|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-567 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 594.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 1 MKRL----KPYWLSITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRI 76
Cdd:COG1132 9 LRRLlrylRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 77 SMGFGKELRDKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFV 156
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 157 VVLPLLLLLVVILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMS 236
Cdd:COG1132 169 LVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 237 PLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERINEVLDMNAEILNPE 316
Cdd:COG1132 249 PLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 317 NPKTSTPPA-KLSFEHVTFRYEGaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREM 395
Cdd:COG1132 329 GAVPLPPVRgEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 396 DQSSLRQKIGLVPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSI 475
Cdd:COG1132 408 TLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAI 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 476 ARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQI 555
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGL 567
|
570
....*....|..
gi 1251574723 556 YQEIMRSQLSEE 567
Cdd:COG1132 568 YARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-564 |
3.92e-128 |
|
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: 391.50 E-value: 3.92e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 1 MKRLKPYWLSITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGF 80
Cdd:COG2274 148 LRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 81 GKELRDKIFTKVEDFSLQEFDKVGTSSLITRTtNDVVQIQNVL-YMMMRLMVMAPIMLLGGIIMAVgRDAKLSLIFVVVL 159
Cdd:COG2274 228 DLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLtGSLLTALLDLLFVLIFLIVLFF-YSPPLALVVLLLI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 160 PLLLLLVVILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLM 239
Cdd:COG2274 306 PLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLS 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 240 MLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERINEVLDMNAEilNPENPK 319
Cdd:COG2274 386 GLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPE--REEGRS 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 320 TSTPPA---KLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMD 396
Cdd:COG2274 464 KLSLPRlkgDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 397 QSSLRQKIGLVPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIA 476
Cdd:COG2274 544 PASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIA 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 477 RSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIY 556
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLY 703
|
....*...
gi 1251574723 557 QEIMRSQL 564
Cdd:COG2274 704 AELVQQQL 711
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
11-302 |
2.10e-118 |
|
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: 352.09 E-value: 2.10e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIFT 90
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 91 KVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVILG 170
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 171 GKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAI 250
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 251 VWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18548 241 LWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
4-564 |
1.19e-103 |
|
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: 323.96 E-value: 1.19e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 4 LKPY-WLSITAVLVLTFGQVIgQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGK 82
Cdd:TIGR02204 13 VRPYrGRVLAALVALLITAAA-TLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 83 ELRDKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLL 162
Cdd:TIGR02204 92 DIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 163 LLLVVILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLL 242
Cdd:TIGR02204 172 LLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 243 MNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERINEVLDMNAEILNPENPKT-S 321
Cdd:TIGR02204 252 VFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTlP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 322 TP-PAKLSFEHVTFRYEG-AEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSS 399
Cdd:TIGR02204 332 VPlRGEIEFEQVNFAYPArPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 400 LRQKIGLVPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSL 479
Cdd:TIGR02204 412 LRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAI 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 480 IRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQEI 559
Cdd:TIGR02204 492 LKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
....*
gi 1251574723 560 MRSQL 564
Cdd:TIGR02204 572 ARLQF 576
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1-566 |
1.14e-101 |
|
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: 318.58 E-value: 1.14e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 1 MKRLKPYWLSITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGF 80
Cdd:TIGR02203 6 WSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 81 GKELRDKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLP 160
Cdd:TIGR02203 86 VRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 161 LLLLLVVILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMM 240
Cdd:TIGR02203 166 VLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 241 LLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERINEVLDmnaeilNPENPKT 320
Cdd:TIGR02203 246 LIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLD------SPPEKDT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 321 STPP-----AKLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREM 395
Cdd:TIGR02203 320 GTRAierarGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 396 DQSSLRQKIGLVPQKAVLFTGTIASNMRYGK-EDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLS 474
Cdd:TIGR02203 400 TLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 475 IARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQ 554
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG 559
|
570
....*....|..
gi 1251574723 555 IYQEIMRSQLSE 566
Cdd:TIGR02203 560 LYAQLHNMQFRE 571
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
83-561 |
3.40e-95 |
|
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: 301.69 E-value: 3.40e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 83 ELRDKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLymmMRL--------------------------MVMAPIM 136
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLY---LRVllpllvallvilaavaflaffspalaLVLALGL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 137 LLGGIIM---AVGRDAKLSlifvvvlplllllvvilggkampmfKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEK 213
Cdd:COG4987 166 LLAGLLLpllAARLGRRAG-------------------------RRLAAARAALRARLTDLLQGAAELAAYGALDRALAR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 214 FEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFiqyAMQIMMSF---MMLSAVFI 290
Cdd:COG4987 221 LDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALL---VLAALALFealAPLPAAAQ 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 291 MIPRAGASAERINEVLDMNAEILNPENPKTSTPPAKLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTL 370
Cdd:COG4987 298 HLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 371 INMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKL 450
Cdd:COG4987 378 LALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAAL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 451 ANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSD 530
Cdd:COG4987 458 PDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMD 537
|
490 500 510
....*....|....*....|....*....|.
gi 1251574723 531 QIIVMNEGKIAGMGTHEELKESNQIYQEIMR 561
Cdd:COG4987 538 RILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
201-570 |
1.47e-93 |
|
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: 298.66 E-value: 1.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 201 VRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMM 280
Cdd:COG5265 231 VKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 281 SFMMLSAVFIMIPRAGASAERINEVLDMNAEILNPENPKT-STPPAKLSFEHVTFRYEgAEKPVIEDITFEANAGETIAI 359
Cdd:COG5265 311 PLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPlVVGGGEVRFENVSFGYD-PERPILKGVSFEVPAGKTVAI 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 360 IGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMRYGKEDATDEEIWEALR 439
Cdd:COG5265 390 VGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAAR 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 440 TAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIV 519
Cdd:COG5265 470 AAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVI 549
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1251574723 520 AQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQEIMRSQLSEEEIA 570
Cdd:COG5265 550 AHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAE 600
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-553 |
6.93e-91 |
|
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: 290.12 E-value: 6.93e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 2 KRLKPY------WLSITAVL-VLTFGQVIGQLYLptlMSNIIDkGVVTGDTDyiWSTGMKMLLISFASVILSVIVVYLAS 74
Cdd:COG4988 6 KRLKRLargarrWLALAVLLgLLSGLLIIAQAWL---LASLLA-GLIIGGAP--LSALLPLLGLLLAVLLLRALLAWLRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 75 RISMGFG----KELRDKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNvlYMM-----MRLMVMAPIMLLG------ 139
Cdd:COG4988 80 RAAFRAAarvkRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDG--YFArylpqLFLAALVPLLILVavfpld 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 140 ---GIIMAVGrdAKLslifvvvlplllllvvilggkaMPMF---------KSLQKKMDKLNR-------VIReGLTGIRV 200
Cdd:COG4988 158 wlsGLILLVT--APL----------------------IPLFmilvgkgaaKASRRQWRALARlsghfldRLR-GLTTLKL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 201 vrsFNRNEDELEKFEEANADYATTAIKVNRllslmsplmmllmnltsIAIVwigSIFigngdmqVGDLMAFIQYAM---Q 277
Cdd:COG4988 213 ---FGRAKAEAERIAEASEDFRKRTMKVLR-----------------VAFL---SSA-------VLEFFASLSIALvavY 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 278 IMMSFM-----MLSAVFIMI-------P-R-----------AGASAERINEVLDMNAEILNPEN-PKTSTPPAKLSFEHV 332
Cdd:COG4988 263 IGFRLLggsltLFAALFVLLlapefflPlRdlgsfyharanGIAAAEKIFALLDAPEPAAPAGTaPLPAAGPPSIELEDV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 333 TFRYEGaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAV 412
Cdd:COG4988 343 SFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPY 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 413 LFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSF 492
Cdd:COG4988 422 LFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPT 501
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251574723 493 SALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESN 553
Cdd:COG4988 502 AHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
327-558 |
5.23e-88 |
|
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: 271.80 E-value: 5.23e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGL 406
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIY 486
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 487 IFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQE 558
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
327-563 |
6.29e-84 |
|
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: 261.40 E-value: 6.29e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGL 406
Cdd:cd03253 1 IEFENVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIY 486
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 487 IFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQEIMRSQ 563
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
325-553 |
7.63e-81 |
|
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: 252.92 E-value: 7.63e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 325 AKLSFEHVTFRYEGaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKI 404
Cdd:cd03254 1 GEIEFENVNFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 405 GLVPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPE 484
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 485 IYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESN 553
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-556 |
2.82e-80 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 266.20 E-value: 2.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 1 MKRL----KPYWLSITAVLVLTFGQVIGQLYLPTLMSNIIDkgVVTGDTDY------IWStgmkMLLISFASVILSV--- 67
Cdd:TIGR00958 149 LFRLlglsGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVID--TLGGDKGPpalasaIFF----MCLLSIASSVSAGlrg 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 68 -IVVYLASRISMgfgkELRDKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVG 146
Cdd:TIGR00958 223 gSFNYTMARINL----RIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLW 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 147 RDAKLSLIFVVVLPLLLLLVVILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAI 226
Cdd:TIGR00958 299 LSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 227 KVNRLLSLMSPLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERINEVL 306
Cdd:TIGR00958 379 RKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYL 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 307 DMNAEIlnpENPKTSTPP---AKLSFEHVTFRYEG-AEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVES 382
Cdd:TIGR00958 459 DRKPNI---PLTGTLAPLnleGLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 383 GVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGG 462
Cdd:TIGR00958 536 GQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 463 NNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAEttEAVTLIVAQRITSVVNSDQIIVMNEGKIAG 542
Cdd:TIGR00958 616 SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA--SRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
570
....*....|....
gi 1251574723 543 MGTHEELKESNQIY 556
Cdd:TIGR00958 694 MGTHKQLMEDQGCY 707
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
246-563 |
1.27e-79 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 261.43 E-value: 1.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 246 TSIAIVWIGSIFIGNGDMQVGDLMAFIQYAmQIMMSfmMLSAVFIMIPRAGASAERINEVLDMNAEILNPENPKTSTPPA 325
Cdd:PRK13657 253 TMLAILVLGAALVQKGQLRVGEVVAFVGFA-TLLIG--RLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLS----FEHVTFRYEGAeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLR 401
Cdd:PRK13657 330 RVKgaveFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 402 QKIGLVPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIR 481
Cdd:PRK13657 409 RNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 482 KPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQEIMR 561
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLR 568
|
..
gi 1251574723 562 SQ 563
Cdd:PRK13657 569 AQ 570
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
329-563 |
1.38e-77 |
|
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: 244.76 E-value: 1.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 329 FEHVTFRY-EGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLV 407
Cdd:cd03249 3 FKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 408 PQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYI 487
Cdd:cd03249 83 SQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 488 FDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQEIMRSQ 563
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
326-545 |
5.11e-69 |
|
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: 221.98 E-value: 5.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIG 405
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKAVLFTGTIASNMRYGKEdATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEI 485
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 486 YIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGT 545
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
327-539 |
2.61e-68 |
|
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: 218.41 E-value: 2.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGL 406
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTGTIASNMrygkedatdeeiwealrtaqaenfvsklanglgsrveqggnnFSGGQKQRLSIARSLIRKPEIY 486
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1251574723 487 IFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGK 539
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
246-564 |
1.13e-61 |
|
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: 215.59 E-value: 1.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 246 TSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERINEVLDMNaeilnPENPKTSTPPA 325
Cdd:TIGR03797 372 TSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEAL-----PEVDEAKTDPG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLS----FEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLR 401
Cdd:TIGR03797 447 KLSgaieVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVR 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 402 QKIGLVPQKAVLFTGTIASNMrYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIR 481
Cdd:TIGR03797 527 RQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVR 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 482 KPEIYIFDDSFSALDFKTDAKLREALKAettEAVTLIV-AQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQEIM 560
Cdd:TIGR03797 606 KPRILLFDEATSALDNRTQAIVSESLER---LKVTRIViAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLA 682
|
....
gi 1251574723 561 RSQL 564
Cdd:TIGR03797 683 RRQL 686
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
294-566 |
1.52e-61 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 213.34 E-value: 1.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 294 RAGASAERINEVLDMNAEIlnpENPKTSTPPAK--LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLI 371
Cdd:PRK11176 310 RGMAACQTLFAILDLEQEK---DEGKRVIERAKgdIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIA 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 372 NMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMRYGKEDA-TDEEIWEALRTAQAENFVSKL 450
Cdd:PRK11176 387 NLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKM 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 451 ANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSD 530
Cdd:PRK11176 467 DNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKAD 546
|
250 260 270
....*....|....*....|....*....|....*.
gi 1251574723 531 QIIVMNEGKIAGMGTHEELKESNQIYQEIMRSQLSE 566
Cdd:PRK11176 547 EILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
327-563 |
8.78e-61 |
|
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: 201.18 E-value: 8.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGL 406
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIY 486
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 487 IFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQEIMRSQ 563
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-535 |
3.69e-60 |
|
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: 208.29 E-value: 3.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 8 WLSITAVL-VLTFGQVIGQLYLptlMSNIIDKGVVTG-DTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELR 85
Cdd:TIGR02857 4 ALALLALLgVLGALLIIAQAWL---LARVVDGLISAGePLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 86 DKIFTKVEDF--SLQEFDKVGT-SSLITRTTNDVV----QIQNVLYMMMR-----LMVMAPIMLLGGIIMAVgrDAKLsl 153
Cdd:TIGR02857 81 ERLLEAVAALgpRWLQGRPSGElATLALEGVEALDgyfaRYLPQLVLAVIvplaiLAAVFPQDWISGLILLL--TAPL-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 154 ifvvvlplllllvvilggkaMPMFKSL------------QKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADY 221
Cdd:TIGR02857 157 --------------------IPIFMILigwaaqaaarkqWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 222 ATTAIKVNRLLSLMSPLMMLLMNLtSIAIVwigSIFIG----NGDMQ-VGDLMAFIqYAMQIMMSFMMLSAVFIMIPRAG 296
Cdd:TIGR02857 217 RERTMRVLRIAFLSSAVLELFATL-SVALV---AVYIGfrllAGDLDlATGLFVLL-LAPEFYLPLRQLGAQYHARADGV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 297 ASAERINEVLDMNAEILNPENPKTSTPPAKLSFEHVTFRYEGAEkPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPR 376
Cdd:TIGR02857 292 AAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 377 FYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGS 456
Cdd:TIGR02857 371 FVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDT 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 457 RVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVM 535
Cdd:TIGR02857 451 PIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
9-569 |
4.09e-59 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 206.49 E-value: 4.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 9 LSITAVLvltfgqvigQLYLPTLMSNIIDkGVVTGDtdyiWSTGMKMLLIsfASVILSVIVVYLAS---RISMgFGK--- 82
Cdd:PRK10789 4 LIIIAML---------QLIPPKVVGIIVD-GVTEQH----MTTGQILMWI--GTMVLIAVVVYLLRyvwRVLL-FGAsyq 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 83 ---ELRDKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQI-----QNVLYMMMRLmVMAPIMLlggIIMAVGRDAKLSLI 154
Cdd:PRK10789 67 lavELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVvfaagEGVLTLVDSL-VMGCAVL---IVMSTQISWQLTLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 155 FVVVLPLLLLLVVILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSL 234
Cdd:PRK10789 143 ALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDAR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 235 MSPLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERINEVLdmnAEILN 314
Cdd:PRK10789 223 FDPTIYIAIGMANLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAML---AEAPV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 315 PENPKTSTPPAK--LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDV 392
Cdd:PRK10789 300 VKDGSEPVPEGRgeLDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 393 REMDQSSLRQKIGLVPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQR 472
Cdd:PRK10789 380 TKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQR 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 473 LSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKES 552
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
570
....*....|....*..
gi 1251574723 553 NQIYQEIMRSQLSEEEI 569
Cdd:PRK10789 540 SGWYRDMYRYQQLEAAL 556
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
326-540 |
1.72e-58 |
|
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: 194.35 E-value: 1.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIG 405
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEI 485
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1251574723 486 YIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKI 540
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
246-563 |
1.13e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 202.36 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 246 TSIAIVWIGSIFIGnGDMQVGDLMAfiqyamqiMMSFMMLSAVFIMIPRAGA---------SAERINEVLDMNAEILNPE 316
Cdd:PRK11160 258 TVVLMLWLAAGGVG-GNAQPGALIA--------LFVFAALAAFEALMPVAGAfqhlgqviaSARRINEITEQKPEVTFPT 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 317 NPKTSTPPAKLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMD 396
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 397 QSSLRQKIGLVPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKlANGLGSRVEQGGNNFSGGQKQRLSIA 476
Cdd:PRK11160 409 EAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIA 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 477 RSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIY 556
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRY 567
|
....*..
gi 1251574723 557 QEIMRSQ 563
Cdd:PRK11160 568 YQLKQRL 574
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
174-559 |
2.07e-56 |
|
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: 201.51 E-value: 2.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 174 MPMFKSL-QKKMDK---LNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIA 249
Cdd:TIGR01193 316 KRTFNKLnHDAMQAnavLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVV 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 250 IVWIGSIFIGNGDMQVGDLMAFiqyamQIMMSFMM--LSAVFIMIPR---AGASAERINEVLDMNAEILNP-ENPKTSTP 323
Cdd:TIGR01193 396 ILWTGAYLVMRGKLTLGQLITF-----NALLSYFLtpLENIINLQPKlqaARVANNRLNEVYLVDSEFINKkKRTELNNL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 324 PAKLSFEHVTFRYeGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQK 403
Cdd:TIGR01193 471 NGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQKAVLFTGTIASNMRYG-KEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRK 482
Cdd:TIGR01193 550 INYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 483 PEIYIFDDSFSALDFKTDAKLREALkAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQEI 559
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
326-545 |
5.86e-54 |
|
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: 181.84 E-value: 5.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIG 405
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKAVLFTGTIASNM-RYGKEDatDEEIWEALrtaqaenfvsklanglgsRVEQGGNNFSGGQKQRLSIARSLIRKPE 484
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251574723 485 IYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGT 545
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
202-522 |
1.99e-53 |
|
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: 189.88 E-value: 1.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 202 RSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMS 281
Cdd:TIGR02868 207 VASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 282 FMMLSAVFIMIPRAGASAERINEVLDMNAEILNPENPKTSTPPAK---LSFEHVTFRYEGAEkPVIEDITFEANAGETIA 358
Cdd:TIGR02868 287 FAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGkptLELRDLSAGYPGAP-PVLDGVSLDLPPGERVA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 359 IIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMRYGKEDATDEEIWEAL 438
Cdd:TIGR02868 366 ILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 439 RTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLI 518
Cdd:TIGR02868 446 ERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVL 525
|
....
gi 1251574723 519 VAQR 522
Cdd:TIGR02868 526 ITHH 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
326-540 |
9.43e-53 |
|
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: 179.59 E-value: 9.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSFEHVTFRYEG-AEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKI 404
Cdd:cd03248 11 IVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 405 GLVPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPE 484
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 485 IYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKI 540
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-570 |
3.59e-52 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 188.00 E-value: 3.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 1 MKRL----KPYWLSITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKM--LLISFASVILSVIVVYLAS 74
Cdd:PRK10790 11 LKRLlaygSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVAGLAAayVGLQLLAAGLHYAQSLLFN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 75 RISMGFGKELRdkifTKVEDFSLQ----EFDKVGTSSLITRTTNDVVQIQNvLYMMMRLMVMAPIMLLGGIIMAV-GRDA 149
Cdd:PRK10790 91 RAAVGVVQQLR----TDVMDAALRqplsAFDTQPVGQLISRVTNDTEVIRD-LYVTVVATVLRSAALIGAMLVAMfSLDW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 150 KLSLIFVVVLPLLLLLVVILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVN 229
Cdd:PRK10790 166 RMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 230 RLLSLMSPLMMLLMNltsiAIVWIGSI----FIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERINEV 305
Cdd:PRK10790 246 RLDGFLLRPLLSLFS----ALILCGLLmlfgFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 306 LDMNAEIL-NPENPKTStppAKLSFEHVTFRYeGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGV 384
Cdd:PRK10790 322 MDGPRQQYgNDDRPLQS---GRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 385 VKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMRYGKeDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNN 464
Cdd:PRK10790 398 IRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 465 FSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAeTTEAVTLIV-AQRITSVVNSDQIIVMNEGKIAGM 543
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA-VREHTTLVViAHRLSTIVEADTILVLHRGQAVEQ 555
|
570 580
....*....|....*....|....*..
