244 A 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
356-538 |
1.40e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIK-LGKESITSYSLQSWRRQIGYVSQDSPLI-DGTIR 433
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILfQGKEIDFKSSKEALENGISMVHQELNLVlQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 434 DNIC---YGVEGEVTDAEIEKVAAMAYVDAFIHDL-PNgyatevgERGVKLSGGQRQRIAIARALLRNPQILMLDEATSS 509
Cdd:PRK10982 92 DNMWlgrYPTKGMFVDQDKMYRDTKAIFDELDIDIdPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190
....*....|....*....|....*....|
gi 446376040 510 LDSKSESVVQKALNNLM-KGRTTLVIAHRL 538
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKeRGCGIVYISHKM 194
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
341-571 |
1.56e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.90 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 341 SIVLENVHFEY-------------------NEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAI-K 400
Cdd:PRK13546 4 SVNIKNVTKEYriyrtnkermkdalipkhkNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 401 LGKESITSyslqswrrqigyvsqdsplidgtirdnICYGVEGEVTDAE-IE-KVAAMAYVDAFIHDLPNGYA--TEVGE- 475
Cdd:PRK13546 84 NGEVSVIA---------------------------ISAGLSGQLTGIEnIEfKMLCMGFKRKEIKAMTPKIIefSELGEf 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 476 --RGVK-LSGGQRQRIAIARALLRNPQILMLDEATSSLDsksESVVQKALNNLMK----GRTTLVIAHRLSTVVD-ADKI 547
Cdd:PRK13546 137 iyQPVKkYSSGMRAKLGFSINITVNPDILVIDEALSVGD---QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKI 213
|
250 260
....*....|....*....|....
gi 446376040 548 IFIEKGNLTGSGTHDELLRTHDMY 571
Cdd:PRK13546 214 AWIEGGKLKDYGELDDVLPKYEAF 237
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
107-307 |
2.64e-07 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350006 [Multi-domain] Cd Length: 289 Bit Score: 52.63 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 107 KVLVLPVSYYDQNRTGDTISRMTNDT----GVVKTLISEHLSNLLtggisivgSLIVL----FVLDWKMTALLLTVIPLS 178
Cdd:cd18562 78 HVITLPLSFHSQRGSGRLLRIMLRGTdalfGLWLGFFREHLAALV--------SLIVLlpvaLWMNWRLALLLVVLAAVY 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 179 VLILVPLGRKmykiSKALQDETASFTSVL----TQVLSEIRLVKSSNTEKREYETGNTGIQKLL--QFglkegkvqalis 252
Cdd:cd18562 150 AALNRLVMRR----TKAGQAAVEEHHSALsgrvGDVIGNVTVVQSYTRLAAETSALRGITRRLLaaQY------------ 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 253 PVMSF--VLMAL--------LVIIVGYGGMRVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQ 307
Cdd:cd18562 214 PVLNWwaLASVLtraastltMVAIFALGAWLVQRGELTVGEIVSFVGFATLLIGRLDQLSGFINR 278
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
95-319 |
2.77e-07 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 52.48 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 95 KIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDtgvVKTLisEHL-----SNLLTGGISIVGSLIVLFVLDWKMtA 169
Cdd:cd18585 65 RLLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVAD---IDTL--DNLylrvlSPPVVALLVILATILFLAFFSPAL-A 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 170 LLLTVIPLSVLILVP-----LGRKmykISKALQDETASFTSVLTQVLSEIRLVKSSNTEKREYETGNTGIQKLLQFGLKE 244
Cdd:cd18585 139 LILLAGLLLAGVVIPllfyrLGKK---IGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRL 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 245 GKVQALISPVMSFVLMALLVIIVGYGGMRVSSGALtTGELVAFILYLV----QIIMPMSQlsmFFTQFQKAIGATERIN 319
Cdd:cd18585 216 ARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGAL-DGALLAMLVFAVlasfEAVAPLPL---AFQYLGETRAAARRLF 290
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
353-561 |
3.48e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 353 EDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLL--ERFYEPTGGAIKLGKESITSYSLQSWRRQIGYVSQDSPL-ID 429
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVeIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 430 GTIRDNICYGVEGEVTD----AEIEKVAAMAYVDAFIH--DLPNGYATEvgERGVKLSGGQRQRIAIARALLRNPQILML 503
Cdd:PRK09580 92 GVSNQFFLQTALNAVRSyrgqEPLDRFDFQDLMEEKIAllKMPEDLLTR--SVNVGFSGGEKKRNDILQMAVLEPELCIL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446376040 504 DEATSSLDSKSESVVQKALNNLMKG-RTTLVIAH--RLSTVVDADKIIFIEKGNLTGSGTH 561
Cdd:PRK09580 170 DESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
357-511 |
8.56e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.60 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 357 VLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLE-RFYEP--TGGAIKLGKESITSYSL------QSWRRQIGYVSQDSPL 427
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGgaPRGARVTGDVTLNGEPLaaidapRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 428 IDGTIRDNICYG------VEGEVT--DAEIEKvAAMAYVDAfihdlpngyATEVGERGVKLSGGQRQRIAIARAL----- 494
Cdd:PRK13547 96 FAFSAREIVLLGrypharRAGALThrDGEIAW-QALALAGA---------TALVGRDVTTLSGGELARVQFARVLaqlwp 165
|
170 180
....*....|....*....|.
gi 446376040 495 ----LRNPQILMLDEATSSLD 511
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTAALD 186
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
27-311 |
8.69e-07 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 51.10 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 27 KGILVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQIVGL-----VAFFVMQTIAAGLSIYLLNYIGQKIVAGLR 101
Cdd:cd18556 1 KLLFFSILFISLLSSILISISPVILAKITDLLTSSSSDSYNYIVVlaalyVITISATKLLGFLSLYLQSSLRVELIISIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 102 ERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSL-IVLFVLDWKMTALLLTVIPLSVL 180
Cdd:cd18556 81 SSYFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIvVILSSGDYFVAALFLLYAVLFVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 181 ILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNT----EKReYETGNTGI----QKLLQFGLKegkvQALIS 252
Cdd:cd18556 161 NNTIFTKKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAfdflFKR-YEATLTNDrnsqKRYWKLTFK----MLILN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 253 PVMSFVLMALLVIIVGYGgmrVSSGALTTGELVAFILYLVQIIMPMSQLSMFFTQFQKA 311
Cdd:cd18556 236 SLLNVILFGLSFFYSLYG---VVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQS 291
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
365-538 |
1.23e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.94 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 365 IESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSySLQSWRRQIGYVSQDSPLIDG-TIRDNI-CYGVEG 442
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLlTGREHLyLYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 443 EVTDAEIEKVAAMAyvdafIHDLpnGYATEVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKAL 522
Cdd:TIGR01257 2041 GVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170
....*....|....*..
gi 446376040 523 NNLMK-GRTTLVIAHRL 538
Cdd:TIGR01257 2114 VSIIReGRAVVLTSHSM 2130
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
356-564 |
2.30e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 356 KVLNNIDFTIESGKVTAIVGPSGSGKTTlFSLLERFYEPTGGAiklgkesiTSYSLQSW-------RRQIGYvsqDSPLI 428
Cdd:NF000106 27 KAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGR--------RPWRF*TWcanrralRRTIG*---HRPVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 429 DG-----TIRDNIcYGVeGEVTDaeIEKVAAMAYVDAFIHDLpnGYATEVGERGVKLSGGQRQRIAIARALLRNPQILML 503
Cdd:NF000106 95 *GrresfSGRENL-YMI-GR*LD--LSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446376040 504 DEATSSLDSKSESVVQKALNNLMK-GRTTLVIAHRLSTVVD-ADKIIFIEKGNLTGSGTHDEL 564
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
335-556 |
2.32e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 335 VSNAKQSIVLEnVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYS-LQS 413
Cdd:PRK09700 257 VSNLAHETVFE-VRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 414 WRRQIGYVSQDSP----LIDGTIRDNICY----------GVEGEVTDAEIEKVAAMAyvdafiHDLPNGYATEVGERGVK 479