gi 1251574723 544 GTHEELKESNQIYQEIMRSQLSEEEIA 570
Cdd:PRK10790 556 GTHQQLLAAQGRYWQMYQLQLAGEELA 582
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
274-549 |
1.57e-47 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 179.16 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 274 YAMQIMMsfmMLSAVFIMIPRAGAS---AERINEVLDMNAE---ILNPENPKTSTPPA-KLSFEHVTFRYEGAEKPVIED 346
Cdd:PLN03130 1181 YALNITS---LLTAVLRLASLAENSlnaVERVGTYIDLPSEaplVIENNRPPPGWPSSgSIKFEDVVLRYRPELPPVLHG 1257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 347 ITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMRYGK 426
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFN 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 427 EDaTDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREA 506
Cdd:PLN03130 1338 EH-NDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKT 1416
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1251574723 507 LKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEEL 549
Cdd:PLN03130 1417 IREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
57-549 |
3.67e-47 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 177.86 E-value: 3.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 57 LISFASVILSVIVVYLASRISMGFGKELRDKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQI-QNVLYMMMRLMVMAPI 135
Cdd:PLN03232 958 LLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIdRNVANLMNMFMNQLWQ 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 136 ML----LGGIIMAVGRDAKLSLIFVVVLplllllvvilggkAMPMFKSLQKKMDKLNRVIRE-----------GLTGIRV 200
Cdd:PLN03232 1038 LLstfaLIGTVSTISLWAIMPLLILFYA-------------AYLYYQSTSREVRRLDSVTRSpiyaqfgealnGLSSIRA 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 201 VRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLmnltsiaIVWIGSIFI----GNGDMQVGdlmafIQYAM 276
Cdd:PLN03232 1105 YKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGV-------MIWLTATFAvlrnGNAENQAG-----FASTM 1172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 277 QIMMSFM-----MLSAVFIMIPRAGAS---AERINEVLDMNAE---ILNPENPKTSTPPA-KLSFEHVTFRYEGAEKPVI 344
Cdd:PLN03232 1173 GLLLSYTlnittLLSGVLRQASKAENSlnsVERVGNYIDLPSEataIIENNRPVSGWPSRgSIKFEDVHLRYRPGLPPVL 1252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 345 EDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMRY 424
Cdd:PLN03232 1253 HGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDP 1332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 425 GKEDaTDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLR 504
Cdd:PLN03232 1333 FSEH-NDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1251574723 505 EALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEEL 549
Cdd:PLN03232 1412 RTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
7-302 |
5.41e-47 |
|
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: 166.07 E-value: 5.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 7 YWLSITAVLVLTfgqvIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRD 86
Cdd:cd18542 1 YLLAILALLLAT----ALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 87 KIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLV 166
Cdd:cd18542 77 DLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 167 VILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLT 246
Cdd:cd18542 157 YVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQ 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 247 SIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18542 237 IVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
296-566 |
7.17e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 173.11 E-value: 7.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 296 GAsAERINEVLDMN-AEILNPENPKTSTPPAKLSFEH-VTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINM 373
Cdd:PRK11174 319 GA-AESLVTFLETPlAHPQQGEKELASNDPVTIEAEDlEILSPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 374 IPRFYDVEsGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANG 453
Cdd:PRK11174 396 LLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 454 LGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQII 533
Cdd:PRK11174 475 LDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIW 554
|
250 260 270
....*....|....*....|....*....|...
gi 1251574723 534 VMNEGKIAGMGTHEELKESNQIYQEIMRSQLSE 566
Cdd:PRK11174 555 VMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
294-548 |
2.20e-46 |
|
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: 171.08 E-value: 2.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 294 RAGASAERINEVLDMNAeilnPENPKTSTPP--AKLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLI 371
Cdd:COG4618 300 SARQAYRRLNELLAAVP----AEPERMPLPRpkGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 372 NMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNM-RYGkeDATDEEIWEALRTAQAENFVSKL 450
Cdd:COG4618 376 RLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 451 ANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVT-LIVAQRITSVVNS 529
Cdd:COG4618 454 PDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATvVVITHRPSLLAAV 533
|
250
....*....|....*....
gi 1251574723 530 DQIIVMNEGKIAGMGTHEE 548
Cdd:COG4618 534 DKLLVLRDGRVQAFGPRDE 552
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
11-302 |
1.95e-45 |
|
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: 161.95 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIFT 90
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 91 KVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVILG 170
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 171 GKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAI 250
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 251 VWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
193-561 |
7.66e-42 |
|
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: 162.04 E-value: 7.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 193 EGLTGIRVVRSFNRNEDELEKFE---EANADYATTAIKVNRLLSLMSPLMMLlmnltsiAIVWIGSIF--IGNGDMQVGD 267
Cdd:TIGR00957 1149 ETLLGVSVIRAFEEQERFIHQSDlkvDENQKAYYPSIVANRWLAVRLECVGN-------CIVLFAALFavISRHSLSAGL 1221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 268 LMAFIQYAMQI---------MMSFMMLSAVfimipragaSAERINEVLDMNAE---ILNPENPKTSTPP-AKLSFEHVTF 334
Cdd:TIGR00957 1222 VGLSVSYSLQVtfylnwlvrMSSEMETNIV---------AVERLKEYSETEKEapwQIQETAPPSGWPPrGRVEFRNYCL 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 335 RYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLF 414
Cdd:TIGR00957 1293 RYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLF 1372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 415 TGTIASNMR-YGKedATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFS 493
Cdd:TIGR00957 1373 SGSLRMNLDpFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 494 ALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQEIMR 561
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
327-564 |
8.75e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.82 E-value: 8.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREmDQSSLRQKIGL 406
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTG-TIASNMR-----YGKEDATDEE-IWEALRTAQaenfvskLANGLGSRVEqggnNFSGGQKQRLSIARSL 479
Cdd:COG1131 78 VPQEPALYPDlTVRENLRffarlYGLPRKEARErIDELLELFG-------LTDAADRKVG----TLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 480 IRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIV-------AQRItsvvnSDQIIVMNEGKIAGMGTHEELKES 552
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLsthyleeAERL-----CDRVAIIDKGRIVADGTPDELKAR 221
|
250
....*....|....
gi 1251574723 553 --NQIYQEIMRSQL 564
Cdd:COG1131 222 llEDVFLELTGEEA 235
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
327-540 |
3.08e-39 |
|
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: 141.20 E-value: 3.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGL 406
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTGTIASNMrygkedatdeeiwealrtaqaenfvsklanglgsrveqggnnFSGGQKQRLSIARSLIRKPEIY 486
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1251574723 487 IFDDSFSALDFKTDAKLREALKAETTEAVTLI-VAQRITSVVNSDQIIVMNEGKI 540
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIvIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
327-549 |
5.30e-39 |
|
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: 142.47 E-value: 5.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGL 406
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAV--LFTGTIAS-------NMRYGKEDAtDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIAR 477
Cdd:COG1122 80 VFQNPDdqLFAPTVEEdvafgpeNLGLPREEI-RERVEEALELVGLEHLADRPPHEL-----------SGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 478 SLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVA-QRITSVV-NSDQIIVMNEGKIAGMGTHEEL 549
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAeLADRVIVLDDGRIVADGTPREV 221
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
326-549 |
7.64e-39 |
|
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: 143.13 E-value: 7.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIG 405
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKAVLFTGTIASNMRYGKEdATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEI 485
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 486 YIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEEL 549
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENL 241
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
327-539 |
1.29e-38 |
|
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: 140.68 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAE---KPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvremdqsslrqK 403
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQKAVLFTGTIASNMRYGKEdaTDEE-IWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRK 482
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP--FDEErYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 483 PEIYIFDDSFSALDFKTDAKL-----REALKAETTeavTLIVAQRITSVVNSDQIIVMNEGK 539
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIfenciLGLLLNNKT---RILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
328-539 |
9.30e-38 |
|
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: 138.37 E-value: 9.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 328 SFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLV 407
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 408 PQKA--VLFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVsklanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEI 485
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELV-----GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 486 YIFDDSFSALDFKTDAKLREALKAETTEAVTLIVaqrITSVVN-----SDQIIVMNEGK 539
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIII---VTHDLDlllelADRVIVLEDGK 211
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
11-302 |
2.69e-37 |
|
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: 139.85 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYLPTLMSNIIDK------GVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKEL 84
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLiieglgGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 85 RDKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLL 164
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 165 LVVILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMN 244
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 245 LTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
327-570 |
6.46e-37 |
|
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: 137.30 E-value: 6.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDqSSLRQKIGL 406
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTG-TIASNMRYgkeDATDEEIWEALRTAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEI 485
Cdd:COG4555 79 LPDERGLYDRlTVRENIRY---FAELYGLFDEELKKRIEELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 486 YIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVN--SDQIIVMNEGKIAGMGTHEELKES---NQIYQEIM 560
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEalCDRVVILHKGKVVAQGSLDELREEigeENLEDAFV 233
|
250
....*....|
gi 1251574723 561 RSQLSEEEIA 570
Cdd:COG4555 234 ALIGSEEGEA 243
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
327-544 |
1.69e-36 |
|
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: 134.95 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVreMDQSSLRQKIGL 406
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTG-TIASNMRYG------KEDATDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSL 479
Cdd:cd03259 77 VFQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251574723 480 IRKPEIYIFDDSFSALDFKTDAKLREALKAetteavtLIVAQRITSVVN----------SDQIIVMNEGKIAGMG 544
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKE-------LQRELGITTIYVthdqeealalADRIAVMNEGRIVQVG 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
252-549 |
3.94e-36 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 144.79 E-value: 3.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 252 WIGSIFIGNGDMQVGDLM----AFI---QYAMQiMMSFMMLSAvfimipRAGASAERINEVLDMNAEILNPEN-----PK 319
Cdd:PTZ00265 1086 WFGSFLIRRGTILVDDFMkslfTFLftgSYAGK-LMSLKGDSE------NAKLSFEKYYPLIIRKSNIDVRDNggiriKN 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 320 TSTPPAKLSFEHVTFRYEGAEK-PVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVE----------------- 381
Cdd:PTZ00265 1159 KNDIKGKIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtn 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 382 -------------------------------------SGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMRY 424
Cdd:PTZ00265 1239 eqdyqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKF 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 425 GKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLR 504
Cdd:PTZ00265 1319 GKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1251574723 505 EAL-----KAETTeavTLIVAQRITSVVNSDQIIVMNEGKIAGM-----GTHEEL 549
Cdd:PTZ00265 1399 KTIvdikdKADKT---IITIAHRIASIKRSDKIVVFNNPDRTGSfvqahGTHEEL 1450
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
344-490 |
6.10e-36 |
|
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: 131.62 E-value: 6.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 344 IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTG-TIASNM 422
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 423 RYGkedATDEEIWEALRTAQAENFVSKLANG--LGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDD 490
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
327-549 |
3.81e-35 |
|
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: 131.92 E-value: 3.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEkpVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVE-----SGVVKINGIDVREMDQS--S 399
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 400 LRQKIGLVPQKAVLFTGTIASNMRYG-------KEDATDEEIWEALRTAQAENFVSKLANGLGsrveqggnnFSGGQKQR 472
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 473 LSIARSLIRKPEIYIFDDSFSALDFKTDAKLREA---LKAETTeavTLIV------AQRItsvvnSDQIIVMNEGKIAGM 543
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELiaeLKKEYT---IVIVthnmqqAARV-----ADRTAFLLNGRLVEF 221
|
....*.
gi 1251574723 544 GTHEEL 549
Cdd:cd03260 222 GPTEQI 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
327-540 |
5.67e-35 |
|
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: 129.74 E-value: 5.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMdQSSLRQKIGL 406
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTGTIASNmrygkedatdeeiwealrtaqaenfvsklangLGSRveqggnnFSGGQKQRLSIARSLIRKPEIY 486
Cdd:cd03247 80 LNQRPYLFDTTLRNN--------------------------------LGRR-------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 487 IFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKI 540
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
327-549 |
5.82e-35 |
|
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: 132.09 E-value: 5.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGL 406
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVL---FT-------GTIASNMRYGKEDATDEEI-WEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSI 475
Cdd:COG1120 80 VPQEPPApfgLTvrelvalGRYPHLGLFGRPSAEDREAvEEALERTGLEHLADRPVDEL-----------SGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 476 ARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEA-VTLIV-------AQRItsvvnSDQIIVMNEGKIAGMGTHE 547
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgRTVVMvlhdlnlAARY-----ADRLVLLKDGRIVAQGPPE 223
|
..
gi 1251574723 548 EL 549
Cdd:COG1120 224 EV 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
312-554 |
9.59e-35 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 140.68 E-value: 9.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 312 ILNPENPKTSTP----PAKLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKI 387
Cdd:PTZ00243 1290 VIEPASPTSAAPhpvqAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 388 NGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMRYGKEdATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSG 467
Cdd:PTZ00243 1370 NGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSV 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 468 GQKQRLSIARSLIRKPEIYIFDDSFS-----ALDFKTDAKLREALKAETteavTLIVAQRITSVVNSDQIIVMNEGKIAG 542
Cdd:PTZ00243 1449 GQRQLMCMARALLKKGSGFILMDEATanidpALDRQIQATVMSAFSAYT----VITIAHRLHTVAQYDKIIVMDHGAVAE 1524
|
250
....*....|..
gi 1251574723 543 MGTHEELKESNQ 554
Cdd:PTZ00243 1525 MGSPRELVMNRQ 1536
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
15-302 |
1.35e-34 |
|
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: 132.30 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 15 LVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYL----ASRISMgfgkELRDKIFT 90
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLfniaGERIVA----RLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 91 KVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVILG 170
Cdd:cd18557 78 SLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 171 GKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAI 250
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 251 VWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18557 238 LWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
323-549 |
1.01e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 131.37 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 323 PPAKLSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVremdqSSL-- 400
Cdd:COG3842 2 AMPALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 401 -RQKIGLVPQKAVLFTG-TIASNMRYG------KEDATDEEIWEALR----TAQAENFVSKLanglgsrveqggnnfSGG 468
Cdd:COG3842 75 eKRNVGMVFQDYALFPHlTVAENVAFGlrmrgvPKAEIRARVAELLElvglEGLADRYPHQL---------------SGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 469 QKQRLSIARSLIRKPEIYIFDDSFSALdfktDAKLREALKAE----------TT--------EAVTLivaqritsvvnSD 530
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSAL----DAKLREEMREElrrlqrelgiTFiyvthdqeEALAL-----------AD 204
|
250
....*....|....*....
gi 1251574723 531 QIIVMNEGKIAGMGTHEEL 549
Cdd:COG3842 205 RIAVMNDGRIEQVGTPEEI 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
327-548 |
1.15e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 128.28 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMdqsslRQKIGL 406
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKA-------------VL--FTGTIASNMRYGKEDatDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQ 471
Cdd:COG1121 80 VPQRAevdwdfpitvrdvVLmgRYGRRGLFRRPSRAD--REAVDEALERVGLEDLADRPIGEL-----------SGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 472 RLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVA----QRITSVVnsDQIIVMNEGKIAgMGTHE 547
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVthdlGAVREYF--DRVLLLNRGLVA-HGPPE 223
|
.
gi 1251574723 548 E 548
Cdd:COG1121 224 E 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
327-540 |
1.60e-33 |
|
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: 125.59 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREmDQSSLRQKIGL 406
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFtgtiasnmrygkEDATdeeIWEALRtaqaenfvsklanglgsrveqggnnFSGGQKQRLSIARSLIRKPEIY 486
Cdd:cd03230 78 LPEEPSLY------------ENLT---VRENLK-------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 487 IFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNS--DQIIVMNEGKI 540
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlcDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
327-540 |
1.61e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.85 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGL 406
Cdd:COG4619 1 LELEGLSFRVGG--KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTGTIASNMRYG---KEDATDEEiwealrtaQAENFVSKLanGLGSRV-EQGGNNFSGGQKQRLSIARSLIRK 482
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPfqlRERKFDRE--------RALELLERL--GLPPDIlDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 483 PEIYIFDDSFSALDFKTDAKLREALKAETTEA-VTLIV-------AQRItsvvnSDQIIVMNEGKI 540
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEgRAVLWvshdpeqIERV-----ADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
328-539 |
2.43e-33 |
|
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: 124.66 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 328 SFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLV 407
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 408 PQkavlftgtiasnmrygkedatdeeiwealrtaqaenfvsklanglgsrveqggnnFSGGQKQRLSIARSLIRKPEIYI 487
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 488 FDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVN--SDQIIVMNEGK 539
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAElaADRVIVLKDGK 157
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
11-282 |
5.86e-33 |
|
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: 127.37 E-value: 5.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISF--ASVILSVIVVYLASRISMGFGKELRDKI 88
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLglAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 89 FTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVI 168
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 169 LGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSI 248
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 1251574723 249 AIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSF 282
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
327-549 |
6.47e-33 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 126.26 E-value: 6.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGL 406
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLF--------TGTIASNMRYGKEDAtDEEIWEALRtaqaenFVSKLANGLGSRVEqggNNFSGGQKQRLSIARS 478
Cdd:cd03295 80 VIQQIGLFphmtveenIALVPKLLKWPKEKI-RERADELLA------LVGLDPAEFADRYP---HELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 479 LIRKPEIYIFDDSFSALDFKTDAKLREA---LKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEEL 549
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEfkrLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
330-544 |
7.49e-33 |
|
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: 124.08 E-value: 7.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 330 EHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQ 409
Cdd:cd03214 3 ENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 410 kavlftgtiasnmrygkedatdeeiweALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSLIRKPEIYIFD 489
Cdd:cd03214 81 ---------------------------ALELLGLAHLADRPFNEL-----------SGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1251574723 490 DSFSALDFKTDAKLREALKAETTEAVTLIV--------AQRItsvvnSDQIIVMNEGKIAGMG 544
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVmvlhdlnlAARY-----ADRVILLKDGRIVAQG 180
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
325-549 |
8.49e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 128.65 E-value: 8.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 325 AKLSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSslRQKI 404
Cdd:COG3839 2 ASLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 405 GLVPQKAVLF-TGTIASNMRYG------KEDATDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIAR 477
Cdd:COG3839 78 AMVFQSYALYpHMTVYENIAFPlklrkvPKAEIDRRVREAAELLGLEDLLDRKPKQL-----------SGGQRQRVALGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 478 SLIRKPEIYIFDDSFSALdfktDAKLREALKAE----------TT--------EAVTLivaqritsvvnSDQIIVMNEGK 539
Cdd:COG3839 147 ALVREPKVFLLDEPLSNL----DAKLRVEMRAEikrlhrrlgtTTiyvthdqvEAMTL-----------ADRIAVMNDGR 211
|
250
....*....|
gi 1251574723 540 IAGMGTHEEL 549
Cdd:COG3839 212 IQQVGTPEEL 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
326-570 |
1.40e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 126.28 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIG 405
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKA-VLFTG-TIASNMRYGKE------DATDEEIWEALRTAQAENFvsklanglgsrVEQGGNNFSGGQKQRLSIAR 477
Cdd:PRK13635 85 MVFQNPdNQFVGaTVQDDVAFGLEnigvprEEMVERVDQALRQVGMEDF-----------LNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 478 SLIRKPEIYIFDDSFSALDFKTDAKLREA---LKAETTEAVtLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQ 554
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETvrqLKEQKGITV-LSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGH 232
|
250 260
....*....|....*....|....*
gi 1251574723 555 IYQEI---------MRSQLSEEEIA 570
Cdd:PRK13635 233 MLQEIgldvpfsvkLKELLKRNGIL 257
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
297-549 |
3.91e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 130.02 E-value: 3.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 297 ASAERINEVLDMNAEILNPENPKTSTPPAkLSFEHVTFRYE---GAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINM 373
Cdd:COG1123 232 AAPQALAAVPRLGAARGRAAPAAAAAEPL-LEVRNLSKRYPvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 374 IPRFYDVESGVVKINGIDVREMDQSS---LRQKIGLVPQ--KAVLFTG-TIAsnmrygkedatdEEIWEALR------TA 441
Cdd:COG1123 311 LLGLLRPTSGSILFDGKDLTKLSRRSlreLRRRVQMVFQdpYSSLNPRmTVG------------DIIAEPLRlhgllsRA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 442 QAENFVSKLAN--GLGSRV------EqggnnFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTE 513
Cdd:COG1123 379 ERRERVAELLErvGLPPDLadryphE-----LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRE 453
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1251574723 514 A-VTLIVaqrIT---SVVN--SDQIIVMNEGKIAGMGTHEEL 549
Cdd:COG1123 454 LgLTYLF---IShdlAVVRyiADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
11-302 |
1.09e-31 |
|
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: 124.07 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIFT 90
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 91 KVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVILG 170
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 171 GKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAI 250
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 251 VWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
327-549 |
2.25e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 127.71 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTL----INMIPRFYDVeSGVVKINGIDVREMDQSSLRQ 402
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLalalMGLLPHGGRI-SGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 403 KIGLVPQ--KAVLFTGTIAsnmrygkedatdEEIWEALRT-----AQAENFVSKLAN--GLGSRVEQGGNNFSGGQKQRL 473
Cdd:COG1123 84 RIGMVFQdpMTQLNPVTVG------------DQIAEALENlglsrAEARARVLELLEavGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 474 SIARSLIRKPEIYIFDDSFSALDFKTDA---KLREALKAETTEAVTLI------VAQRitsvvnSDQIIVMNEGKIAGMG 544
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAeilDLLRELQRERGTTVLLIthdlgvVAEI------ADRVVVMDDGRIVEDG 225
|
....*
gi 1251574723 545 THEEL 549
Cdd:COG1123 226 PPEEI 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
284-562 |
2.95e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 129.71 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 284 MLSAVFIMIPRAGASAERINEVLDMNAEILNPENPKTSTPPAkLSFEHVTFRYEG-AEKPVIEDITFEANAGETIAIIGS 362
Cdd:PLN03232 573 MLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGAPA-ISIKNGYFSWDSkTSKPTLSDINLEIPVGSLVAIVGG 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 363 TGAGKSTLIN-MIPRFYDVESGVVKINGidvremdqsslrqKIGLVPQKAVLFTGTIASNMRYGkEDATDEEIWEALRTA 441
Cdd:PLN03232 652 TGEGKTSLISaMLGELSHAETSSVVIRG-------------SVAYVPQVSWIFNATVRENILFG-SDFESERYWRAIDVT 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 442 QAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKT-----DAKLREALKAETteavT 516
Cdd:PLN03232 718 ALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVahqvfDSCMKDELKGKT----R 793
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1251574723 517 LIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQEIMRS 562
Cdd:PLN03232 794 VLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMEN 839
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
327-542 |
4.69e-31 |
|
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: 120.27 E-value: 4.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYE--GAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREmdqssLRQKI 404
Cdd:cd03293 1 LEVRNVSKTYGggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 405 GLVPQKAVLFT-GTIASNMRYGKEDAtdeEIWEALRTAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKP 483
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQ---GVPKAEARERAEELLELV--GLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251574723 484 EIYIFDDSFSALDFKTDAKLREAL-----KAETT---------EAVTLivaqritsvvnSDQIIVMNE--GKIAG 542
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELldiwrETGKTvllvthdidEAVFL-----------ADRVVVLSArpGRIVA 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
321-535 |
5.26e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 121.35 E-value: 5.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 321 STPPAKLSFEHVTFRY--EGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREmdqs 398
Cdd:COG1116 2 SAAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 399 sLRQKIGLVPQKAVLF---TgtIASNMRYGKEDATdeeIWEALRTAQAENFVSKLanGLGSRveqgGNNF----SGGQKQ 471
Cdd:COG1116 78 -PGPDRGVVFQEPALLpwlT--VLDNVALGLELRG---VPKAERRERARELLELV--GLAGF----EDAYphqlSGGMRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 472 RLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREAL-----KAETT---------EAVTLivaqritsvvnSDQIIVM 535
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELlrlwqETGKTvlfvthdvdEAVFL-----------ADRVVVL 212
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
11-302 |
1.07e-30 |
|
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: 121.46 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVT----GDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRD 86
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQlgpgGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 87 KIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLV 166
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 167 VILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLT 246
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 247 SIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
190-536 |
1.48e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 127.45 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 190 VIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIGSIFI--------GNG 261
Cdd:PTZ00265 238 IIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIisdlsnqqPNN 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 262 DMQVGDLMAFIqyaMQIMMSFMMLSAVFIMIPRAGASAERIN---EVLDMNAEILNPENPKTSTPPAKLSFEHVTFRYEG 338
Cdd:PTZ00265 318 DFHGGSVISIL---LGVLISMFMLTIILPNITEYMKSLEATNslyEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDT 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 339 AEK-PVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKIN-GIDVREMDQSSLRQKIGLVPQKAVLFTG 416
Cdd:PTZ00265 395 RKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSN 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 417 TIASNMRYG--------------KEDAT-------------------------------------------DEEIWEALR 439
Cdd:PTZ00265 475 SIKNNIKYSlyslkdlealsnyyNEDGNdsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikDSEVVDVSK 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 440 TAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTD---AKLREALKAETTEaVT 516
Cdd:PTZ00265 555 KVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLKGNENR-IT 633
|
410 420
....*....|....*....|
gi 1251574723 517 LIVAQRITSVVNSDQIIVMN 536
Cdd:PTZ00265 634 IIIAHRLSTIRYANTIFVLS 653
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
327-549 |
2.25e-30 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 119.84 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVreMDQSSL---RQK 403
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLweiRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLV---P--QkavlFTGTIAsnmrygkEDatD------------EEIWEalRTAQAENFVsklanGLGSRVEQGGNNFS 466
Cdd:TIGR04520 79 VGMVfqnPdnQ----FVGATV-------ED--DvafglenlgvprEEMRK--RVDEALKLV-----GMEDFRDREPHLLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 467 GGQKQRLSIARSLIRKPEIYIFDDSFSALD-------FKTDAKLREalkaetTEAVTLI-VAQRITSVVNSDQIIVMNEG 538
Cdd:TIGR04520 139 GGQKQRVAIAGVLAMRPDIIILDEATSMLDpkgrkevLETIRKLNK------EEGITVIsITHDMEEAVLADRVIVMNKG 212
|
250
....*....|.