Cdd:PRK09700 336 VKKGMAYITESRRdngfFPNFSIAQNMAIsrslkdggykGAMGLFHEVDEQRTAENQ------RELLALKCHSVNQNITE 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 480 LSGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVDA-DKIIFIEKGNLT 556
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLT 488
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
31-185 |
5.51e-06 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 48.56 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 31 VFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQIVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWKKVLV 110
Cdd:cd18584 3 LLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446376040 111 LPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLDWkMTALLLTViplsVLILVPL 185
Cdd:cd18584 83 LGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDW-VSALILLV----TAPLIPL 152
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
361-536 |
1.20e-05 |
|
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: 46.49 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 361 IDFT-IESGKVTAIVGPSGSGKTTLFSLLErfYEPTGGAIKLGKESITSYSLQSwRRQIGYVSQDSPLIDGTIRdnicyg 439
Cdd:cd03279 20 IDFTgLDNNGLFLICGPTGAGKSTILDAIT--YALYGKTPRYGRQENLRSVFAP-GEDTAEVSFTFQLGGKKYR------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 440 vegevtdaeIEKVAAMAYvDAFIHD--LPNGYATEVGERGVK-LSGGQRQRIAIARAL-----LRNP-----QILMLDEA 506
Cdd:cd03279 91 ---------VERSRGLDY-DQFTRIvlLPQGEFDRFLARPVStLSGGETFLASLSLALalsevLQNRggarlEALFIDEG 160
|
170 180 190
....*....|....*....|....*....|.
gi 446376040 507 TSSLDSKSESVVQKALNNL-MKGRTTLVIAH 536
Cdd:cd03279 161 FGTLDPEALEAVATALELIrTENRMVGVISH 191
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
361-558 |
1.21e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 361 IDFtiESGkVTAIVGPSGSGKTTLFSLLerFYEPTGgaiklgkESITSYSLQSWRRQIGYVSQDSPLIDGTIRDNIcyGV 440
Cdd:cd03240 18 IEF--FSP-LTLIVGQNGAGKTTIIEAL--KYALTG-------ELPPNSKGGAHDPKLIREGEVRAQVKLAFENAN--GK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 441 EGEVTdaeiEKVAAMAYVdAFIHD------LPNgyatevgERGvKLSGGQRQ------RIAIARALLRNPQILMLDEATS 508
Cdd:cd03240 84 KYTIT----RSLAILENV-IFCHQgesnwpLLD-------MRG-RCSGGEKVlasliiRLALAETFGSNCGILALDEPTT 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 509 SLDsksESVVQKALNNLMKGRTTL------VIAHRLSTVVDADKIIFIEKGNLTGS 558
Cdd:cd03240 151 NLD---EENIEESLAEIIEERKSQknfqliVITHDEELVDAADHIYRVEKDGRQKS 203
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
29-186 |
2.71e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 46.32 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 29 ILVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQIVGLVAFF-VMQTIAAGLSIYLLNYIGQKIVAGLRERLWKK 107
Cdd:cd18603 4 ILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRDYRLGVYGALgLGQAIFVFLGSLALALGCVRASRNLHNKLLHN 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446376040 108 VLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVlfvldwkmtalLLTVIPLSVLILVPLG 186
Cdd:cd18603 84 ILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVV-----------ISISTPIFLVVIIPLA 151
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
481-569 |
3.05e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 481 SGGQRQRIAIARALLRNPQILMLDEATSSLDSKSESVVQKALnnLMKGRTTLVIAHR---LSTVVdaDKIIFIEKGNLTG 557
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSHArefLNTVV--TDILHLHGQKLVT 421
|
90
....*....|...
gi 446376040 558 -SGTHDELLRTHD 569
Cdd:PLN03073 422 yKGDYDTFERTRE 434
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
358-511 |
3.17e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 358 LNNIDFTIESGKVTAIVGPSGSGKT----TLFSLLERfyepTGGAIKL-GKESITSYSLQSW----------RRQIGYVS 422
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTdiveTLFGIREK----SAGTITLhGKKINNHNANEAInhgfalvteeRRSTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 423 QDSPLIDGTIRDNICYGVEGEVTDAEIEKVAAMAYVDAFIHDLPnGYATEVGErgvkLSGGQRQRIAIARALLRNPQILM 502
Cdd:PRK10982 340 YLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTP-GHRTQIGS----LSGGNQQKVIIGRWLLTQPEILM 414
|
....*....
gi 446376040 503 LDEATSSLD 511
Cdd:PRK10982 415 LDEPTRGID 423
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
342-519 |
5.56e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIklgkesitsysLQSWRRQIGYV 421
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------FRSAKVRMAVF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 422 SQDSplIDGTirdnicygvegevtDAEIEKVAAMAYvdAFIHDLPNGYATEVGERGVK----------LSGGQRQRIAIA 491
Cdd:PLN03073 578 SQHH--VDGL--------------DLSSNPLLYMMR--CFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSRVAFA 639
|
170 180
....*....|....*....|....*....
gi 446376040 492 RALLRNPQILMLDEATSSLDSKS-ESVVQ 519
Cdd:PLN03073 640 KITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
359-552 |
1.20e-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: 42.73 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 359 NNIDFTieSGKVTAIVGPSGSGKTTLFsllerfyeptggaiklgkesitsyslqswrrqigyvsqdsplidgtirDNICY 438
Cdd:cd03227 14 NDVTFG--EGSLTIITGPNGSGKSTIL------------------------------------------------DAIGL 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 439 GVEGEVTDAEIEKVAAMAYVDAFIHdlpngyATEVGERgVKLSGGQRQRIAIARAL----LRNPQILMLDEATSSLDSKS 514
Cdd:cd03227 44 ALGGAQSATRRRSGVKAGCIVAAVS------AELIFTR-LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRD 116
|
170 180 190
....*....|....*....|....*....|....*....
gi 446376040 515 -ESVVQKALNNLMKGRTTLVIAHRLSTVVDADKIIFIEK 552
Cdd:cd03227 117 gQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKK 155
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
350-526 |
1.87e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 350 EYNEDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLERFYEPTGGAIKLGKESITSYSlqswRRQIGYVSQDSPL-I 428
Cdd:PRK13541 8 QFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----KPYCTYIGHNLGLkL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 429 DGTIRDNICYGveGEVTDAEIEKVAAMAYVDafIHDLpngyateVGERGVKLSGGQRQRIAIARALLRNPQILMLDEATS 508
Cdd:PRK13541 84 EMTVFENLKFW--SEIYNSAETLYAAIHYFK--LHDL-------LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170
....*....|....*...
gi 446376040 509 SLDSKSesvvQKALNNLM 526
Cdd:PRK13541 153 NLSKEN----RDLLNNLI 166
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
30-224 |
2.04e-04 |
|
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group represents the transmembrane (TM) domain of an active lipid-linked oligosaccharides flippase PglK (protein glycosylation K), which is a homodimeric ABC transporter that flips a lipid-linked oligosaccharide that serves as a glycan donor in N-linked protein glycosylation. Pglk mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. This TM subunit exhibits the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 349997 Cd Length: 300 Bit Score: 43.69 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 30 LVFALLMSLLST-GASLFIPMLTkgLVDNFSLssISTGQI---------------------VGLVAFFVMQTIAAGLSIY 87
Cdd:cd18553 1 LLFSIFVSLIETiGISAIMPFIS--VASNFSL--ILSNKYykfiynffgfsspvnfviffgIILIGFYIFRSLYNIFYTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 88 LLNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSnLLTGGISIVGSLIVLFVLDWKM 167
Cdd:cd18553 77 LLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNLSQVIQSFLF-ILSEIFVILFIYSLLLYVNWKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 168 TALLLTVIPLSVLILVP-LGRKMYKISKALQDETASFTSVLTQVLSEIRLVKSSNTEK 224
Cdd:cd18553 156 TLVLTLFLGLNVFFITKiVSKKIKKQGKKREESQKKFYKILSETFGNFKIIKLKSNEK 213
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
354-565 |
2.62e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 354 DEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLErfyeptggaiklGKESITSYSLQSWRRQIGYVS--QDSPLIDGT 431
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALA------------GELPLLSGERQSQFSHITRLSfeQLQKLVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 432 IRDNICYGV-EGE----VTDAEI------EKVAAMAYVDAF-IHDLpngyateVGERGVKLSGGQRQRIAIARALLRNPQ 499
Cdd:PRK10938 83 WQRNNTDMLsPGEddtgRTTAEIiqdevkDPARCEQLAQQFgITAL-------LDRRFKYLSTGETRKTLLCQALMSEPD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 500 ILMLDEATSSLDSKSESVVQKALNNLMKGRTTLV-IAHRLSTVVD-ADKIIFIEKGNLTGSGTHDELL 565
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL 223
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
480-568 |
3.11e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 480 LSGGQRQRIAIARALL---RNPQILMLDEATSSLDSKSESVVQKALNNLM-KGRTTLVIAHRLSTVVDADKIIFI--EKG 553
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYVLELgpEGG 889
|
90
....*....|....*....