gi 1251574723 539 KIAGMGTHEEL 549
Cdd:TIGR04520 213 KIVAEGTPREI 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
331-552 |
2.33e-30 |
|
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: 119.14 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 331 HVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQ- 409
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 410 -KAVL---FT--GTIASNMRYGKEDATDEEIWEALRTAqaenfvsklanGLGSRV-----EQggnnFSGGQKQRLSIARS 478
Cdd:COG1124 88 pYASLhprHTvdRILAEPLRIHGLPDREERIAELLEQV-----------GLPPSFldrypHQ----LSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 479 LIRKPEIYIFDDSFSALDFKTDAK---LREALKAETTEAVTLI-----VAQRItsvvnSDQIIVMNEGKIAGMGTHEELK 550
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEilnLLKDLREERGLTYLFVshdlaVVAHL-----CDRVAVMQNGRIVEELTVADLL 227
|
..
gi 1251574723 551 ES 552
Cdd:COG1124 228 AG 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
327-540 |
2.45e-30 |
|
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: 118.38 E-value: 2.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEH--VTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMD---QSSLR 401
Cdd:cd03257 2 LEVKNlsVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 402 QKIGLVPQKAvlftgtIAS---NMRYGkedatdEEIWEALR-------TAQAENFVSKLANGLG---SRVEQGGNNFSGG 468
Cdd:cd03257 82 KEIQMVFQDP------MSSlnpRMTIG------EQIAEPLRihgklskKEARKEAVLLLLVGVGlpeEVLNRYPHELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 469 QKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTE---AVTLI-----VAQRItsvvnSDQIIVMNEGKI 540
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElglTLLFIthdlgVVAKI-----ADRVAVMYAGKI 224
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
7-302 |
5.24e-30 |
|
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: 119.44 E-value: 5.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 7 YWLSITAVLVLTfgqvIGQLYLPTLMSNIIDK-GVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELR 85
Cdd:cd18541 1 YLLGILFLILVD----LLQLLIPRIIGRAIDAlTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 86 DKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLL 165
Cdd:cd18541 77 NDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 166 VVILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNL 245
Cdd:cd18541 157 VYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 246 TSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18541 237 SFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
11-302 |
1.39e-29 |
|
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: 118.26 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDY--IWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKI 88
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLqgLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 89 FTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMrLMVMAPIMLLGGIIMAVGR-DAKLSLIFVVvlplllllvv 167
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGL-VTLIGDLLLLIGILIAMFLlNWRLALISLL---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 168 ilggkAMPMF----KSLQKKMDKLNRVIR-----------EGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLL 232
Cdd:cd18544 150 -----VLPLLllatYLFRKKSRKAYREVReklsrlnaflqESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLF 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 233 SLMSPLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18544 225 ALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
328-541 |
3.02e-29 |
|
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: 114.94 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 328 SFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMdqsslRQKIGLV 407
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 408 PQKAVL---------------FTGTIASNMRYGKEDAtdEEIWEALRTAQAENFVSKLangLGSrveqggnnFSGGQKQR 472
Cdd:cd03235 74 PQRRSIdrdfpisvrdvvlmgLYGHKGLFRRLSKADK--AKVDEALERVGLSELADRQ---IGE--------LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251574723 473 LSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVT-LIVAQRITSVVNS-DQIIVMNEGKIA 541
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTiLVVTHDLGLVLEYfDRVLLLNRTVVA 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
328-559 |
3.25e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.63 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 328 SFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLV 407
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 408 PQKA-VLFTG-TIASNMRYGKEDA--TDEEIWEALrtaqaeNFVSKLAnGLGSRVEQGGNNFSGGQKQRLSIARSLIRKP 483
Cdd:PRK13632 89 FQNPdNQFIGaTVEDDIAFGLENKkvPPKKMKDII------DDLAKKV-GMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 484 EIYIFDDSFSALDFKTDAKLRE---ALKAETTEavTLIvaqRIT----SVVNSDQIIVMNEGKIAGMGTHEELKESNQIY 556
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKimvDLRKTRKK--TLI---SIThdmdEAILADKVIVFSEGKLIAQGKPKEILNNKEIL 236
|
...
gi 1251574723 557 QEI 559
Cdd:PRK13632 237 EKA 239
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
327-558 |
3.61e-29 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 115.92 E-value: 3.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQ---K 403
Cdd:COG3638 3 LELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQ-----------KAVL-----FTGTIAS-NMRYGKEDAtdEEIWEALRTaqaenfVsklanGLGSRVEQGGNNFS 466
Cdd:COG3638 82 IGMIFQqfnlvprlsvlTNVLagrlgRTSTWRSlLGLFPPEDR--ERALEALER------V-----GLADKAYQRADQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 467 GGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEavtlivaQRITSVVN----------SDQIIVMN 536
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARE-------DGITVVVNlhqvdlarryADRIIGLR 221
|
250 260
....*....|....*....|....
gi 1251574723 537 EGKIAGMGTHEELKES--NQIYQE 558
Cdd:COG3638 222 DGRVVFDGPPAELTDAvlREIYGG 245
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
11-302 |
4.02e-29 |
|
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: 116.81 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIFT 90
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 91 KVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVgRDAKLSLIFVVVLPLLLLLVVILG 170
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVVMLV-LSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 171 GKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAI 250
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 251 VWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18543 240 LALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
327-552 |
5.46e-29 |
|
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: 114.91 E-value: 5.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQS---SLRQK 403
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQKAVLFTG-TIASNMRYG---KEDATDEEIWEalRTAQAENFVsklanGLGSRVEQGGNNFSGGQKQRLSIARSL 479
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIRE--IVLEKLEAV-----GLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 480 IRKPEIYIFDDSFSALDFKTDAKLREALK--AETTEAVTLIVAQRITSVVN-SDQIIVMNEGKIAGMGTHEELKES 552
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
317-540 |
1.15e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 114.75 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 317 NPKTSTPPAKLSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGV-----VKINGID 391
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 392 V--REMDQSSLRQKIGLVPQKAVLFTGTIASNMRYG--------KEDAtDEEIWEALRTAQaenfvskLANGLGSRVEQG 461
Cdd:COG1117 80 IydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksKSEL-DEIVEESLRKAA-------LWDEVKDRLKKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 462 GNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLRE---ALKAETTeavTLIV------AQRItsvvnSDQI 532
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEElilELKKDYT---IVIVthnmqqAARV-----SDYT 223
|
....*...
gi 1251574723 533 IVMNEGKI 540
Cdd:COG1117 224 AFFYLGEL 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
284-569 |
2.16e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 121.00 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 284 MLSAVFIMIPRAGASAERINEVLDMNAEILNPENPKTSTPPAkLSFEHVTFRYEG-AEKPVIEDITFEANAGETIAIIGS 362
Cdd:PLN03130 573 MLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGLPA-ISIKNGYFSWDSkAERPTLSNINLDVPVGSLVAIVGS 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 363 TGAGKSTLIN-MIPRFYDVESGVVKINGidvremdqsslrqKIGLVPQKAVLFTGTIASNMRYGKE-DAtdEEIWEALRT 440
Cdd:PLN03130 652 TGEGKTSLISaMLGELPPRSDASVVIRG-------------TVAYVPQVSWIFNATVRDNILFGSPfDP--ERYERAIDV 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 441 AQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKT-----DAKLREALKAETTEAV 515
Cdd:PLN03130 717 TALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgrqvfDKCIKDELRGKTRVLV 796
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 516 TlivaQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQEIMRSQLSEEEI 569
Cdd:PLN03130 797 T----NQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEY 846
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
248-560 |
4.23e-28 |
|
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: 120.02 E-value: 4.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 248 IAIVWIGSIFIGNGDMQVGDLMAFiqyAMQIMMSFMMLSAVFIMIPRAGASAERINEVLDMNAEILNPENPKTSTPPAK- 326
Cdd:TIGR01271 1124 IAVTFIAIGTNQDGEGEVGIILTL---AMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKYQLSTv 1200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 -----------------LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVEsGVVKING 389
Cdd:TIGR01271 1201 lvienphaqkcwpsggqMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG 1279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 390 IDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMRyGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQ 469
Cdd:TIGR01271 1280 VSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGH 1358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 470 KQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEEL 549
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKL 1438
|
330
....*....|.
gi 1251574723 550 KESNQIYQEIM 560
Cdd:TIGR01271 1439 LNETSLFKQAM 1449
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
327-551 |
4.28e-28 |
|
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: 112.33 E-value: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSslRQKIGL 406
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTG-TIASNMRYG------KEDATDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSL 479
Cdd:cd03300 77 VFQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 480 IRKPEIYIFDDSFSALDFKTDAKLREALKA-----ETT---------EAVTLivaqritsvvnSDQIIVMNEGKIAGMGT 545
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRlqkelGITfvfvthdqeEALTM-----------SDRIAVMNKGKIQQIGT 214
|
....*.
gi 1251574723 546 HEELKE 551
Cdd:cd03300 215 PEEIYE 220
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
8-302 |
6.46e-28 |
|
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: 113.40 E-value: 6.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 8 WLSITAVLVLTfgqvIGQLYLPTLMSNIIDK-GVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRD 86
Cdd:cd18778 2 ILTLLCALLST----LLGLVPPWLIRELVDLvTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 87 KIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLV 166
Cdd:cd18778 78 DLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 167 VILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLT 246
Cdd:cd18778 158 WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLG 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 247 SIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18778 238 TVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
327-539 |
6.49e-28 |
|
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: 109.97 E-value: 6.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSS--LRQKI 404
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 405 GLVPQKAVLFTG-TIASNMRYGkedatdeeiwealrtaqaenfvsklanglgsrveqggnnFSGGQKQRLSIARSLIRKP 483
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 484 EIYIFDDSFSALDFKTDAKLREALKA-ETTEAVTLIV-------AQRItsvvnSDQIIVMNEGK 539
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSlQAQLGITVVLvthdldeAARL-----ADRVVVLRDGK 178
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
11-302 |
1.40e-27 |
|
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: 112.56 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIFT 90
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 91 KVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVILG 170
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 171 GKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAI 250
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 251 VWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18545 242 YWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
327-556 |
4.82e-27 |
|
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: 109.58 E-value: 4.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQ---K 403
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQ-----------KAVLfTGTIA--SNMRYGKEDATDEEIWEALrtaQAENFVsklanGLGSRVEQGGNNFSGGQK 470
Cdd:cd03256 80 IGMIFQqfnlierlsvlENVL-SGRLGrrSTWRSLFGLFPKEEKQRAL---AALERV-----GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 471 QRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTE-AVTLIV-------AQRITsvvnsDQIIVMNEGKIAG 542
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVslhqvdlAREYA-----DRIVGLKDGRIVF 225
|
250
....*....|....*.
gi 1251574723 543 MGTHEELKES--NQIY 556
Cdd:cd03256 226 DGPPAELTDEvlDEIY 241
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
346-549 |
5.07e-27 |
|
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: 110.43 E-value: 5.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 346 DITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQ----KIGLVPQKAVLFTG-TIAS 420
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 421 NMRYGKEDA-TDEEIWEAlRTAQAENFVsklanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKT 499
Cdd:cd03294 122 NVAFGLEVQgVPRAEREE-RAAEALELV-----GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 500 DAKLRE---ALKAE---TTEAVT--LIVAQRItsvvnSDQIIVMNEGKIAGMGTHEEL 549
Cdd:cd03294 196 RREMQDellRLQAElqkTIVFIThdLDEALRL-----GDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
327-540 |
7.13e-27 |
|
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: 108.35 E-value: 7.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYE--GAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSL---- 400
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 401 RQKIGLVPQK-AVLFTGTIASN----MRYGKEDATDeeiwealRTAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSI 475
Cdd:cd03255 81 RRHIGFVFQSfNLLPDLTALENvelpLLLAGVPKKE-------RRERAEELLERV--GLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 476 ARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEA-VTLIVAQRITSVVN-SDQIIVMNEGKI 540
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHDPELAEyADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
327-542 |
7.96e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 108.59 E-value: 7.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYE--GAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMI-----PrfydvESGVVKINGIDVREMDQSS 399
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrP-----TSGEVLIDGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 400 L----RQKIGLVPQKAVLFTG-TIASN----MRYGKEDATDeeiwealRTAQAENFVSKLanGLGSRVEQGGNNFSGGQK 470
Cdd:COG1136 80 LarlrRRHIGFVFQFFNLLPElTALENvalpLLLAGVSRKE-------RRERARELLERV--GLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 471 QRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEA-VTLIVA---QRITSVvnSDQIIVMNEGKIAG 542
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVthdPELAAR--ADRVIRLRDGRIVS 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
329-549 |
1.27e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 108.26 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 329 FEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVR--EMDQSSLRQKIGL 406
Cdd:PRK09493 4 FKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTGTIA-SNMRYG--------KEDATDeeiwealrtaQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIAR 477
Cdd:PRK09493 82 VFQQFYLFPHLTAlENVMFGplrvrgasKEEAEK----------QARELLAKV--GLAERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 478 SLIRKPEIYIFDDSFSALdfktDAKLR-EALK-----AEttEAVTLIV-------AQRITSvvnsdQIIVMNEGKIAGMG 544
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSAL----DPELRhEVLKvmqdlAE--EGMTMVIvtheigfAEKVAS-----RLIFIDKGRIAEDG 218
|
....*
gi 1251574723 545 THEEL 549
Cdd:PRK09493 219 DPQVL 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
327-549 |
1.37e-26 |
|
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: 108.05 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVT--FRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSL---R 401
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 402 QKIGLVPQKAVLFTG-TIASNMRY-----GKEDATDEEiwealRTAQAENFVsklanGLGSRVEQGGNNFSGGQKQRLSI 475
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALpleiaGVPKAEIEE-----RVLELLELV-----GLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 476 ARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTE-AVTLIVaqrIT---SVVNS--DQIIVMNEGKIAGMGTHEEL 549
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVL---IThemEVVKRicDRVAVMEKGEVVEEGTVEEV 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
322-553 |
2.50e-26 |
|
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: 107.37 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 322 TPPAKLSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQS--- 398
Cdd:COG1127 1 MSEPMIEVRNLTKSFGD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKely 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 399 SLRQKIGLVPQKAVLFTG-TIASNMRYG-------KEDATDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQK 470
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSlTVFENVAFPlrehtdlSEAEIRELVLEKLELVGLPGAADKMPSEL-----------SGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 471 QRLSIARSLIRKPEIYIFDDSFSALDFKTDA-------KLREALKaeTTeavTLIVAQRITSVVN-SDQIIVMNEGKIAG 542
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPITSAvidelirELRDELG--LT---SVVVTHDLDSAFAiADRVAVLADGKIIA 222
|
250
....*....|.
gi 1251574723 543 MGTHEELKESN 553
Cdd:COG1127 223 EGTPEELLASD 233
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
326-540 |
4.24e-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: 108.02 E-value: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVEsGVVKINGIDVREMDQSSLRQKIG 405
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKAVLFTGTIASNMR-YGKEdaTDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPE 484
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 485 IYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKI 540
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
330-540 |
4.99e-26 |
|
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: 105.80 E-value: 4.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 330 EHVTFRYEGAEKpVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDqssLRQKIGLVPQ 409
Cdd:cd03226 3 ENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 410 KA--VLFTGTIASNMRYGKEDATDEEiwealrtAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYI 487
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGN-------EQAETVLKDL--DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 488 FDDSFSALDFKTDAKLREALKAETTEAVTLIV-------AQRItsvvnSDQIIVMNEGKI 540
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVithdyefLAKV-----CDRVLLLANGAI 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
327-550 |
5.07e-26 |
|
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: 106.05 E-value: 5.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREmDQSSLRQKIGL 406
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTG-TIASNMRY-----GKEDAT-DEEIWEALRTAQAENFVSKLAnglgsrveqggNNFSGGQKQRLSIARSL 479
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkGLPKSEiKEEVELLLRVLGLTDKANKRA-----------RTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 480 IRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVN-SDQIIVMNEGKIAGMGTHEELK 550
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
327-544 |
5.63e-26 |
|
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: 105.80 E-value: 5.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEgaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSslRQKIGL 406
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTG-TIASNMRYG------KEDATDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSL 479
Cdd:cd03301 77 VFQNYALYPHmTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRVALGRAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 480 IRKPEIYIFDDSFSALdfktDAKLREALKAE----------TT--------EAVTLivaqritsvvnSDQIIVMNEGKIA 541
Cdd:cd03301 146 VREPKVFLMDEPLSNL----DAKLRVQMRAElkrlqqrlgtTTiyvthdqvEAMTM-----------ADRIAVMNDGQIQ 210
|
...
gi 1251574723 542 GMG 544
Cdd:cd03301 211 QIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
343-548 |
1.29e-25 |
|
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: 105.50 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 343 VIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMdqSSLRQKIGLVPQKAVLFTG-TIASN 421
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL--PPEKRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 422 MRYG--KEDATDEEIWEALRTAQAENFVSKLANGLGSRVeqggnnfSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKT 499
Cdd:cd03299 92 IAYGlkKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETL-------SGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 500 DAKLREALK-AETTEAVTLI-VAQRITSV-VNSDQIIVMNEGKIAGMGTHEE 548
Cdd:cd03299 165 KEKLREELKkIRKEFGVTVLhVTHDFEEAwALADKVAIMLNGKLIQVGKPEE 216
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
313-558 |
1.58e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 108.50 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 313 LNPENPKTSTPPAKLSfeHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDV 392
Cdd:PRK09452 3 KLNKQPSSLSPLVELR--GISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 393 RemDQSSLRQKIGLVPQKAVLFTG-TIASNMRYG------KEDATDEEIWEALRTAQAENFVSKlanglgsRVEQggnnF 465
Cdd:PRK09452 79 T--HVPAENRHVNTVFQSYALFPHmTVFENVAFGlrmqktPAAEITPRVMEALRMVQLEEFAQR-------KPHQ----L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 466 SGGQKQRLSIARSLIRKPEIYIFDDSFSALDFktdaKLREALKAEtteavtLIVAQR---ITSV----------VNSDQI 532
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALDY----KLRKQMQNE------LKALQRklgITFVfvthdqeealTMSDRI 215
|
250 260
....*....|....*....|....*.
gi 1251574723 533 IVMNEGKIAGMGTHEElkesnqIYQE 558
Cdd:PRK09452 216 VVMRDGRIEQDGTPRE------IYEE 235
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
26-301 |
1.82e-25 |
|
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: 106.38 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 26 LYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVY----LASRISmgfgKELRDKIFTKVEDFSLQEFD 101
Cdd:cd18549 19 LVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYwghvMGARIE----TDMRRDLFEHLQKLSFSFFD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 102 KVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVILGGKAMPMFKSLQ 181
Cdd:cd18549 95 NNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 182 KKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIGSIFIGNG 261
Cdd:cd18549 175 EKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKG 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1251574723 262 DMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAER 301
Cdd:cd18549 255 EITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
11-302 |
2.19e-25 |
|
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: 105.98 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYLPTLMSNIIDKGvvtGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIFT 90
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDAL---SAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 91 KVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVILG 170
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 171 GKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAI 250
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 251 VWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18551 238 LGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
9-302 |
3.58e-25 |
|
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: 105.64 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 9 LSITAVLVLTFGQVIGQLylptlmsniIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKI 88
Cdd:cd18576 5 LLLSSAIGLVFPLLAGQL---------IDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 89 FTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVI 168
Cdd:cd18576 76 YRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 169 LGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSI 248
Cdd:cd18576 156 FGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 249 AIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18576 236 AVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
324-544 |
7.01e-25 |
|
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: 101.86 E-value: 7.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 324 PAKLSFEHVTF----RYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIP--RFYDVESGVVKINGIDVremDQ 397
Cdd:cd03213 1 GVTLSFRNLTVtvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 398 SSLRQKIGLVPQKAVLFtgtiasnmrygkEDATdeeIWEALRtaqaenFVSKLaNGLgsrveqggnnfSGGQKQRLSIAR 477
Cdd:cd03213 78 RSFRKIIGYVPQDDILH------------PTLT---VRETLM------FAAKL-RGL-----------SGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 478 SLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVA--QRITSVVNS-DQIIVMNEGKIAGMG 544
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSihQPSSEIFELfDKLLLLSQGRVIYFG 194
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
327-541 |
7.60e-25 |
|
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: 102.66 E-value: 7.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGeTIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSsLRQKIGL 406
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQ--------KAVLFTGTIA--SNMRYGKEDATDEEIWEALrtaqaenfvsklanGLGSRVEQGGNNFSGGQKQRLSIA 476
Cdd:cd03264 77 LPQefgvypnfTVREFLDYIAwlKGIPSKEVKARVDEVLELV--------------NLGDRAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 477 RSLIRKPEIYIFDDSFSALDFKTDAKLREALkAETTEAVTLIVAQRITSVVNS--DQIIVMNEGKIA 541
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLL-SELGEDRIVILSTHIVEDVESlcNQVAVLNKGKLV 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
330-550 |
1.12e-24 |
|
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: 102.45 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 330 EHVTFRYEGAEkpVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREmDQSSLRQKIGLVPQ 409
Cdd:cd03265 4 ENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 410 KAVL---FTGTiaSNMR-----YG-KEDATDEEIWEALRTAQAENFVSKLAnglgsrveqggNNFSGGQKQRLSIARSLI 480
Cdd:cd03265 81 DLSVddeLTGW--ENLYiharlYGvPGAERRERIDELLDFVGLLEAADRLV-----------KTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 481 RKPEIYIFDDSFSALDFKTDAKLREALKA-ETTEAVTLIV-------AQRItsvvnSDQIIVMNEGKIAGMGTHEELK 550
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKlKEEFGMTILLtthymeeAEQL-----CDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
11-302 |
1.89e-24 |
|
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: 103.34 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIFT 90
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 91 KVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVILG 170
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 171 GKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAI 250
Cdd:cd18546 161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 251 VWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18546 241 LLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
327-549 |
2.05e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 101.76 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKpvieDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMD---------- 396
Cdd:COG3840 2 LRLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpaerpvsmlf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 397 QS-------SLRQKIGLvpqkavlftGtIASNMRYGKEDAtdEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQ 469
Cdd:COG3840 78 QEnnlfphlTVAQNIGL---------G-LRPGLKLTAEQR--AQVEQALERVGLAGLLDRLPGQL-----------SGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 470 KQRLSIARSLIRKPEIYIFDDSFSALDFktdaklreALKAE----------TTEAVTLIV------AQRITsvvnsDQII 533
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDP--------ALRQEmldlvdelcrERGLTVLMVthdpedAARIA-----DRVL 201
|
250
....*....|....*.
gi 1251574723 534 VMNEGKIAGMGTHEEL 549
Cdd:COG3840 202 LVADGRIAADGPTAAL 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
327-540 |
2.39e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 101.28 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSS---LRQK 403
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQKAVLFTG-TIASN----MRY-GKEDAT-DEEIWEALR----TAQAENFVSKLanglgsrveqggnnfSGGQKQR 472
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENvalpLRVtGKSRKEiRRRVREVLDlvglSDKAKALPHEL---------------SGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 473 LSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNS--DQIIVMNEGKI 540
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRmpKRVLELEDGRL 215
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
270-568 |
2.54e-24 |
|
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: 108.11 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 270 AFIQYAMQIMMSF--MMLSAVFIMIPRAGASAERINEVLdmNAEILNPEN----PKTSTPPAKLSFEHVTFRYEGAEKPV 343
Cdd:TIGR00957 576 AFVSLALFNILRFplNILPMVISSIVQASVSLKRLRIFL--SHEELEPDSierrTIKPGEGNSITVHNATFTWARDLPPT 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 344 IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvremdqsslrqKIGLVPQKAVLFTGTIASNMR 423
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENIL 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 424 YGKedATDEEIWEALRTAQAE-NFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAK 502
Cdd:TIGR00957 721 FGK--ALNEKYYQQVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1251574723 503 LRE-------ALKAETteavTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQEIMRSQLSEEE 568
Cdd:TIGR00957 799 IFEhvigpegVLKNKT----RILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQ 867
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
330-548 |
3.56e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.43 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 330 EHVTFRY-EGA--EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDV--REMDQSSLRQKI 404
Cdd:PRK13637 6 ENLTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 405 GLVPQ--KAVLFTGTIASNMRYGKED--ATDEEIWEalRTAQAENFVsklanGLGSRVEQGGNNF--SGGQKQRLSIARS 478
Cdd:PRK13637 86 GLVFQypEYQLFEETIEKDIAFGPINlgLSEEEIEN--RVKRAMNIV-----GLDYEDYKDKSPFelSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1251574723 479 LIRKPEIYIFDDSFSALDFKTDAKLREALKA--ETTEAVTLIVAQRITSVVN-SDQIIVMNEGKIAGMGTHEE 548
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
261-522 |
7.27e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 105.66 E-value: 7.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 261 GDMQVGDLMafiqyamQIMMSFMMLS---AVFIM----IPRAGASAERI---NEVLDMNAEILNPENPKTSTPPAKLSFE 330
Cdd:COG4178 294 GEITLGGLM-------QAASAFGQVQgalSWFVDnyqsLAEWRATVDRLagfEEALEAADALPEAASRIETSEDGALALE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 331 HVT-FRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVkingidVREMDQSSLrqkigLVPQ 409
Cdd:COG4178 367 DLTlRTPDG--RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI------ARPAGARVL-----FLPQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 410 KAVLFTGTIASNMRY--GKEDATDEEIWEALRTAQAENFVSKLanglgSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYI 487
Cdd:COG4178 434 RPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLF 508
|
250 260 270
....*....|....*....|....*....|....*.
gi 1251574723 488 FDDSFSALDFKTDAKLREALKAETTEAvTLI-VAQR 522
Cdd:COG4178 509 LDEATSALDEENEAALYQLLREELPGT-TVIsVGHR 543
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
327-549 |
8.83e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 102.92 E-value: 8.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMI-----PrfydvESGVVKINGIDVrEMDQSSLR 401
Cdd:COG1118 3 IEVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagletP-----DSGRIVLNGRDL-FTNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 402 QKIGLVPQKAVLF-TGTIASNMRYG------KEDATDEEIWEALRTAQAEnfvsklanGLGSR-VEQggnnFSGGQKQRL 473
Cdd:COG1118 75 RRVGFVFQHYALFpHMTVAENIAFGlrvrppSKAEIRARVEELLELVQLE--------GLADRyPSQ----LSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 474 SIARSLIRKPEIYIFDDSFSALdfktDAKLREALKA------ETTEAVTLIV------AQRItsvvnSDQIIVMNEGKIA 541
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGAL----DAKVRKELRRwlrrlhDELGGTTVFVthdqeeALEL-----ADRVVVMNQGRIE 213
|
....*...
gi 1251574723 542 GMGTHEEL 549
Cdd:COG1118 214 QVGTPDEV 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
327-549 |
2.42e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 101.31 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKPVI--EDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSL---R 401
Cdd:COG1135 2 IELENLSKTFPTKGGPVTalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 402 QKIGLVPQKAVLFTG-TIASN----MRYGKEDAtdEEIWEalRTAQAENFVsklanGLGSRVEQGGNNFSGGQKQRLSIA 476
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENvalpLEIAGVPK--AEIRK--RVAELLELV-----GLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 477 RSLIRKPEIYIFDDSFSALDfktdaklrealkAETTEAV-------------TLIVaqrIT---SVVNS--DQIIVMNEG 538
Cdd:COG1135 153 RALANNPKVLLCDEATSALD------------PETTRSIldllkdinrelglTIVL---IThemDVVRRicDRVAVLENG 217
|
250
....*....|.
gi 1251574723 539 KIAGMGTHEEL 549
Cdd:COG1135 218 RIVEQGPVLDV 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
327-549 |
2.88e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 98.53 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDV--REMDQSSLRQKI 404
Cdd:COG1126 2 IEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 405 GLVPQKAVLFTG-TIASNMRYG--------KEDATdeeiwealrtAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSI 475
Cdd:COG1126 80 GMVFQQFNLFPHlTVLENVTLApikvkkmsKAEAE----------ERAMELLERV--GLADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 476 ARSLIRKPEIYIFDDSFSALD-------FKTDAKLREalkaettEAVTLIV-------AQRItsvvnSDQIIVMNEGKIA 541
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDpelvgevLDVMRDLAK-------EGMTMVVvthemgfAREV-----ADRVVFMDGGRIV 215
|
....*...
gi 1251574723 542 GMGTHEEL 549
Cdd:COG1126 216 EEGPPEEF 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
329-552 |
3.12e-23 |
|
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: 98.57 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 329 FEHVTFRYEGAekPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDqssLRQK-IGLV 407
Cdd:cd03296 5 VRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERnVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 408 PQKAVLFTG-TIASNMRYG----------KEDATDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIA 476
Cdd:cd03296 80 FQHYALFRHmTVFDNVAFGlrvkprserpPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 477 RSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAvtlivaqRITSV-VNSDQ---------IIVMNEGKIAGMGTH 546
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDEL-------HVTTVfVTHDQeealevadrVVVMNKGRIEQVGTP 221
|
....*.
gi 1251574723 547 EELKES 552
Cdd:cd03296 222 DEVYDH 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
325-520 |
3.30e-23 |
|
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: 97.55 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 325 AKLSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREmDQSSLRQKI 404
Cdd:COG4133 1 MMLEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 405 GLVPQKAVLFTG-TIASNMRY----GKEDATDEEIWEALRTAqaenfvsklanGLGSRVEQGGNNFSGGQKQRLSIARSL 479
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1251574723 480 IRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVA 520
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
346-549 |
3.89e-23 |
|
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: 100.96 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 346 DITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQ----SSLRQKIGLVPQKAVLFTG-TIAS 420
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKgiflPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 421 NMRYGKEDATDEEiwealRTAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTD 500
Cdd:TIGR02142 95 NLRYGMKRARPSE-----RRISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1251574723 501 AKL---REALKAETTEAVtLIVAQRITSVVN-SDQIIVMNEGKIAGMGTHEEL 549
Cdd:TIGR02142 168 YEIlpyLERLHAEFGIPI-LYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
9-302 |
8.92e-23 |
|
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: 98.71 E-value: 8.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 9 LSITAVLVLTFGQVIGQLylptlmsniIDKGVVTGDTDYIwstGMKMLLISFASVILSVIV---VYLASRISMGFGKELR 85
Cdd:cd18575 5 LLIAAAATLALGQGLRLL---------IDQGFAAGNTALL---NRAFLLLLAVALVLALASalrFYLVSWLGERVVADLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 86 DKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLL 165
Cdd:cd18575 73 KAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 166 VVILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNL 245
Cdd:cd18575 153 IILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 246 TSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18575 233 AIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
35-302 |
1.22e-22 |
|
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: 98.32 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 35 IIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIFTKVEDFSLQEFDKVGTSSLITRTTN 114
Cdd:cd18540 28 AIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 115 DVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVvlplllllvvilggkAMP------MFksLQKKMDKLN 188
Cdd:cd18540 108 DTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLA---------------VVPvlavvsIY--FQKKILKAY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 189 RVIR-----------EGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIGSIF 257
Cdd:cd18540 171 RKVRkinsritgafnEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGIL 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1251574723 258 IGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18540 251 VLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
327-559 |
1.34e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.95 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKST---LINMIPRFYDVESGVVKINGIDVREMDQSSLRQK 403
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQKA-VLFTG-TIASNMRYGKEDatdeeiwEALRTAQAENFVSKLAN--GLGSRVEQGGNNFSGGQKQRLSIARSL 479
Cdd:PRK13640 86 VGIVFQNPdNQFVGaTVGDDVAFGLEN-------RAVPRPEMIKIVRDVLAdvGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 480 IRKPEIYIFDDSFSALDFKTDAK-LREALKAETTEAVTLI-VAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQ 557
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQiLKLIRKLKKKNNLTVIsITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
..
gi 1251574723 558 EI 559
Cdd:PRK13640 239 EI 240
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
327-540 |
2.14e-22 |
|
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: 95.67 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDV--REMDQSSLRQKI 404
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 405 GLV-------PQKAVLFTGTIASNMRYGKEDATDEEIwealrtaqAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIAR 477
Cdd:cd03262 79 GMVfqqfnlfPHLTVLENITLAPIKVKGMSKAEAEER--------ALELLEKV--GLADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 478 SLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIV-------AQRItsvvnSDQIIVMNEGKI 540
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVvthemgfAREV-----ADRVIFMDDGRI 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
329-540 |
2.36e-22 |
|
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: 95.55 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 329 FEHVTFRYeGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSS---LRQKIG 405
Cdd:cd03292 3 FINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKA-VLFTGTIASNMRYGKE--DATDEEIWEalRTAQAENFVsklanGLGSRVEQGGNNFSGGQKQRLSIARSLIRK 482
Cdd:cd03292 82 VVFQDFrLLPDRNVYENVAFALEvtGVPPREIRK--RVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 483 PEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQ--IIVMNEGKI 540
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
317-550 |
2.74e-22 |
|
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: 97.23 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 317 NPKTSTPPAKLSFEHvtFRYEGAekPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvremd 396
Cdd:cd03291 30 DRKHSSDDNNLFFSN--LCLVGA--PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 397 qsslrqKIGLVPQKAVLFTGTIASNMRYGKedATDEEIWEA-LRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSI 475
Cdd:cd03291 99 ------RISFSSQFSWIMPGTIKENIIFGV--SYDEYRYKSvVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 476 ARSLIRKPEIYIFDDSFSALDFKTDAKLREA----LKAETTEavtLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELK 550
Cdd:cd03291 171 ARAVYKDADLYLLDSPFGYLDVFTEKEIFEScvckLMANKTR---ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 246
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
346-544 |
2.76e-22 |
|
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: 95.05 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 346 DITFEANaGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKING---IDVR-EMDQSSLRQKIGLVPQKAVLFTG-TIAS 420
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRkKINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 421 NMRYGKEDATDEEiwealRTAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTD 500
Cdd:cd03297 95 NLAFGLKRKRNRE-----DRISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 501 AKLREALK--AETTEAVTLIV------AQRITsvvnsDQIIVMNEGKIAGMG 544
Cdd:cd03297 168 LQLLPELKqiKKNLNIPVIFVthdlseAEYLA-----DRIVVMEDGRLQYIG 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
332-544 |
4.50e-22 |
|
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: 94.48 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 332 VTFRYEgaEKPVIEDITFEAnaGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSslRQKIGLVPQKA 411
Cdd:cd03298 6 IRFSYG--EQPMHFDLTFAQ--GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 412 VLFTG-TIASNMRYG-----KEDATDEE-IWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSLIRKPE 484
Cdd:cd03298 80 NLFAHlTVEQNVGLGlspglKLTAEDRQaIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251574723 485 IYIFDDSFSALDfktdaklrEALKAETTEAVTLIVAQRITSVVN-----------SDQIIVMNEGKIAGMG 544
Cdd:cd03298 149 VLLLDEPFAALD--------PALRAEMLDLVLDLHAETKMTVLMvthqpedakrlAQRVVFLDNGRIAAQG 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
343-564 |
6.03e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.46 E-value: 6.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 343 VIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMdqSSLRQKIGLVPQKAVLFTG-TIASN 421
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 422 MRYG----------KEDATDEEIWEALRTAQaenfVSKLANGLGSRVeqggnnfSGGQKQRLSIARSLIRKPEIYIFDDS 491
Cdd:PRK10851 95 IAFGltvlprrerpNAAAIKAKVTQLLEMVQ----LAHLADRYPAQL-------SGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 492 FSALDFKTDAKLREALKAETTEAvtlivaqRITSV-VNSDQ---------IIVMNEGKIAGMGTHEE------------- 548
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEEL-------KFTSVfVTHDQeeamevadrVVVMSQGNIEQAGTPDQvwrepatrfvlef 236
|
250
....*....|....*.
gi 1251574723 549 LKESNQIYQEIMRSQL 564
Cdd:PRK10851 237 MGEVNRLQGTIRGGQF 252
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
327-549 |
2.57e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.11 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAekPVieDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSslRQKIGL 406
Cdd:PRK10771 2 LKLTDITWLYHHL--PM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTG-TIASNMRYG-----KEDATDEEIWEAL-RTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSL 479
Cdd:PRK10771 76 LFQENNLFSHlTVAQNIGLGlnpglKLNAAQREKLHAIaRQMGIEDLLARLPGQL-----------SGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 480 IRKPEIYIFDDSFSALDfktdaklrEALKAETTEAVTLIVAQR-IT------SVVNSDQI----IVMNEGKIAGMGTHEE 548
Cdd:PRK10771 145 VREQPILLLDEPFSALD--------PALRQEMLTLVSQVCQERqLTllmvshSLEDAARIaprsLVVADGRIAWDGPTDE 216
|
.
gi 1251574723 549 L 549
Cdd:PRK10771 217 L 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
331-549 |
4.00e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 93.64 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 331 HVTFRY-EGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQ 409
Cdd:PRK13650 9 NLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 410 KA-VLFTG-TIASNMRYGKEDA--TDEEIWEalRTAQAENFVsklanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEI 485
Cdd:PRK13650 89 NPdNQFVGaTVEDDVAFGLENKgiPHEEMKE--RVNEALELV-----GMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 486 YIFDDSFSALDFKTDAKLREALKA--ETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGirDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
327-551 |
5.06e-21 |
|
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: 91.73 E-value: 5.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAekPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSS-LRQKIG 405
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKAVLFTG-TIASNMR---YGKEDATDEEIWEAL-----RtaqaenfvsklangLGSRVEQGGNNFSGGQKQRLSIA 476
Cdd:cd03224 79 YVPEGRRIFPElTVEENLLlgaYARRRAKRKARLERVyelfpR--------------LKERRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 477 RSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVT-LIVAQRITSVVN-SDQIIVMNEGKIAGMGTHEELKE 551
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTiLLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
327-559 |
5.55e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.89 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGL 406
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAV-LFTGTI-ASNMRYGKE------DATDEEIWEALRTAqaenfvsklanGLGSRVEQGGNNFSGGQKQRLSIARS 478
Cdd:PRK13648 88 VFQNPDnQFVGSIvKYDVAFGLEnhavpyDEMHRRVSEALKQV-----------DMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 479 LIRKPEIYIFDDSFSALDFKTDAKLREAL-KAETTEAVTLI-VAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIY 556
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVrKVKSEHNITIIsITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
...