gi 446376040 554 NLTG----SGTHDELLRTH 568
Cdd:PRK00635 890 NLGGyllaSCSPEELIHLH 908
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
480-548 |
3.35e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.85 E-value: 3.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446376040 480 LSGGQRQRIAIARALLR---NPQILMLDEATSSLD----SKSESVVQKALNnlmKGRTTLVIAHRLSTVVDADKII 548
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHfddiKKLLEVLQRLVD---KGNTVVVIEHNLDVIKTADYII 902
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
29-194 |
3.54e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 42.90 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 29 ILVFALLMSLLSTGASLFIPMLTKGLVDNFSLSSISTGQ--IVGLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWK 106
Cdd:cd18605 4 ILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFINDSFNffLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 107 KVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLdwkMTALLLTVIPLSVLilvplg 186
Cdd:cd18605 84 SILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQ---LPWLLLLLLPLAFI------ 154
|
....*...
gi 446376040 187 rkMYKISK 194
Cdd:cd18605 155 --YYRIQR 160
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
32-218 |
4.01e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 42.83 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 32 FALLMSLLSTGASLFIPMLTKGLVD-------NFSLSSISTGqiVGL-VAFFVMQTIAAGL---SIYLLNYIGQKIVAGL 100
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINfvedaylGGPPPSIGYG--IGYaIGLFLLQLLSSLLlnhFFYRSMLTGAQVRAAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 101 RERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISeHLSNLLTGGISIVGSLIVLFV-LDWkmTALL-LTVIPLS 178
Cdd:cd18597 79 TKAIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALG-FFHFLWTAPIQIIIAIALLIVnLGP--SALVgIGVLILS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446376040 179 VLILVPLGRKMYKISKALQDETASFTSVLTQVLSEIRLVK 218
Cdd:cd18597 156 IPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIK 195
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
29-180 |
5.12e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 42.45 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 29 ILVFALLMSLLSTGASLFIPMLT--KGLVDNFSLSSISTGQIVGLVAFFVMQTIAAGLSIYLLNYIGqkivaGLR----- 101
Cdd:cd18604 4 LLLLFVLSQLLSVGQSWWLGIWAsaYETSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFG-----SLRasrkl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 102 -ERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLdwkMTALLLTVIPLSVL 180
Cdd:cd18604 79 hERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVV---SPAFLLPAVVLAAL 155
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
48-218 |
1.20e-03 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 41.08 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 48 PMLTKGLVDNFSLSSISTGQIV-----GLVAFFVMQTIAAGLSIYLLNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRTG 122
Cdd:cd18594 17 PLLLGRLVAYFVPDSTVTKTEAylyalGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALSKITTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 123 DTISRMTNDTGVVKtLISEHLSNLLTGGIsivgSLIVLFVLDWKMT--------ALLLTVIPLSVLilvpLGRKMYKisk 194
Cdd:cd18594 97 HIVNLLSNDVQKFD-EVLVYLHFLWIAPL----QVIVLTGLLWREIgpsslaglGVLLLLLPLQAY----LGKLFAK--- 164
|
170 180
....*....|....*....|....*...