gi 1251574723 557 QEI 559
Cdd:PRK13648 237 TRI 239
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
11-302 |
6.03e-21 |
|
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: 93.32 E-value: 6.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIFT 90
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 91 KVEDFSLQEFDKVGTSSLITRTTNDVVQIQNV------------------LYMMMRL--------MVMAPIMLLGGIIMA 144
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVvtgtltsvvsnvvtlvatLVAMLALdwrlallsLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 145 VGRdAKLSlifvvvlplllllvvilggkampmfKSLQKKMDKLNRVIREGLT--GIRVVRSFNRNEDELEKFEEANADYA 222
Cdd:cd18550 161 RRR-RKLT-------------------------REQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 223 TTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18550 215 DLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
330-544 |
7.86e-21 |
|
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: 91.28 E-value: 7.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 330 EHVTFRYEGAEKPV--IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREmDQSSLRQKIGLV 407
Cdd:cd03266 5 DALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 408 PQKAVLFTG-TIASNMRYGKEdatdeeiWEALRTAQAENFVSKLANGLGSR--VEQGGNNFSGGQKQRLSIARSLIRKPE 484
Cdd:cd03266 84 SDSTGLYDRlTARENLEYFAG-------LYGLKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 485 IYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNS--DQIIVMNEGKIAGMG 544
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlcDRVVVLHRGRVVYEG 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
327-549 |
7.94e-21 |
|
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: 92.07 E-value: 7.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRF-YDVESGVVKI-----NGIDVREmdqssL 400
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLfgerrGGEDVWE-----L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 401 RQKIGLV-PQ------------KAVL--FTGTIASNMRYGKEDAtdEEIWEALRTAQAENFVSKLANGLgsrveqggnnf 465
Cdd:COG1119 77 RKRIGLVsPAlqlrfprdetvlDVVLsgFFDSIGLYREPTDEQR--ERARELLELLGLAHLADRPFGTL----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 466 SGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALK--AETTEAVTLIVAQRITSVVNS-DQIIVMNEGKIAG 542
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDklAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVA 223
|
....*..
gi 1251574723 543 MGTHEEL 549
Cdd:COG1119 224 AGPKEEV 230
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
15-302 |
1.62e-20 |
|
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: 91.84 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 15 LVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILS----VIVVYLASRISMGfgkeLRDKIFT 90
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSglrgGCFSYAGTRLVRR----LRRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 91 KVedfSLQE---FDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVV 167
Cdd:cd18572 78 SL---LRQDiafFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 168 ILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTS 247
Cdd:cd18572 155 VYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQ 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1251574723 248 IAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18572 235 VLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
343-549 |
1.65e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 91.68 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 343 VIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVReMDQSSL---RQKIGLVPQKA--VLFTGT 417
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKTVGIVFQNPddQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 418 IASNMRYG------KEDATDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSLIRKPEIYIFDDS 491
Cdd:PRK13639 96 VEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 492 FSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVN--SDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPvyADKVYVMSDGKIIKEGTPKEV 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
342-550 |
7.34e-20 |
|
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: 94.21 E-value: 7.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 342 PVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvremdqsslrqKIGLVPQKAVLFTGTIASN 421
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 422 MRYGKedATDEEIWEALRTA-QAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTD 500
Cdd:TIGR01271 507 IIFGL--SYDEYRYTSVIKAcQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1251574723 501 AKLREALKAETTEAVT-LIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELK 550
Cdd:TIGR01271 585 KEIFESCLCKLMSNKTrILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQ 635
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
308-551 |
9.27e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.44 E-value: 9.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 308 MNAEILNPEN--PKTSTPpaKLSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVV 385
Cdd:PRK11607 1 MNDAIPRPQAktRKALTP--LLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 386 KINGIDVREMdqSSLRQKIGLVPQKAVLFTG-TIASNMRYG-KED--ATDE---EIWEALRTAQAENFVSKLANGLgsrv 458
Cdd:PRK11607 77 MLDGVDLSHV--PPYQRPINMMFQSYALFPHmTVEQNIAFGlKQDklPKAEiasRVNEMLGLVHMQEFAKRKPHQL---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 459 eqggnnfSGGQKQRLSIARSLIRKPEIYIFDDSFSALdfktDAKLREALKAETTEAVTLIVAQRItsVVNSDQ------- 531
Cdd:PRK11607 151 -------SGGQRQRVALARSLAKRPKLLLLDEPMGAL----DKKLRDRMQLEVVDILERVGVTCV--MVTHDQeeamtma 217
|
250 260
....*....|....*....|..
gi 1251574723 532 --IIVMNEGKIAGMGTHEELKE 551
Cdd:PRK11607 218 grIAIMNRGKFVQIGEPEEIYE 239
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
324-549 |
1.10e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 90.67 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 324 PAKLSFEHVTFRYEGaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSlrQK 403
Cdd:PRK11650 1 MAGLKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQKAVLFTG-TIASNMRYG------KEDATDEEIWEALRTAQAENFvsklangLGSRVEQggnnFSGGQKQRLSIA 476
Cdd:PRK11650 78 IAMVFQNYALYPHmSVRENMAYGlkirgmPKAEIEERVAEAARILELEPL-------LDRKPRE----LSGGQRQRVAMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 477 RSLIRKPEIYIFDDSFSALdfktDAKLREALKAE---------TT---------EAVTLivAQRitsvvnsdqIIVMNEG 538
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNL----DAKLRVQMRLEiqrlhrrlkTTslyvthdqvEAMTL--ADR---------VVVMNGG 211
|
250
....*....|.
gi 1251574723 539 KIAGMGTHEEL 549
Cdd:PRK11650 212 VAEQIGTPVEV 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
343-549 |
1.91e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.16 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 343 VIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREmdqSSLRQK-IGLVPQKAVLFTG-TIAS 420
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRdICMVFQSYALFPHmSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 421 NMRYG--KEDATDEEIWEalRTAQAENFVSkLAnGLGSR-VEQggnnFSGGQKQRLSIARSLIRKPEIYIFDDSFSALdf 497
Cdd:PRK11432 98 NVGYGlkMLGVPKEERKQ--RVKEALELVD-LA-GFEDRyVDQ----ISGGQQQRVALARALILKPKVLLFDEPLSNL-- 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 498 ktDAKLREALKAETTEavtliVAQR--ITSV----------VNSDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK11432 168 --DANLRRSMREKIRE-----LQQQfnITSLyvthdqseafAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
343-548 |
1.99e-19 |
|
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: 87.49 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 343 VIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSL-RQKIGLVPQKAVLFTG-TIAS 420
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 421 NMRYG----------------KEDATDEEIWEALRTAqaenfvsklanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPE 484
Cdd:cd03219 95 NVMVAaqartgsglllararrEEREARERAEELLERV-----------GLADLADRPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 485 IYIFDDSFsaldfktdAKLREALKAETTEAVTLIVAQRIT--------SVVN--SDQIIVMNEGKIAGMGTHEE 548
Cdd:cd03219 164 LLLLDEPA--------AGLNPEETEELAELIRELRERGITvllvehdmDVVMslADRVTVLDQGRVIAEGTPDE 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
331-549 |
2.46e-19 |
|
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: 88.96 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 331 HVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYD---VESGVVKINGIDVREMDQSSLRQ----K 403
Cdd:COG0444 8 KVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKirgrE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQKAvlftgtIAS-N--MRYGkedatdEEIWEALRT------AQAENFVSKLAN--GLGSRVEQGGN---NFSGGQ 469
Cdd:COG0444 88 IQMIFQDP------MTSlNpvMTVG------DQIAEPLRIhgglskAEARERAIELLErvGLPDPERRLDRyphELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 470 KQRLSIARSLIRKPEIYIFDDSFSALDFKTDAK----LREaLKAETTEAVTLI-----VAQRItsvvnSDQIIVMNEGKI 540
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQilnlLKD-LQRELGLAILFIthdlgVVAEI-----ADRVAVMYAGRI 229
|
....*....
gi 1251574723 541 AGMGTHEEL 549
Cdd:COG0444 230 VEEGPVEEL 238
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
327-540 |
5.40e-19 |
|
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: 85.80 E-value: 5.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvrEMDQSSLRQKIGL 406
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDIAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTG-TIASNMRY-------GKEDATdEEIWEALrtaqaENFvsKLANGLGSRVEQggnnFSGGQKQRLSIARS 478
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVYlaqlkglKKEEAR-RRIDEWL-----ERL--ELSEYANKRVEE----LSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 479 LIRKPEIYIFDDSFSALD------FKTdaKLREALKAETTeavTLIVAQRITSVVN-SDQIIVMNEGKI 540
Cdd:cd03269 143 VIHDPELLILDEPFSGLDpvnvelLKD--VIRELARAGKT---VILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
320-566 |
6.11e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 91.38 E-value: 6.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 320 TSTPPAKLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVkingidvremdqsS 399
Cdd:PTZ00243 652 TSERSAKTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------W 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 400 LRQKIGLVPQKAVLFTGTIASN-MRYGKEDATDeeIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARS 478
Cdd:PTZ00243 719 AERSIAYVPQQAWIMNATVRGNiLFFDEEDAAR--LADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARA 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 479 LIRKPEIYIFDDSFSALDFKTDAKLRE-----ALKAETTEAVTlivaQRITSVVNSDQIIVMNEGKIAGMGTHEELKESN 553
Cdd:PTZ00243 797 VYANRDVYLLDDPLSALDAHVGERVVEecflgALAGKTRVLAT----HQVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
250
....*....|...
gi 1251574723 554 qIYqEIMRSQLSE 566
Cdd:PTZ00243 873 -LY-ATLAAELKE 883
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
327-518 |
1.27e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.52 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVR--EMDQSSLRQKI 404
Cdd:PRK11248 2 LQISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpGAERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 405 GLVPQKAVLftgtiaSNMRYGKEDATdeeIWEALRTAQAENFVSKLA-NGLGSR-VEQggnnFSGGQKQRLSIARSLIRK 482
Cdd:PRK11248 80 GLLPWRNVQ------DNVAFGLQLAG---VEKMQRLEIAHQMLKKVGlEGAEKRyIWQ----LSGGQRQRVGIARALAAN 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 1251574723 483 PEIYIFDDSFSALDFKTDAKLREALK---AETTEAVTLI 518
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLklwQETGKQVLLI 185
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
342-547 |
3.10e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 84.29 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 342 PVIEDITFEANAGETIAIIGSTGAGKSTLINM-----IPRfydveSGVVKING------IDVREMDQSSLRQKIGLVPQK 410
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVlnlleTPD-----SGQLNIAGhqfdfsQKPSEKAIRLLRQKVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 411 AVLFTG-TIASNM--------RYGKEDATDEEIwEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSLIR 481
Cdd:COG4161 91 YNLWPHlTVMENLieapckvlGLSKEQAREKAM-KLLARLRLTDKADRFPLHL-----------SGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1251574723 482 KPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIV-------AQRITSvvnsdQIIVMNEGKIAGMGTHE 547
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIvthevefARKVAS-----QVVYMEKGRIIEQGDAS 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
325-540 |
3.32e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.24 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 325 AKLSFEHVTFRYEGAEKP--VIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSL-- 400
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 401 --RQKIGLVPQKAVLFTG-TIASNMRYGKEDATDEeiwEALRTAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIAR 477
Cdd:PRK10535 83 lrREHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLE---RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 478 SLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVN-SDQIIVMNEGKI 540
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAqAERVIEIRDGEI 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
343-549 |
3.50e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.42 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 343 VIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDV---REMDQS-----SLRQKIGLVPQKAVLF 414
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQkglirQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 415 TG-TIASNMRYGKEDATDEEIWEAlrTAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFS 493
Cdd:PRK11264 98 PHrTVLENIIEGPVIVKGEPKEEA--TARARELLAKV--GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 494 ALDFKTDAKLREALKAETTEAVTLIVAQRITSVVN--SDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdvADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
346-549 |
3.55e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 86.24 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 346 DITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSslRQKIGLVPQKAVLFTG-TIASNMRY 424
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMVFQSYALYPHlSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 425 GKEDATDEEIWEALRTAQAENFVSklangLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALdfktDAKLR 504
Cdd:PRK11000 99 GLKLAGAKKEEINQRVNQVAEVLQ-----LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL----DAALR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1251574723 505 EALKAETT------------------EAVTLivaqritsvvnSDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK11000 170 VQMRIEISrlhkrlgrtmiyvthdqvEAMTL-----------ADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
326-541 |
3.71e-18 |
|
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: 83.47 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSFEHVT--FRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIP---RFYDVESGVVKINGidvREMDQSSL 400
Cdd:cd03234 3 VLPWWDVGlkAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNG---QPRKPDQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 401 RQKIGLVPQKAVLFTG-TIASNMRYGKEDATDEEIWEALRTAQAENFVSK-LANG-LGSRVEQGgnnFSGGQKQRLSIAR 477
Cdd:cd03234 80 QKCVAYVRQDDILLPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRdLALTrIGGNLVKG---ISGGERRRVSIAV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 478 SLIRKPEIYIFDDSFSALDFKTDAKLREALK--AETTEAVTLIVAQRITSVVNS-DQIIVMNEGKIA 541
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSqlARRNRIVILTIHQPRSDLFRLfDRILLLSSGEIV 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
330-561 |
5.34e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.40 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 330 EHVTFRYEGAEKpVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQ 409
Cdd:PRK13647 8 EDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 410 KA--VLFTGTI-------ASNMRYGKEDaTDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSLI 480
Cdd:PRK13647 87 DPddQVFSSTVwddvafgPVNMGLDKDE-VERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 481 RKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNS--DQIIVMNEGKIAGMGTHEELKESNQIYQE 558
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwaDQVIVLKEGRVLAEGDKSLLTDEDIVEQA 234
|
...
gi 1251574723 559 IMR 561
Cdd:PRK13647 235 GLR 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
344-549 |
8.11e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.76 E-value: 8.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 344 IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQK---IGLVPQK--AVL----- 413
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDplASLnprmt 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 414 FTGTIASNMRYGKEDATDEEIWEALRTAQAEnfVSKLANgLGSRVEqggNNFSGGQKQRLSIARSLIRKPEIYIFDDSFS 493
Cdd:PRK15079 117 IGEIIAEPLRTYHPKLSRQEVKDRVKAMMLK--VGLLPN-LINRYP---HEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 494 ALDFKTDAKLREALKAETTE-AVTLIVAQRITSVVN--SDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKhiSDRVLVMYLGHAVELGTYDEV 249
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
346-547 |
8.80e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 82.75 E-value: 8.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 346 DITFEANAGETIAIIGSTGAGKSTLI---NM--IPRfydveSGVVKING--------IDVREMDQssLRQKIGLVPQKAV 412
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLrvlNLleMPR-----SGTLNIAGnhfdfsktPSDKAIRE--LRRNVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 413 LFTG-TIASN-----MR---YGKEDATDE--EIWEALRTAQ-AENFVSKLanglgsrveqggnnfSGGQKQRLSIARSLI 480
Cdd:PRK11124 93 LWPHlTVQQNlieapCRvlgLSKDQALARaeKLLERLRLKPyADRFPLHL---------------SGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 481 RKPEIYIFDDSFSALDFKTDAKLREALK--AET-------TEAVTliVAQRITSVVnsdqiIVMNEGKIAGMGTHE 547
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRelAETgitqvivTHEVE--VARKTASRV-----VYMENGHIVEQGDAS 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
327-540 |
9.38e-18 |
|
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: 81.88 E-value: 9.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVRemDQSSLRQKIG- 405
Cdd:cd03268 1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKAVLFTGTIASNMRYGKE--DATDEEIWEALRTAqaenfvsklanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKP 483
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLARllGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 484 EIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVN--SDQIIVMNEGKI 540
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQkvADRIGIINKGKL 204
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
325-518 |
1.01e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 83.37 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 325 AKLSFEHVTFRYEG--AEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVR--EMDQSSL 400
Cdd:COG4525 2 SMLTVRHVSVRYPGggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 401 RQKIGLVPQKAVLftGTIASNMRYGKEDAtdeeiweALRTAQAENFVSK--LANGLGSRVEQggnnFSGGQKQRLSIARS 478
Cdd:COG4525 82 FQKDALLPWLNVL--DNVAFGLRLRGVPK-------AERRARAEELLALvgLADFARRRIWQ----LSGGMRQRVGIARA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1251574723 479 LIRKPEIYIFDDSFSALDFKTDAKLREAL---KAETTEAVTLI 518
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLldvWQRTGKGVFLI 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
327-552 |
1.09e-17 |
|
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: 82.21 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVR--EMDQSSlRQKI 404
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITklPMHKRA-RLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 405 GLVPQKAVLFTG-TIASNMRYGKEDAT-DEEIWEALRTAQAENF-VSKLANGLGSRVeqggnnfSGGQKQRLSIARSLIR 481
Cdd:cd03218 78 GYLPQEASIFRKlTVEENILAVLEIRGlSKKEREEKLEELLEEFhITHLRKSKASSL-------SGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 482 KPEIYIFDDSFSALD---------------------FKTDAKLREALKaetteavtlivaqrITsvvnsDQIIVMNEGKI 540
Cdd:cd03218 151 NPKFLLLDEPFAGVDpiavqdiqkiikilkdrgigvLITDHNVRETLS--------------IT-----DRAYIIYEGKV 211
|
250
....*....|..
gi 1251574723 541 AGMGTHEELKES 552
Cdd:cd03218 212 LAEGTPEEIAAN 223
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-489 |
1.16e-17 |
|
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: 86.01 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 4 LKPYWLSITAVLVLTFGQVIGQLYLPTLMSNIIdkgvvTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKE 83
Cdd:COG4615 8 LRESRWLLLLALLLGLLSGLANAGLIALINQAL-----NATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 84 LRDKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMA---------------PIMLLGGIIMAVGrd 148
Cdd:COG4615 83 LRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSValvlgclaylawlspPLFLLTLVLLGLG-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 149 aklslifvvvlpllLLLVVILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRsFN--RNEDELEKfeeanaDYATTAI 226
Cdd:COG4615 161 --------------VAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELK-LNrrRRRAFFDE------DLQPTAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 227 KVNRLLSLMSPLMMLLMNLTSIAI-VWIGSIFIGNGDMQVGDLMAFIQYAMQIMmsFMM--LSAVFIMIP---RAGASAE 300
Cdd:COG4615 220 RYRDLRIRADTIFALANNWGNLLFfALIGLILFLLPALGWADPAVLSGFVLVLL--FLRgpLSQLVGALPtlsRANVALR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 301 RINEV-LDMNAEILNPENPKTSTPPA---KLSFEHVTFRYEGAEK-------PVieDITFEAnaGETIAIIGSTGAGKST 369
Cdd:COG4615 298 KIEELeLALAAAEPAAADAAAPPAPAdfqTLELRGVTYRYPGEDGdegftlgPI--DLTIRR--GELVFIVGGNGSGKST 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 370 LINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTiasnmrYGKEDATDEEiwealrtaQAENFVSK 449
Cdd:COG4615 374 LAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEADPA--------RARELLER 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1251574723 450 LanGLGSRVE-QGGN----NFSGGQKQRLSIARSLIRKPEIYIFD 489
Cdd:COG4615 440 L--ELDHKVSvEDGRfsttDLSQGQRKRLALLVALLEDRPILVFD 482
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
327-555 |
1.20e-17 |
|
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: 82.34 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAekPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSL-RQKIG 405
Cdd:COG0410 4 LEVENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKAVLFTG-TIASNMRYG--------KEDATDEEIWEAL-RtaqaenfvsklangLGSRVEQGGNNFSGGQKQRLSI 475
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLGayarrdraEVRADLERVYELFpR--------------LKERRRQRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 476 ARSLIRKPEIYIFD------------DSFSALdfktdAKLREalkaettEAVT-LIVAQRITSVVN-SDQIIVMNEGKIA 541
Cdd:COG0410 148 GRALMSRPKLLLLDepslglapliveEIFEII-----RRLNR-------EGVTiLLVEQNARFALEiADRAYVLERGRIV 215
|
250
....*....|....
gi 1251574723 542 GMGTHEELKESNQI 555
Cdd:COG0410 216 LEGTAAELLADPEV 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
344-544 |
1.39e-17 |
|
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: 82.13 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 344 IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREM--DQSSLRQKIGLVPQKAVLFTGTIASN 421
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 422 mrygkedatdeEIWEALRTAQAENFVSKLAN--GLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKT 499
Cdd:TIGR01184 81 -----------RVLPDLSKSERRAIVEEHIAlvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1251574723 500 DAKLREALK--AETTEAVTLIVAQRI-TSVVNSDQIIVMNEGKIAGMG 544
Cdd:TIGR01184 150 RGNLQEELMqiWEEHRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
346-549 |
1.60e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 84.01 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 346 DITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSL---RQKIGLV---------PQKAVl 413
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVfqdpyaslnPRMTV- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 414 ftGTIAS----NMRYGKEDATDEEIWEALRTaqaenfVsklanGLgsRVEQGGNN---FSGGQKQRLSIARSLIRKPEIY 486
Cdd:COG4608 115 --GDIIAeplrIHGLASKAERRERVAELLEL------V-----GL--RPEHADRYpheFSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251574723 487 IFDDSFSALDFKTDAK-------LREALKaetteaVTLIVaqrIT---SVVN--SDQIIVMNEGKIAGMGTHEEL 549
Cdd:COG4608 180 VCDEPVSALDVSIQAQvlnlledLQDELG------LTYLF---IShdlSVVRhiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
338-523 |
3.17e-17 |
|
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: 80.94 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 338 GAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKIN----GIDV-----REMDQssLRQK-IGLV 407
Cdd:COG4778 21 GKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLaqaspREILA--LRRRtIGYV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 408 PQ--KAVLFTGTIASNMRYGKEDATDEEiwEALrtAQAENFVSKLanGLGSRVEQ-GGNNFSGGQKQRLSIARSLIRKPE 484
Cdd:COG4778 99 SQflRVIPRVSALDVVAEPLLERGVDRE--EAR--ARARELLARL--NLPERLWDlPPATFSGGEQQRVNIARGFIADPP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1251574723 485 IYIFDDSFSALDFKTDAKLRE---ALKAETT--------EAVTLIVAQRI 523
Cdd:COG4778 173 LLLLDEPTASLDAANRAVVVElieEAKARGTaiigifhdEEVREAVADRV 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
329-545 |
3.55e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.93 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 329 FEHVTFRYEGAEKPVI--EDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSL---RQK 403
Cdd:PRK11153 4 LKNISKVFPQGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaRRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQKAVLFTG-TIASNMrygkedATDEEIwEALRTAQAENFVSKLAN--GLGSRVEQGGNNFSGGQKQRLSIARSLI 480
Cdd:PRK11153 84 IGMIFQHFNLLSSrTVFDNV------ALPLEL-AGTPKAEIKARVTELLElvGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 481 RKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAqrIT---SVVNS--DQIIVMNEGKIAGMGT 545
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVL--IThemDVVKRicDRVAVIDAGRLVEQGT 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
340-507 |
4.01e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.36 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 340 EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVE-----SGVVKINGIDV--REMDQSSLRQKIGLVPQKAV 412
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 413 LFTGTIASNMRYG------KEDAT-DEEIWEALRTAQAENFVSklanglgSRVEQGGNNFSGGQKQRLSIARSLIRKPEI 485
Cdd:PRK14239 97 PFPMSIYENVVYGlrlkgiKDKQVlDEAVEKSLKGASIWDEVK-------DRLHDSALGLSGGQQQRVCIARVLATSPKI 169
|
170 180
....*....|....*....|..
gi 1251574723 486 YIFDDSFSALDFKTDAKLREAL 507
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETL 191
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
331-540 |
4.06e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.29 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 331 HVTFrYEGA--EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVP 408
Cdd:COG1101 8 SKTF-NPGTvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 409 QKAVLFTG---TIASNM--------RYGkedatdeeIWEALRTAQAENF---VSKLANGLGSRVEQGGNNFSGGQKQRLS 474
Cdd:COG1101 87 QDPMMGTApsmTIEENLalayrrgkRRG--------LRRGLTKKRRELFrelLATLGLGLENRLDTKVGLLSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1251574723 475 IARSLIRKPEIYIFDDSFSALDFKTDAKLREAlkaeTTEAV------TLIVAQRITSVVN-SDQIIVMNEGKI 540
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLEL----TEKIVeennltTLMVTHNMEQALDyGNRLIMMHEGRI 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-566 |
5.90e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.85 E-value: 5.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 324 PAkLSFEHVTFRYEgaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVEsGVVKING--------IDVREM 395
Cdd:PRK14258 6 PA-IKVNNLSFYYD--TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqnIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 396 DQSSLRQKIGLVPQKAVLFTGTIASNMRYG-------KEDATDEEIWEALRTAQaenfvskLANGLGSRVEQGGNNFSGG 468
Cdd:PRK14258 82 NLNRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrPKLEIDDIVESALKDAD-------LWDEIKHKIHKSALDLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 469 QKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLRE-----ALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGM 543
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESliqslRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQL 234
|
250 260
....*....|....*....|...
gi 1251574723 544 gthEELKESNQIYQEIMRSQLSE 566
Cdd:PRK14258 235 ---VEFGLTKKIFNSPHDSRTRE 254
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
329-549 |
6.27e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.60 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 329 FEHVTFRYEGA---EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKInGIDV-----REMDQSSL 400
Cdd:PRK13634 5 FQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKKLKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 401 RQKIGLVPQ--KAVLFTGTIASNMRYGKED-ATDEEiwEALRTAQAenfVSKLAnGLGSRV-EQGGNNFSGGQKQRLSIA 476
Cdd:PRK13634 84 RKKVGIVFQfpEHQLFEETVEKDICFGPMNfGVSEE--DAKQKARE---MIELV-GLPEELlARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 477 RSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEA--VTLIVAQRITSVVN-SDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
344-549 |
6.92e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.77 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 344 IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQ----KIGLVPQK-AVLFTGTI 418
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSfALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 419 ASNMRYGKEDA------TDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSLIRKPEIYIFDDSF 492
Cdd:PRK10070 124 LDNTAFGMELAginaeeRREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 493 SALDFKTDAKLRE---ALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK10070 193 SALDPLIRTEMQDelvKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
344-519 |
1.00e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.21 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 344 IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYD-VES----GVVKINGIDV--REMDQSSLRQKIGLVPQKAVLFTG 416
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlIPGfrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 417 TIASNMRYG------KEDaTDEEIWEALRTAqaenfvsKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDD 490
Cdd:PRK14243 106 SIYDNIAYGaringyKGD-MDELVERSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180
....*....|....*....|....*....
gi 1251574723 491 SFSALDFKTDAKLREALKaETTEAVTLIV 519
Cdd:PRK14243 178 PCSALDPISTLRIEELMH-ELKEQYTIII 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
326-549 |
1.01e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.01 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGID---VREMDQS---- 398
Cdd:PRK10619 5 KLNVIDLHKRY--GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlVRDKDGQlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 399 ------SLRQKIGLVPQKAVLFtgtiaSNMrygkedATDEEIWEA------LRTAQAENFVSKLANGLGSRVEQGGN--- 463
Cdd:PRK10619 83 dknqlrLLRTRLTMVFQHFNLW-----SHM------TVLENVMEApiqvlgLSKQEARERAVKYLAKVGIDERAQGKypv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 464 NFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVN--SDQIIVMNEGKIA 541
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARhvSSHVIFLHQGKIE 231
|
....*...
gi 1251574723 542 GMGTHEEL 549
Cdd:PRK10619 232 EEGAPEQL 239
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
327-549 |
1.12e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.42 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQ-SSLRQKIG 405
Cdd:PRK13644 2 IRLENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKA-VLFTG-TIASNMRYGKEDAT--DEEIWEALRTAQAEnfvsklaNGLGSRVEQGGNNFSGGQKQRLSIARSLIR 481
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDLAFGPENLClpPIEIRKRVDRALAE-------IGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 482 KPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLI-VAQRITSVVNSDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
327-542 |
1.39e-16 |
|
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: 77.47 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAekPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVR-EMDQSSLRQKIG 405
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQkavlftgtiasnmrygkedatdeeiwealrtaqaenfvsklanglgsrveqggnnFSGGQKQRLSIARSLIRKPEI 485
Cdd:cd03216 79 MVYQ-------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 486 YIFDDSFSALDFKTDAKLREALKAETTEAVTLI-VAQRITSVVN-SDQIIVMNEGKIAG 542
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVVG 162
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
327-548 |
2.04e-16 |
|
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: 79.31 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEkpVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDV-------------- 392
Cdd:COG0411 5 LEVRGLTKRFGGLV--AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphriarlgia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 393 ------REMDQSSLRQ--KIGLVPQKAVLFTGTIASNMRYGK-EDATDEEIWEALRtaqaenFVsklanGLGSRVEQGGN 463
Cdd:COG0411 83 rtfqnpRLFPELTVLEnvLVAAHARLGRGLLAALLRLPRARReEREARERAEELLE------RV-----GLADRADEPAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 464 NFSGGQKQRLSIARSLIRKPEIYIFDDSFsaldfktdAKLREALKAETTEAVTLIVAQRITSVV-----------NSDQI 532
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPA--------AGLNPEETEELAELIRRLRDERGITILliehdmdlvmgLADRI 223
|
250
....*....|....*.
gi 1251574723 533 IVMNEGKIAGMGTHEE 548
Cdd:COG0411 224 VVLDFGRVIAEGTPAE 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
327-559 |
3.43e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.98 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEG-AEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIG 405
Cdd:PRK13642 5 LEVENLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKA--VLFTGTIASNMRYGKE------DATDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIAR 477
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMEnqgiprEEMIKRVDEALLAVNMLDFKTREPARL-----------SGGQKQRVAVAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 478 SLIRKPEIYIFDDSFSALDFKTDAKLREALK--AETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQI 555
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSED 233
|
....
gi 1251574723 556 YQEI 559
Cdd:PRK13642 234 MVEI 237
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
340-509 |
4.09e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 77.01 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 340 EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIA 419
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 420 SNMRYGKED--ATDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSLIRKPEIYIFDDSFSALDF 497
Cdd:TIGR01189 92 ENLHFWAAIhgGAQRTIEDALAAVGLTGFEDLPAAQL-----------SAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170
....*....|..
gi 1251574723 498 KTDAKLREALKA 509
Cdd:TIGR01189 161 AGVALLAGLLRA 172
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
327-496 |
4.24e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.45 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGL 406
Cdd:PRK10247 8 LQLQNVGYLAGD--AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTGTIASNMRYG---KEDATDEEIWEA--LRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSLIR 481
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFPwqiRNQQPDPAIFLDdlERFALPDTILTKNIAEL-----------SGGEKQRISLIRNLQF 154
|
170
....*....|....*
gi 1251574723 482 KPEIYIFDDSFSALD 496
Cdd:PRK10247 155 MPKVLLLDEITSALD 169
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
327-548 |
4.85e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 78.23 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGL 406
Cdd:COG4559 2 LEAENLSVRLGG--RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVL---FT-------GTIAsnmrYGKEDATDEEI-WEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSI 475
Cdd:COG4559 80 LPQHSSLafpFTveevvalGRAP----HGSSAAQDRQIvREALALVGLAHLAGRSYQTL-----------SGGEQQRVQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 476 ARSL--IRKPEI----YIF-DDSFSALDFKTDAKLREALKAetteavtliVAQRITSVV------N-----SDQIIVMNE 537
Cdd:COG4559 145 ARVLaqLWEPVDggprWLFlDEPTSALDLAHQHAVLRLARQ---------LARRGGGVVavlhdlNlaaqyADRILLLHQ 215
|
250
....*....|.
gi 1251574723 538 GKIAGMGTHEE 548
Cdd:COG4559 216 GRLVAQGTPEE 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
340-511 |
5.49e-16 |
|
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: 76.76 E-value: 5.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 340 EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIA 419
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 420 SNMRYGKEDATDEEIWEALRTAqaenfvsklanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKT 499
Cdd:cd03231 92 ENLRFWHADHSDEQVEEALARV-----------GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170
....*....|..
gi 1251574723 500 DAKLREALKAET 511
Cdd:cd03231 161 VARFAEAMAGHC 172
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
346-549 |
5.61e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 79.24 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 346 DITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMD---QSSLRQKIGLV---------PQKAVl 413
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVfqnpygslnPRKKV- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 414 ftGTI-----ASNMRYGKEDatdeeiwealRTAQAENFVSKLanglGSRVEQGG---NNFSGGQKQRLSIARSLIRKPEI 485
Cdd:PRK11308 112 --GQIleeplLINTSLSAAE----------RREKALAMMAKV----GLRPEHYDrypHMFSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 486 YIFDDSFSALDFKTDAK---LREALKAETTEAVTLIVAQriTSVVN--SDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK11308 176 VVADEPVSALDVSVQAQvlnLMMDLQQELGLSYVFISHD--LSVVEhiADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-552 |
5.88e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 321 STPPakLSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSl 400
Cdd:PRK13537 4 SVAP--IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 401 RQKIGLVPQKAVL---FTgtIASNMR-YGKedatdeeiWEALRTAQAENFVSKLAN--GLGSRVEQGGNNFSGGQKQRLS 474
Cdd:PRK13537 79 RQRVGVVPQFDNLdpdFT--VRENLLvFGR--------YFGLSAAAARALVPPLLEfaKLENKADAKVGELSGGMKRRLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 475 IARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIV-------AQRItsvvnSDQIIVMNEGKIAGMGTHE 547
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPH 223
|
....*
gi 1251574723 548 ELKES 552
Cdd:PRK13537 224 ALIES 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
340-549 |
6.69e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.86 E-value: 6.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 340 EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPrFYD----VESGVVKING--IDVREMDQSS--LRQKIGLVPQKA 411
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSpkgvKGSGSVLLNGmpIDAKEMRAISayVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 412 VLFTGTIASNMRYGKEDATDE------EIWEALRTAQAENFVSklanGLGSRVEqggnNFSGGQKQRLSIARSLIRKPEI 485
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKKEkrervdEVLQALGLRKCANTRI----GVPGRVK----GLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 486 YIFDDSFSALDFKTDAKLREALKAETTEAVTLIVA-QRITSVV--NSDQIIVMNEGKIAGMGTHEEL 549
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSELfeLFDKIILMAEGRVAYLGSPDQA 254
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
326-549 |
6.86e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.28 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSFEHVTFRYEGA---EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDV----REMDQS 398
Cdd:PRK13646 2 TIRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 399 SLRQKIGLVPQ--KAVLFTGTIASNMRYGKEDAtdeeiweALRTAQAENFVSKLANGLG-SR--VEQGGNNFSGGQKQRL 473
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNF-------KMNLDEVKNYAHRLLMDLGfSRdvMSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 474 SIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKA-ETTEAVTLI-VAQRITSVVN-SDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENKTIIlVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
327-548 |
7.27e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.50 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGL 406
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVL---FT-------GTIAsnmRYGKEDATDEEIWEALrtAQAEnfVSKLAnglGSRVEQggnnFSGGQKQRLSIA 476
Cdd:PRK13548 81 LPQHSSLsfpFTveevvamGRAP---HGLSRAEDDALVAAAL--AQVD--LAHLA---GRDYPQ----LSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 477 RSLIR------KPEIYIFDDSFSALDFKTDAKLREALKAETTEA-VTLIV-------AQRItsvvnSDQIIVMNEGKIAG 542
Cdd:PRK13548 147 RVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERgLAVIVvlhdlnlAARY-----ADRIVLLHQGRLVA 221
|
....*.
gi 1251574723 543 MGTHEE 548
Cdd:PRK13548 222 DGTPAE 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
330-549 |
8.32e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.82 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 330 EHVTFRY----EGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQS-SLRQKI 404
Cdd:PRK13633 8 KNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 405 GLV---PQKAVLFTgTIASNMRYGKED--ATDEEIWEalrtaQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSL 479
Cdd:PRK13633 88 GMVfqnPDNQIVAT-IVEEDVAFGPENlgIPPEEIRE-----RVDESLKKV--GMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251574723 480 IRKPEIYIFDDSFSALDfktDAKLREALKA----ETTEAVTLI-VAQRITSVVNSDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK13633 160 AMRPECIIFDEPTAMLD---PSGRREVVNTikelNKKYGITIIlITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-551 |
1.06e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 78.72 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 321 STPPAKLSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGvvKINGIDVREMDQSSL 400
Cdd:PRK13536 36 SMSTVAIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG--KITVLGVPVPARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 401 -RQKIGLVPQKAVL-FTGTIASNM----RYGKEDATDEE--IWEALRTAQAENFVSklanglgSRVEQggnnFSGGQKQR 472
Cdd:PRK13536 112 aRARIGVVPQFDNLdLEFTVRENLlvfgRYFGMSTREIEavIPSLLEFARLESKAD-------ARVSD----LSGGMKRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 473 LSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNS--DQIIVMNEG-KIAGMGTHEEL 549
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERlcDRLCVLEAGrKIAEGRPHALI 260
|
..
gi 1251574723 550 KE 551
Cdd:PRK13536 261 DE 262
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
329-489 |
2.20e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 329 FEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKI-NGIDVremdqSSLRQKIGLV 407
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRI-----GYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 408 PQKAVL------FTGTIASNMRY----GKEDATDE------EIWEALRTA---QAENFVSKLANGLGSRVEQGG---NNF 465
Cdd:COG0488 74 DDLTVLdtvldgDAELRALEAELeeleAKLAEPDEdlerlaELQEEFEALggwEAEARAEEILSGLGFPEEDLDrpvSEL 153
|
170 180
....*....|....*....|....
gi 1251574723 466 SGGQKQRLSIARSLIRKPEIYIFD 489
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLD 177
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
327-552 |
2.77e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 76.69 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvREMDQSSlRQKIGL 406
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPED-RRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPqkavlftgtiasnmrygkedatdEE--------IWEALR-------------TAQAENFVSKLanGLGSRVEQGGNNF 465
Cdd:COG4152 76 LP-----------------------EErglypkmkVGEQLVylarlkglskaeaKRRADEWLERL--GLGDRANKKVEEL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 466 SGGQKQRLSIARSLIRKPEIYIFDDSFSALD-FKTDaKLREALKAETTEAVTLI-------VAQRItsvvnSDQIIVMNE 537
Cdd:COG4152 131 SKGNQQKVQLIAALLHDPELLILDEPFSGLDpVNVE-LLKDVIRELAAKGTTVIfsshqmeLVEEL-----CDRIVIINK 204
|
250
....*....|....*
gi 1251574723 538 GKIAGMGTHEELKES 552
Cdd:COG4152 205 GRKVLSGSVDEIRRQ 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
333-544 |
2.78e-15 |
|
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: 75.26 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 333 TFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVremdqSSLRQKIGLVPQkav 412
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLLGLGGGFNPE--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 413 lFTGT--IASNMR-YGKedaTDEEIwealrtAQAENFVSKLAnGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFD 489
Cdd:cd03220 99 -LTGRenIYLNGRlLGL---SRKEI------DEKIDEIIEFS-ELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 490 DSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNS--DQIIVMNEGKIAGMG 544
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRlcDRALVLEKGKIRFDG 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
341-540 |
3.73e-15 |
|
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: 73.62 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 341 KPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMD-QSSLRQKIGLVP---QKAVLFTG 416
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 417 -TIASNMRygkedatdeeiwealrtaqaenfvskLANGLgsrveqggnnfSGGQKQRLSIARSLIRKPEIYIFDDSFSAL 495
Cdd:cd03215 93 lSVAENIA--------------------------LSSLL-----------SGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1251574723 496 DFKTDAKLREALKAETTEAVTLIVaqrITS-----VVNSDQIIVMNEGKI 540
Cdd:cd03215 136 DVGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
338-538 |
4.67e-15 |
|
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: 74.29 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 338 GAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVV----KINGIDVREMDQSSLRQKIGLVPQKAVL 413
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 414 FTGTIASNMRYGKedATDEEIWEALRTA-QAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSF 492
Cdd:cd03290 91 LNATVEENITFGS--PFNKQRYKAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1251574723 493 SALDFKTDAKLREA--LKAETTEAVTLI-VAQRITSVVNSDQIIVMNEG 538
Cdd:cd03290 169 SALDIHLSDHLMQEgiLKFLQDDKRTLVlVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
327-549 |
5.02e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.65 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRY-EGAEkpVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKING--IDVREMDQSSLRQK 403
Cdd:PRK13636 6 LKVEELNYNYsDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQKA--VLFTGTIASNMRYGKEDAT--DEEIWEALRTAQAENFVSKLANglgsrveQGGNNFSGGQKQRLSIARSL 479
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1251574723 480 IRKPEIYIFDDSFSALDFKTDAKLREALKAETTE-AVTLIVAQRITSVVN--SDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPlyCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
343-557 |
1.53e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.89 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 343 VIEDITFEANAGETIAIIGSTGAGKSTLIN-----MIPRFYDVESGVVKINGIDVREMDQSS-----------LRQKIGL 406
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQ--KAVLFTGTIASNMRYGKedatdeeIWEALRTAQAENFVSKLANGLG---SRVEQGGNNFSGGQKQRLSIARSLIR 481
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMFGP-------VALGVKKSEAKKLAKFYLNKMGlddSYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 482 KPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVaqrITSVVN-----SDQIIVMNEGKIAGMGTHEELKESNQIY 556
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFV---ITHTMEhvlevADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
.