gi 446376040 195 aLQDETASFTS----VLTQVLSEIRLVK 218
Cdd:cd18594 165 -YRRKTAGLTDervkIMNEIISGMRVIK 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
342-511 |
1.90e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 342 IVLENVHFEYNeDEKVLNNIDFTIESGKVTAIVGPSGSGKTTLFSLLerfyeptGGAIKLGKESIT----SYSLQSWRRQ 417
Cdd:NF033858 2 ARLEGVSHRYG-KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGARKIQQGRVEvlggDMADARHRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 418 ----IGYVSQdsplidG---------TIRDNI-----CYGVEGEVTDAEIEKVAAMAYVDAFiHDLPNGyatevgergvK 479
Cdd:NF033858 74 vcprIAYMPQ------GlgknlyptlSVFENLdffgrLFGQDAAERRRRIDELLRATGLAPF-ADRPAG----------K 136
|
170 180 190
....*....|....*....|....*....|..
gi 446376040 480 LSGGQRQRIAIARALLRNPQILMLDEATSSLD 511
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
341-407 |
2.95e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.22 E-value: 2.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446376040 341 SIVLENvhFEYNEDEKVlnnIDFTiesGKVTAIVGPSGSGKTTLFSLLER-FYEPTGGAIKLGKESIT 407
Cdd:COG0419 4 RLRLEN--FRSYRDTET---IDFD---DGLNLIVGPNGAGKSTILEAIRYaLYGKARSRSKLRSDLIN 63
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
80-180 |
3.40e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 39.89 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 80 IAAGLSIYLLNYIGQKIVAGLRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIV 159
Cdd:cd18602 65 ILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIV 144
|
90 100
....*....|....*....|..
gi 446376040 160 -LFVLDWkmtaLLLTVIPLSVL 180
Cdd:cd18602 145 nAIVTPY----FLIALIPIIIV 162
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
117-318 |
4.24e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 39.40 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 117 DQNRTGDTISRMTNDTGVVkTLISEHLSNLLTGGISIVGSLIVLF-VLDWKM---TALLLTVIPLSVLIlvplGRKMYKI 192
Cdd:cd18596 110 SSASVGKINNLMSVDANRI-SEFAAFLHLLVSAPLQIVIAIVFLYrLLGWSAlvgLAVMVLLLPLNGYL----AKRYSRA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 193 SKALQDETASFTSVLTQVLSEIRLVKSSNTEKREyetgntgIQKLLQFGLKEGKVQalispVMSFVLMALLVIIVGYGGM 272
Cdd:cd18596 185 QKELMKARDARVQLVTEVLQGIRMIKFFAWERKW-------EERILEAREEELKWL-----RKRFLLDLLLSLLWFLIPI 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446376040 273 RVSSGALTT------GEL---VAF-ILYLVQII-MPMSQLSMFFTQFQKAIGATERI 318
Cdd:cd18596 253 LVTVVTFATytlvmgQELtasVAFtSLALFNMLrGPLNVLPELITQLLQAKVSLDRI 309
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
339-384 |
4.82e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 4.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446376040 339 KQSIVLENVHfEYNedekvLNNIDFTIESGKVTAIVGPSGSGKTTL 384
Cdd:PRK00349 612 GKFLKLKGAR-ENN-----LKNVDVEIPLGKFTCVTGVSGSGKSTL 651
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
100-183 |
5.93e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 39.23 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 100 LRERLWKKVLVLPVSYYDQNRTGDTISRMTNDTGVVKTLISEHLSNLLTGGISIVGSLIVLFVLdwkMTALLLTVIPLSV 179
Cdd:cd18601 94 LHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVV---NPWVLIPVIPLVI 170
|
....
gi 446376040 180 LILV 183
Cdd:cd18601 171 LFLF 174
|
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
367-414 |
7.99e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 37.93 E-value: 7.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446376040 367 SGKVTAIVGPSGSGKTTLFSLLERFYE----------PTG-GAIKLGKES-ITSYSLQSW 414
Cdd:pfam13604 17 GDRVAVLVGPAGTGKTTALKALREAWEaagyrviglaPTGrAAKVLGEELgIPADTIAKL 76
|
|
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