gi 1251574723 557 Q 557
Cdd:PRK13631 271 N 271
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
330-549 |
1.56e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.58 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 330 EHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQ 409
Cdd:COG4604 5 KNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 410 kavlfTGTIASNM---------RY----GKEDATDEE-IWEALR----TAQAENFVSKLanglgsrveqggnnfSGGQKQ 471
Cdd:COG4604 83 -----ENHINSRLtvrelvafgRFpyskGRLTAEDREiIDEAIAyldlEDLADRYLDEL---------------SGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 472 RLSIARSLIRKPEiYIF-DDSFSALDFKTDAKLREALKAETTEA--VTLIVAQRItsvvN-----SDQIIVMNEGKIAGM 543
Cdd:COG4604 143 RAFIAMVLAQDTD-YVLlDEPLNNLDMKHSVQMMKLLRRLADELgkTVVIVLHDI----NfascyADHIVAMKDGRVVAQ 217
|
....*.
gi 1251574723 544 GTHEEL 549
Cdd:COG4604 218 GTPEEI 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
321-540 |
1.70e-14 |
|
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: 73.24 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 321 STPPAkLSFEHVTFRYEGAEKPV--IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQS 398
Cdd:COG4181 4 SSAPI-IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 399 SL----RQKIGLVPQKAVLftgtIAS-----N-M----RYGKEDATDeeiwealrTAQAEnfvskLAN-GLGSRVEQGGN 463
Cdd:COG4181 83 ARarlrARHVGFVFQSFQL----LPTltaleNvMlpleLAGRRDARA--------RARAL-----LERvGLGHRLDHYPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 464 NFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEA-VTLIV-------AQRitsvvnSDQIIVM 535
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVLvthdpalAAR------CDRVLRL 219
|
....*
gi 1251574723 536 NEGKI 540
Cdd:COG4181 220 RAGRL 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
346-549 |
1.79e-14 |
|
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: 75.14 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 346 DITFEANAGETIAIIGSTGAGKSTLINMI-----PrfydvESGVVKING---------IDV-REmdqsslRQKIGLVPQK 410
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglerP-----DSGRIRLGGevlqdsargIFLpPH------RRRIGYVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 411 AVLF-TGTIASNMRYGkedatdeeIWEALRTAQAENF---VSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIY 486
Cdd:COG4148 86 ARLFpHLSVRGNLLYG--------RKRAPRAERRISFdevVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 487 IFDDSFSALDFKTDAKLR---EALKAET-----------TEAVTLivaqritsvvnSDQIIVMNEGKIAGMGTHEEL 549
Cdd:COG4148 156 LMDEPLAALDLARKAEILpylERLRDELdipilyvshslDEVARL-----------ADHVVLLEQGRVVASGPLAEV 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
324-570 |
2.27e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.48 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 324 PAKLSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQK 403
Cdd:PRK10253 5 VARLRGEQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQKAV--------------------LFTgtiasnmRYGKEDatDEEIWEALRtaqaenfvsklANGLGSRVEQGGN 463
Cdd:PRK10253 83 IGLLAQNATtpgditvqelvargryphqpLFT-------RWRKED--EEAVTKAMQ-----------ATGITHLADQSVD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 464 NFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREAL------KAETTEAVTLIVAQritSVVNSDQIIVMNE 537
Cdd:PRK10253 143 TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLselnreKGYTLAAVLHDLNQ---ACRYASHLIALRE 219
|
250 260 270
....*....|....*....|....*....|....*.
gi 1251574723 538 GKIAGMGTHEELKESN---QIYQeiMRSQLSEEEIA 570
Cdd:PRK10253 220 GKIVAQGAPKEIVTAElieRIYG--LRCMIIDDPVA 253
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-549 |
2.50e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.16 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 340 EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGI------DVREMDQSSLRQKIGLVPQKAVL 413
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 414 FTG-TIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSF 492
Cdd:PRK14246 102 FPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 493 SALDFKTDAKLREALKAETTEAVTLIVAQRITSVVN-SDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
332-549 |
2.75e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.30 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 332 VTFRYEGAEKpVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKA 411
Cdd:PRK13652 9 LCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 412 --VLFTGTIASNMRYG------KEDATDEEIWEALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSLIRKP 483
Cdd:PRK13652 88 ddQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 484 EIYIFDDSFSALDFKTDAKLREALKA-ETTEAVTLIVAQRITSVVNS--DQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDlPETYGMTVIFSTHQLDLVPEmaDYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
343-549 |
2.84e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.02 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 343 VIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVE-----SGVVKINGIDVREMDQSSLRQKIGLV-----PQKAV 412
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVfqipnPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 413 LFTGTIASNMRYGKEDATDEEIWEALRTAQAEnfvSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSF 492
Cdd:PRK14247 98 SIFENVALGLKLNRLVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 493 SALDFKTDAKLrEALKAETTEAVTLIV-------AQRItsvvnSDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK14247 175 ANLDPENTAKI-ESLFLELKKDMTIVLvthfpqqAARI-----SDYVAFLYKGQIVEWGPTREV 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
327-540 |
3.19e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.32 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGA---EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQS----S 399
Cdd:PRK13641 3 IKFENVDYIYSPGtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 400 LRQKIGLVPQ--KAVLFTGTIASNMRYGKED--ATDEEIWEalrtaQAENFVSKLanGLGSRV-EQGGNNFSGGQKQRLS 474
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKE-----KALKWLKKV--GLSEDLiSKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 475 IARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLI-VAQRITSVVN-SDQIIVMNEGKI 540
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVIlVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
327-540 |
5.11e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.72 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKInGIDVremdqsslrqKIGL 406
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTG--TIASNMRYGKEDATDEEIWEAL-----RTAQAENFVSKLanglgsrveqggnnfSGGQKQRLSIARSL 479
Cdd:COG0488 383 FDQHQEELDPdkTVLDELRDGAPGGTEQEVRGYLgrflfSGDDAFKPVGVL---------------SGGEKARLALAKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 480 IRKPEIYIFD----DsfsaLDFKTdaklREALkaetTEAV-----TLIVA-------QRITsvvnsDQIIVMNEGKI 540
Cdd:COG0488 448 LSPPNVLLLDeptnH----LDIET----LEAL----EEALddfpgTVLLVshdryflDRVA-----TRILEFEDGGV 507
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
327-524 |
5.15e-14 |
|
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: 69.88 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFrYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvremdqsslRQKIGL 406
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTGTIASNMRYGkedatdeeiWealrtaqaenfvsklanglgsrveqgGNNFSGGQKQRLSIARSLIRKPEIY 486
Cdd:cd03223 69 LPQRPYLPLGTLREQLIYP---------W--------------------------DDVLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*....
gi 1251574723 487 IFDDSFSALDFKTDAKLREALKAETTeavTLI-VAQRIT 524
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKELGI---TVIsVGHRPS 149
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
327-540 |
7.71e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.03 E-value: 7.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRY-------EGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQS- 398
Cdd:PRK10419 4 LNVSGLSHHYahgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 399 --SLRQKIGLV---------PQKAVlfTGTIASNMRYgkedATDEEiwEALRTAQAENFVS--KLANGLGSRVEQggnNF 465
Cdd:PRK10419 84 rkAFRRDIQMVfqdsisavnPRKTV--REIIREPLRH----LLSLD--KAERLARASEMLRavDLDDSVLDKRPP---QL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 466 SGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDA---KLREALKAETTEAVTLI-----VAQRITSVVnsdqiIVMNE 537
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAgviRLLKKLQQQFGTACLFIthdlrLVERFCQRV-----MVMDN 227
|
...
gi 1251574723 538 GKI 540
Cdd:PRK10419 228 GQI 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
327-539 |
8.30e-14 |
|
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: 68.63 E-value: 8.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvremdqsslRQKIGL 406
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQkavlftgtiasnmrygkedatdeeiwealrtaqaenfvsklanglgsrveqggnnFSGGQKQRLSIARSLIRKPEIY 486
Cdd:cd03221 68 FEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 487 IFDDSFSALDFKTDAKLREALKAETTeavTLIVA----QRITSVVNsdQIIVMNEGK 539
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEYPG---TVILVshdrYFLDQVAT--KIIELEDGK 144
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
335-551 |
8.74e-14 |
|
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: 70.25 E-value: 8.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 335 RYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMI---PRfYDVESGVVKINGIDVREMD-QSSLRQKIGLVPQK 410
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghPK-YEVTEGEILFKGEDITDLPpEERARLGIFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 411 AVLFTG-TIASNMRYgkedatdeeiwealrtaqaenfvsklanglgsrVEQGgnnFSGGQKQRLSIARSLIRKPEIYIFD 489
Cdd:cd03217 86 PPEIPGvKNADFLRY---------------------------------VNEG---FSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 490 DSFSALD---FKTDAKLREALKAETTEAvtLIVA--QRITSVVNSDQIIVMNEGKIAGMGTHEELKE 551
Cdd:cd03217 130 EPDSGLDidaLRLVAEVINKLREEGKSV--LIIThyQRLLDYIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
325-496 |
1.32e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.69 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 325 AKLSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMD-QSSLRQK 403
Cdd:PRK10895 2 ATLTAKNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQKAVLFTGTIASNMRYG----KEDATDEEIWEALRTAQAENFVSKLANGLgsrveqgGNNFSGGQKQRLSIARSL 479
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAvlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARAL 152
|
170
....*....|....*..
gi 1251574723 480 IRKPEIYIFDDSFSALD 496
Cdd:PRK10895 153 AANPKFILLDEPFAGVD 169
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
326-552 |
1.42e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.64 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVE-----SGVVKINGIDV--REMDQS 398
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 399 SLRQKIGLVPQKAVLFTG-TIASNMRYG--------KEDATDEEIWEALRTAqaenfvsKLANGLGSRVEQGGNNFSGGQ 469
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHlTIYDNVAIGvklnglvkSKKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 470 KQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIV------AQRItsvvnSDQIIVMNEGKIAGM 543
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVthspaqAARV-----SDYVAFLYLGKLIEV 229
|
....*....
gi 1251574723 544 GTHEELKES 552
Cdd:PRK14267 230 GPTRKVFEN 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
327-559 |
1.54e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 71.31 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGA---EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVR----EMDQSS 399
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 400 LRQKIGLVPQ--KAVLFTGTIASNMRYGKED-ATDEEiwEALRTAQAENFVSKLANGLGSRveqggNNF--SGGQKQRLS 474
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfGVSQE--EAEALAREKLALVGISESLFEK-----NPFelSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 475 IARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLI-VAQRITSVVN-SDQIIVMNEGKIAGMGtheelkES 552
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSG------KP 229
|
....*..
gi 1251574723 553 NQIYQEI 559
Cdd:PRK13649 230 KDIFQDV 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
327-559 |
2.09e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.92 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEgAEKP----VIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDV----REMDQS 398
Cdd:PRK13643 2 IKFEKVNYTYQ-PNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 399 SLRQKIGLVPQ--KAVLFTGTIASNMRYGKED-ATDEEIWEALRTAQAENFvsklanGLGSRV-EQGGNNFSGGQKQRLS 474
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEETVLKDVAFGPQNfGIPKEKAEKIAAEKLEMV------GLADEFwEKSPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 475 IARSLIRKPEIYIFDDSFSALDFKTDAKLREALKA--ETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTheelkeS 552
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESihQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT------P 228
|
....*..
gi 1251574723 553 NQIYQEI 559
Cdd:PRK13643 229 SDVFQEV 235
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-552 |
2.22e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.51 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 339 AEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGV-----VKINGIDV-REMDQSSLRQKIGLVPQKAV 412
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIfNYRDVLEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 413 LFTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSF 492
Cdd:PRK14271 112 PFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251574723 493 SALDFKTDAKLREALKAETTEAVTLIVAQRITSVVN-SDQIIVMNEGKIAGMGTHEELKES 552
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
358-568 |
2.42e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.44 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 358 AIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQS-SL---RQKIGLVPQKAVLFTG-TIASNMRYG--KEDAt 430
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLppeKRRIGYVFQDARLFPHyKVRGNLRYGmaKSMV- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 431 deeiwealrtAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFktdAKLREALK-- 508
Cdd:PRK11144 107 ----------AQFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL---PRKRELLPyl 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 509 ---AETTEAVTLIVAQRITSVVN-SDQIIVMNEGKIAGMGTHEELKESnqiyqEIMRSQLSEEE 568
Cdd:PRK11144 172 erlAREINIPILYVSHSLDEILRlADRVVVLEQGKVKAFGPLEEVWAS-----SAMRPWLPKEE 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
323-549 |
2.96e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 323 PPAKLSFEHVTFryegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQ 402
Cdd:PRK09536 2 PMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 403 KIGLVPQKAVL---FTGTIASNM-------RYGKEDATDEEIWE-ALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQ 471
Cdd:PRK09536 78 RVASVPQDTSLsfeFDVRQVVEMgrtphrsRFDTWTETDRAAVErAMERTGVAQFADRPVTSL-----------SGGERQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 472 RLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALK--AETTEAVT-----LIVAQRItsvvnSDQIIVMNEGKIAGMG 544
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRrlVDDGKTAVaaihdLDLAARY-----CDELVLLADGRVRAAG 221
|
....*
gi 1251574723 545 THEEL 549
Cdd:PRK09536 222 PPADV 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
334-549 |
3.78e-13 |
|
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: 72.02 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 334 FRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTL----INMIPRfydveSGVVKINGIDVREMDQS---SLRQKIGL 406
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLDGLSRRalrPLRRRMQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 V---------PQKAVlfTGTIASNMRYGKEDATDEEIWEALRTAQAEnfVsklanGLGSRV------EqggnnFSGGQKQ 471
Cdd:COG4172 367 VfqdpfgslsPRMTV--GQIIAEGLRVHGPGLSAAERRARVAEALEE--V-----GLDPAArhryphE-----FSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 472 RLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKaetteavTLivaQR--------IT---SVVN--SDQIIVMNEG 538
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLR-------DL---QRehglaylfIShdlAVVRalAHRVMVMKDG 502
|
250
....*....|.
gi 1251574723 539 KIAGMGTHEEL 549
Cdd:COG4172 503 KVVEQGPTEQV 513
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
318-569 |
3.89e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 318 PKTSTPPAK--LSFEHVTFRyegaekPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREM 395
Cdd:COG1129 246 PKRAAAPGEvvLEVEGLSVG------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 396 D-QSSLRQKIGLVP----QKAVLFTGTIASNM------RYGKedatdeeiWEALRTAQAENFVSKLANGLG---SRVEQG 461
Cdd:COG1129 320 SpRDAIRAGIAYVPedrkGEGLVLDLSIRENItlasldRLSR--------GGLLDRRRERALAEEYIKRLRiktPSPEQP 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 462 GNNFSGGQKQRLSIARSLIRKPEIYIFDDSfsaldfkT---D--AK------LREAlkAEttEAVTLIVaqrITS----V 526
Cdd:COG1129 392 VGNLSGGNQQKVVLAKWLATDPKVLILDEP-------TrgiDvgAKaeiyrlIREL--AA--EGKAVIV---ISSelpeL 457
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1251574723 527 V-NSDQIIVMNEGKIAGmgtheelkesnqiyqEIMRSQLSEEEI 569
Cdd:COG1129 458 LgLSDRILVMREGRIVG---------------ELDREEATEEAI 486
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
326-565 |
6.06e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.89 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIG 405
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKAVLFTG-TIASNMRYGKE---------DATDEEIWE-ALRTAQAENFVSKLANGLgsrveqggnnfSGGQKQRLS 474
Cdd:PRK11231 80 LLPQHHLTPEGiTVRELVAYGRSpwlslwgrlSAEDNARVNqAMEQTRINHLADRRLTDL-----------SGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 475 IARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIV-------AQRItsvvnSDQIIVMNEGKIAGMGTHE 547
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTvlhdlnqASRY-----CDHLVVLANGHVMAQGTPE 223
|
250 260
....*....|....*....|....
gi 1251574723 548 E------LKESNQIYQEIMRSQLS 565
Cdd:PRK11231 224 EvmtpglLRTVFDVEAEIHPEPVS 247
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
340-501 |
6.08e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.98 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 340 EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGlvPQKAVLFTGTIA 419
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 420 SNMRYGKE--DATDEEIWEALrtaqaeNFVsklanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDF 497
Cdd:PRK13539 92 ENLEFWAAflGGEELDIAAAL------EAV-----GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
....
gi 1251574723 498 KTDA 501
Cdd:PRK13539 161 AAVA 164
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
28-302 |
6.30e-13 |
|
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: 69.47 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 28 LPTLMSNIIDkgVVTGDTDYIwsTGMKMLLISFASVILSVIV---------VYLASRISMGFGKELRDKIFTKVEDfslQ 98
Cdd:cd18573 15 VPFAIGKLID--VASKESGDI--EIFGLSLKTFALALLGVFVvgaaanfgrVYLLRIAGERIVARLRKRLFKSILR---Q 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 99 E---FDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVILGGKAMP 175
Cdd:cd18573 88 DaafFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 176 MFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIGS 255
Cdd:cd18573 168 LSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1251574723 256 IFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18573 248 SLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
11-302 |
6.80e-13 |
|
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: 69.46 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGM-----KMLLISFASVILSVIVV----------YLASR 75
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLGLAPllgpdPLALLLLAAAALVGIALlrglasyagtYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 76 ISMGFGKELRDKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNV--------LYMMMRLMVMAPIML-----LGGII 142
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLlvsgvlplLTNLLTLVGMLGVMFwldwqLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 143 MAVgrdaklslifvvvlplllllvvilggkaMPMF----KSLQKKMDKLNRVIR-----------EGLTGIRVVRSFNRN 207
Cdd:cd18564 161 LAV----------------------------APLLllaaRRFSRRIKEASREQRrregalasvaqESLSAIRVVQAFGRE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 208 EDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYaMQIMMSFM-MLS 286
Cdd:cd18564 213 EHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY-LKNLYKPVrDLA 291
|
330
....*....|....*.
gi 1251574723 287 AVFIMIPRAGASAERI 302
Cdd:cd18564 292 KLTGRIAKASASAERV 307
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
322-489 |
7.75e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 322 TPPAKLSFEHVTFRYEGaekpVI--EDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvREMDQSS 399
Cdd:COG3845 1 MMPPALELRGITKRFGG----VVanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 400 ----LRQKIGLVPQKAVLF-TGTIASNMRYGKEDATdeeiWEALRTAQAENFVSKLANGLG------SRVEQggnnFSGG 468
Cdd:COG3845 74 prdaIALGIGMVHQHFMLVpNLTVAENIVLGLEPTK----GGRLDRKAARARIRELSERYGldvdpdAKVED----LSVG 145
|
170 180
....*....|....*....|.
gi 1251574723 469 QKQRLSIARSLIRKPEIYIFD 489
Cdd:COG3845 146 EQQRVEILKALYRGARILILD 166
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
340-563 |
8.19e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.18 E-value: 8.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 340 EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvremdqsslrqKI--------GLVPQka 411
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVsallelgaGFHPE-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 412 vlFTGT--IASNMR-YGkedATDEEIwealrtAQAENFVSKLAnGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIF 488
Cdd:COG1134 103 --LTGRenIYLNGRlLG---LSRKEI------DEKFDEIVEFA-ELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 489 DDSFSALD--FKtdAKLREALKAETTEAVTLIVAQRITSVVNS--DQIIVMNEGKIAGMGTHEELKEsnqIYQEIMRSQ 563
Cdd:COG1134 171 DEVLAVGDaaFQ--KKCLARIRELRESGRTVIFVSHSMGAVRRlcDRAIWLEKGRLVMDGDPEEVIA---AYEALLAGR 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
327-549 |
8.26e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.99 E-value: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEkpVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRF--YDVESGVV------------------- 385
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 386 --------------KINGIDVREMDQSSLRQKIglvpqkAVLFTGTIAsnmRYGkEDATDEEIWEALRTA--QAENFVSK 449
Cdd:TIGR03269 79 gepcpvcggtlepeEVDFWNLSDKLRRRIRKRI------AIMLQRTFA---LYG-DDTVLDNVLEALEEIgyEGKEAVGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 450 LAN-----GLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREAL-KAETTEAVTLIVAQRI 523
Cdd:TIGR03269 149 AVDliemvQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVLTSHW 228
|
250 260
....*....|....*....|....*...
gi 1251574723 524 TSVVN--SDQIIVMNEGKIAGMGTHEEL 549
Cdd:TIGR03269 229 PEVIEdlSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
331-540 |
9.01e-13 |
|
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: 67.29 E-value: 9.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 331 HVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLI----NMIPRFYDVEsGVVKINGIDVREMDQSslrqkigl 406
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkalaNRTEGNVSVE-GDIHYNGIPYKEFAEK-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 vpqkavlFTGTIASNmryGKEDA-----TDEEIWEALRTAQAENFVSKlanglgsrveqggnnFSGGQKQRLSIARSLIR 481
Cdd:cd03233 81 -------YPGEIIYV---SEEDVhfptlTVRETLDFALRCKGNEFVRG---------------ISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 482 KPEIYIFD------DSFSALDFKTdaKLREalKAETTEAVTLIV----AQRITSVVnsDQIIVMNEGKI 540
Cdd:cd03233 136 RASVLCWDnstrglDSSTALEILK--CIRT--MADVLKTTTFVSlyqaSDEIYDLF--DKVLVLYEGRQ 198
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
334-544 |
1.20e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 334 FRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKST----LINMIPrfydvESGVVKINGidvREMDQSSLRQKIGLVPQ 409
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDG---QPLHNLNRRQLLPVRHR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 410 KAVLFTGTIAS-NMRYGKEdatdEEIWEALRT-------AQAENFVSKLANGLG----SRvEQGGNNFSGGQKQRLSIAR 477
Cdd:PRK15134 364 IQVVFQDPNSSlNPRLNVL----QIIEEGLRVhqptlsaAQREQQVIAVMEEVGldpeTR-HRYPAEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 478 SLIRKPEIYIFDDSFSALDFKTDAKLREALKA-ETTEAVTLIVAQRITSVVNS--DQIIVMNEGKIAGMG 544
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDKTVQAQILALLKSlQQKHQLAYLFISHDLHVVRAlcHQVIVLRQGEVVEQG 508
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
343-499 |
1.36e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.53 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 343 VIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSS---LR-QKIGLVPQKAVL---FT 415
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQKLGFIYQFHHLlpdFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 416 G--TIASNMRYGKEdatdeeiwealRTAQAENFVSKL--ANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDS 491
Cdd:PRK11629 104 AleNVAMPLLIGKK-----------KPAEINSRALEMlaAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
....*...
gi 1251574723 492 FSALDFKT 499
Cdd:PRK11629 173 TGNLDARN 180
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
327-489 |
1.71e-12 |
|
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: 67.17 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEkpVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMD-QSSLRQKIG 405
Cdd:TIGR03410 1 LEVSNLNVYYGQSH--ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKAVLFTG-TIASNMRYG------KEDATDEEIWE---ALRTAqaenfvsklangLGSRveqgGNNFSGGQKQRLSI 475
Cdd:TIGR03410 79 YVPQGREIFPRlTVEENLLTGlaalprRSRKIPDEIYElfpVLKEM------------LGRR----GGDLSGGQQQQLAI 142
|
170
....*....|....
gi 1251574723 476 ARSLIRKPEIYIFD 489
Cdd:TIGR03410 143 ARALVTRPKLLLLD 156
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
314-540 |
1.97e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.40 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 314 NPENPKTSTPpakLSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMI-----PRFYDVESGVVKIN 388
Cdd:PRK11247 3 NTARLNQGTP---LLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLagletPSAGELLAGTAPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 389 GI--DVREMDQSSlRqkigLVPQKAVLftgtiaSNMRYGKEDATDEEIWEALRtaqaenfvsklANGLGSRVEQGGNNFS 466
Cdd:PRK11247 78 EAreDTRLMFQDA-R----LLPWKKVI------DNVGLGLKGQWRDAALQALA-----------AVGLADRANEWPAALS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 467 GGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAK---LREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKI 540
Cdd:PRK11247 136 GGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEmqdLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
324-496 |
2.41e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.98 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 324 PAKLSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVRE--MDQSSlR 401
Cdd:COG1137 1 MMTLEAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpMHKRA-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 402 QKIGLVPQKAVLFTG-TIASNMR-----YGKEDATDEEIWEALrtaqAENF-VSKLANGLGSRVeqggnnfSGGQKQRLS 474
Cdd:COG1137 78 LGIGYLPQEASIFRKlTVEDNILavlelRKLSKKEREERLEEL----LEEFgITHLRKSKAYSL-------SGGERRRVE 146
|
170 180
....*....|....*....|..
gi 1251574723 475 IARSLIRKPEIYIFDDSFSALD 496
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVD 168
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
334-540 |
2.70e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 66.59 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 334 FRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREmDQSSLRQKIGLV-PQKAv 412
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVfGQKT- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 413 lftgTIASNMRYGKEDATDEEIWEaLRTAQAENFVSKLANGL--GSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDD 490
Cdd:cd03267 105 ----QLWWDLPVIDSFYLLAAIYD-LPPARFKKRLDELSELLdlEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1251574723 491 SFSALDFKTDAKLREALKAETTEAVTLIV-----AQRITSVvnSDQIIVMNEGKI 540
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLltshyMKDIEAL--ARRVLVIDKGRL 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
344-554 |
2.86e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 344 IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvREMDQSSLRQKIGLVPQKAVLFTGTIASnmr 423
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG---QRIDTLSPGKLQALRRDIQFIFQDPYAS--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 424 YGKEDATDEEIWEALRT------AQAENFVSKLANGLGSRVEQG---GNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSA 494
Cdd:PRK10261 414 LDPRQTVGDSIMEPLRVhgllpgKAAAARVAWLLERVGLLPEHAwryPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 495 LDFKTDAK---LREALKAETTEAVTLI-----VAQRItsvvnSDQIIVMNEGKIAGMGTHEELKESNQ 554
Cdd:PRK10261 494 LDVSIRGQiinLLLDLQRDFGIAYLFIshdmaVVERI-----SHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
327-496 |
3.35e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAekPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMD-QSSLRQKIG 405
Cdd:COG1129 5 LEMRGISKSFGGV--KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKAVLFTG-TIASNMRYGKEDAT----DeeiWEALRtAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLI 480
Cdd:COG1129 83 IIHQELNLVPNlSVAENIFLGREPRRggliD---WRAMR-RRARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170
....*....|....*.
gi 1251574723 481 RKPEIYIFDDSFSALD 496
Cdd:COG1129 157 RDARVLILDEPTASLT 172
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
354-519 |
4.40e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.96 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 354 GETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQ---SSLR-QKIGLVPQKAVLF-TGTIASNMRY---- 424
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRaKHVGFVFQSFMLIpTLNALENVELpall 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 425 -GKEDATDEEiwealrtaQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKL 503
Cdd:PRK10584 116 rGESSRQSRN--------GAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170
....*....|....*..
gi 1251574723 504 REALKAETTE-AVTLIV 519
Cdd:PRK10584 186 ADLLFSLNREhGTTLIL 202
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
347-550 |
5.04e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.17 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 347 ITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGID--------------VREMDQSSLRQKIG-----LV 407
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqiarmgvVRTFQHVRLFREMTvienlLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 408 PQ----KAVLFTGTIAS-NMRYGKEDATDeeiwealRTAQAENFVsklanGLGSRVEQGGNNFSGGQKQRLSIARSLIRK 482
Cdd:PRK11300 104 AQhqqlKTGLFSGLLKTpAFRRAESEALD-------RAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1251574723 483 PEIYIFDDSFSALDFKTDAKLRE---ALKAETTEAVTLIvaQRITSVVN--SDQIIVMNEGKIAGMGTHEELK 550
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDEliaELRNEHNVTVLLI--EHDMKLVMgiSDRIYVVNQGTPLANGTPEEIR 242
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
333-549 |
5.67e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.35 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 333 TFRYEG---------AEKPViediTFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQK 403
Cdd:PRK15112 13 TFRYRTgwfrrqtveAVKPL----SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQKAvlfTGTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLGSRVEQGG---NNFSGGQKQRLSIARSLI 480
Cdd:PRK15112 89 IRMIFQDP---STSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASyypHMLAPGQKQRLGLARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 481 RKPEIYIFDDSFSALDFKTDAKLRE-ALKAETTEAVTLI-VAQRITSVVN-SDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK15112 166 LRPKVIIADEALASLDMSMRSQLINlMLELQEKQGISYIyVTQHLGMMKHiSDQVLVMHQGEVVERGSTADV 237
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
340-551 |
7.52e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.82 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 340 EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMI---PRfYDVESGVVKINGIDVREMDqSSLRQKIG--LVPQKAVLF 414
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghPA-YKILEGDILFKGESILDLE-PEERAHLGifLAFQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 415 TGT-------IASNMR---YGKEDATDEEIWEALRTAQaeNFVSKLANGLGSRVEQGgnnFSGGQKQRLSIARSLIRKPE 484
Cdd:CHL00131 97 PGVsnadflrLAYNSKrkfQGLPELDPLEFLEIINEKL--KLVGMDPSFLSRNVNEG---FSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 485 IYIFDDSFSALD---FKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKE 551
Cdd:CHL00131 172 LAILDETDSGLDidaLKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGDAELAKE 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
331-549 |
9.57e-12 |
|
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: 67.40 E-value: 9.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 331 HVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKS----TLINMIPRFYDVESGVVKINGIDVREMDQSSLRQ---- 402
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 403 KIGLVPQKAV-----LFT-G-----TIASNMRYGKEDATdEEIWEALRT---AQAEnfvsklanglgSRVEQGGNNFSGG 468
Cdd:COG4172 93 RIAMIFQEPMtslnpLHTiGkqiaeVLRLHRGLSGAAAR-ARALELLERvgiPDPE-----------RRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 469 QKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAK----LREaLKAETTEAVTLI-----VAQRItsvvnSDQIIVMNEGK 539
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQildlLKD-LQRELGMALLLIthdlgVVRRF-----ADRVAVMRQGE 234
|
250
....*....|
gi 1251574723 540 IAGMGTHEEL 549
Cdd:COG4172 235 IVEQGPTAEL 244
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
26-302 |
1.25e-11 |
|
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: 65.90 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 26 LYLPTLMSNIIDkGVVTGDTDYIWSTGMKMLLISFASVILSVIV--------VYLASRISMGFGKELRDKIFTKVEDFSL 97
Cdd:cd18554 16 LLLPLILKYIVD-DVIQGSSLTLDEKVYKLFTIIGIMFFIFLILrppveyyrQYFAQWIANKILYDIRKDLFDHLQKLSL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 98 QEFDKVGTSSLITRTTNDVVQIQN-VLYMMMRLMVMAPIMLLGGIIMAVGrDAKLSLIFVVVLPLLLLLVVILGGKAMPM 176
Cdd:cd18554 95 RYYANNRSGEIISRVINDVEQTKDfITTGLMNIWLDMITIIIAICIMLVL-NPKLTFVSLVIFPFYILAVKYFFGRLRKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 177 FKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIGSI 256
Cdd:cd18554 174 TKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAY 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1251574723 257 FIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18554 254 LVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
18-299 |
1.41e-11 |
|
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: 65.35 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 18 TFGQVIG---QLYLPTLMSNIID------KGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKI 88
Cdd:cd18780 2 TIALLVSsgtNLALPYFFGQVIDavtnhsGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 89 FTKVedfSLQE---FDKVGTSSLITRTTNDVVQIQNV----LYMMMRLMVMApimlLGGIIMAVGRDAKLSLIFVVVLPL 161
Cdd:cd18780 82 FSAI---IAQEiafFDVTRTGELLNRLSSDTQVLQNAvtvnLSMLLRYLVQI----IGGLVFMFTTSWKLTLVMLSVVPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 162 LLLLVVILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMML 241
Cdd:cd18780 155 LSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 242 LMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRA-GASA 299
Cdd:cd18780 235 AAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAvGASV 293
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
332-554 |
1.43e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 332 VTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKING----------IDVREMDQSSLR 401
Cdd:PRK10261 20 IAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 402 Q----KIGLVPQKAV-----LFT--GTIASNMR----YGKEDATDE--EIWEALRTAQAENFVSKLANGLgsrveqggnn 464
Cdd:PRK10261 100 HvrgaDMAMIFQEPMtslnpVFTvgEQIAESIRlhqgASREEAMVEakRMLDQVRIPEAQTILSRYPHQL---------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 465 fSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDA---KLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIA 541
Cdd:PRK10261 170 -SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAqilQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250
....*....|...
gi 1251574723 542 GMGTHEELKESNQ 554
Cdd:PRK10261 249 ETGSVEQIFHAPQ 261
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
327-542 |
2.42e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.74 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKpVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSS---LRQK 403
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 IGLVPQKA-VLFTGTIASN--MRYGKEDATDEEIWEalRTAQAENFVsklanGLGSRVEQGGNNFSGGQKQRLSIARSLI 480
Cdd:PRK10908 81 IGMIFQDHhLLMDRTVYDNvaIPLIIAGASGDDIRR--RVSAALDKV-----GLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 481 RKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNSD--QIIVMNEGKIAG 542
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRsyRMLTLSDGHLHG 217
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1-312 |
2.48e-11 |
|
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: 65.17 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 1 MKRLKPYWL-----SITAVLV--------LTFGQVIGQLYLPtlmsniidkgvvtgDTDYIWSTGMK----MLLISFASV 63
Cdd:cd18578 1 LKLNKPEWPllllgLIGAIIAgavfpvfaILFSKLISVFSLP--------------DDDELRSEANFwalmFLVLAIVAG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 64 ILSVIVVYLASRISMGFGKELRDKIFTKVedfSLQE---FDKVG--TSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLL 138
Cdd:cd18578 67 IAYFLQGYLFGIAGERLTRRLRKLAFRAI---LRQDiawFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 139 GGIIMAVGRDAKLSLIFVVvlplllllvvilggkAMPMF---------------KSLQKKMDKLNRVIREGLTGIRVVRS 203
Cdd:cd18578 144 AGLIIAFVYGWKLALVGLA---------------TVPLLllagylrmrllsgfeEKNKKAYEESSKIASEAVSNIRTVAS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 204 FNRNEDELEKFEEANADYATTAIKvnrllslmsplmmlLMNLTSIA--------------IVWIGSIFIGNGDMQVGDLM 269
Cdd:cd18578 209 LTLEDYFLEKYEEALEEPLKKGLR--------------RALISGLGfglsqsltffayalAFWYGGRLVANGEYTFEQFF 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1251574723 270 -AFiqyaMQIMMSFMMLSAVFIMIP---RAGASAERINEVLDMNAEI 312
Cdd:cd18578 275 iVF----MALIFGAQSAGQAFSFAPdiaKAKAAAARIFRLLDRKPEI 317
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
340-496 |
6.93e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 340 EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQ--KIGLVPQ-KAVLftg 416
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllYLGHQPGiKTEL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 417 TIASNMRY---GKEDATDEEIWEALRTAqaenfvsklanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFS 493
Cdd:PRK13538 90 TALENLRFyqrLHGPGDDEALWEALAQV-----------GLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
...
gi 1251574723 494 ALD 496
Cdd:PRK13538 159 AID 161
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
327-540 |
7.05e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.02 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYeGAEKPvIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKING-----IDVREMDQSS-- 399
Cdd:PRK11701 7 LSVRGLTKLY-GPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAErr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 400 --LRQKIGLVPQKA-------VLFTGTI-----ASNMR-YGKedatdeeiweaLRtAQAENFVSKLANGLgSRVEQGGNN 464
Cdd:PRK11701 85 rlLRTEWGFVHQHPrdglrmqVSAGGNIgerlmAVGARhYGD-----------IR-ATAGDWLERVEIDA-ARIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 465 FSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEA------VT--LIVAQRItsvvnSDQIIVMN 536
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglavviVThdLAVARLL-----AHRLLVMK 226
|
....
gi 1251574723 537 EGKI 540
Cdd:PRK11701 227 QGRV 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
327-496 |
8.16e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKingidvremDQSSLRqkIGL 406
Cdd:PRK09544 5 VSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR--IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLFTG---TIASNMRYgKEDATDEEIWEALRTAQAENFvsklanglgsrVEQGGNNFSGGQKQRLSIARSLIRKP 483
Cdd:PRK09544 72 VPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHL-----------IDAPMQKLSGGETQRVLLARALLNRP 139
|
170
....*....|...
gi 1251574723 484 EIYIFDDSFSALD 496
Cdd:PRK09544 140 QLLVLDEPTQGVD 152
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
344-547 |
8.23e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.98 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 344 IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLrqkIGLVPQK-------AVLFTG 416
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 417 TIASNmRYG------KEDATDEEIW-EALRTAQAENFvsklanglgsRVEQGGNnFSGGQKQRLSIARSLIRKPEIYIFD 489
Cdd:PRK15056 100 VVMMG-RYGhmgwlrRAKKRDRQIVtAALARVDMVEF----------RHRQIGE-LSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 490 DSFSALDFKTDAKLREALKAETTEAVTLIVA-QRITSVVNSDQIIVMNEGKIAGMGTHE 547
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEGKTMLVStHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
327-539 |
1.14e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEH--VTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKST-------LINMIPRFYdvESGVVKINGIDVREMDQ 397
Cdd:PRK15134 6 LAIENlsVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVtalsilrLLPSPPVVY--PSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 398 SSLRQ----KIGLVPQKAV-----LFT-----GTIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANglgsrveqGGN 463
Cdd:PRK15134 84 QTLRGvrgnKIAMIFQEPMvslnpLHTlekqlYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTD--------YPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 464 NFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAK----LREaLKAETTEAVTLIVAQriTSVVN--SDQIIVMNE 537
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQilqlLRE-LQQELNMGLLFITHN--LSIVRklADRVAVMQN 232
|
..
gi 1251574723 538 GK 539
Cdd:PRK15134 233 GR 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
336-550 |
1.67e-10 |
|
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: 64.26 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 336 YEGAEKPVIE--DITFEANagETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVrEMDQSSLRQKIGLVPQKAVL 413
Cdd:TIGR01257 938 FEPSGRPAVDrlNITFYEN--QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 414 FTG-TIASNMRYGKEdaTDEEIWEalrTAQAENFVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSF 492
Cdd:TIGR01257 1015 FHHlTVAEHILFYAQ--LKGRSWE---EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 493 SALDFKTDAKLRE-ALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELK 550
Cdd:TIGR01257 1090 SGVDPYSRRSIWDlLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLK 1148
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
11-302 |
4.16e-10 |
|
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: 60.95 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGQVIGQLYlpTLMSNIIDKGVVTGDtdyIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIFT 90
Cdd:cd18577 14 ALPLMTIVFGDLFDAFT--DFGSGESSPDEFLDD---VNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 91 KVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVILG 170
Cdd:cd18577 89 ALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 171 GKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAI 250
Cdd:cd18577 169 KLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALA 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 251 VWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18577 249 FWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
292-549 |
5.76e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 61.74 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 292 IPRAGASAERINEVLDMNAEILNPENPKTSTPPAKLsfEHVTFRYEGAEKPVI---EDITFEANAGETIAIIGSTGAGKS 368
Cdd:TIGR03269 247 IKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKV--RNVSKRYISVDRGVVkavDNVSLEVKEGEIFGIVGTSGAGKT 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 369 TLINMIPRFYDVESGVVKIN-GIDVREMDQSS-------------LRQKIGLVPQKAVLFTGTIASNMRYGKEDATDEEI 434
Cdd:TIGR03269 325 TLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGpdgrgrakryigiLHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 435 WeALRTA-----QAENFVSKLANGLgsrveqggnnfSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREA-LK 508
Cdd:TIGR03269 405 I-TLKMVgfdeeKAEEILDKYPDEL-----------SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSiLK 472
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1251574723 509 A-ETTEAVTLIVAQRITSVVN-SDQIIVMNEGKIAGMGTHEEL 549
Cdd:TIGR03269 473 ArEEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEI 515
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
340-553 |
6.51e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.16 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 340 EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSL---RQKIGLVPQKAVLFTG 416
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 417 -TIASNMRYGKEDATD--EEIweaLRTAqaenFVSKL-ANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSF 492
Cdd:PRK11831 99 mNVFDNVAYPLREHTQlpAPL---LHST----VMMKLeAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251574723 493 SALDFKTDAKLREaLKAETTEA--VTLIVAQRITSVVNS--DQIIVMNEGKIAGMGTHEELKESN 553
Cdd:PRK11831 172 VGQDPITMGVLVK-LISELNSAlgVTCVVVSHDVPEVLSiaDHAYIVADKKIVAHGSAQALQANP 235
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
331-549 |
6.74e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.89 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 331 HVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKS----TLINMIPRFYDVeSGVVKING---IDVREMDQSSLRQK 403
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRI-GGSATFNGreiLNLPEKELNKLRAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 404 iglvpQKAVLFTGTIAS-N--MR--------------YGKEDATDEEI--WEALRTAQAENfvsklanglgsRVEQGGNN 464
Cdd:PRK09473 98 -----QISMIFQDPMTSlNpyMRvgeqlmevlmlhkgMSKAEAFEESVrmLDAVKMPEARK-----------RMKMYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 465 FSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAK---LREALKAETTEAVTLIVAQriTSVVNS--DQIIVMNEGK 539
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQimtLLNELKREFNTAIIMITHD--LGVVAGicDKVLVMYAGR 239
|
250
....*....|
gi 1251574723 540 IAGMGTHEEL 549
Cdd:PRK09473 240 TMEYGNARDV 249
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
325-505 |
7.32e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.51 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 325 AKLSFEHVTFRYegAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMI---PRfydVESGVVKINGIDVREMDQSS-L 400
Cdd:PRK11614 4 VMLSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLcgdPR---ATSGRIVFDGKDITDWQTAKiM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 401 RQKIGLVPQKAVLFTG-TIASNMRYGKEDATDEEIWEALRTaqaenfVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSL 479
Cdd:PRK11614 79 REAVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKW------VYELFPRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190
....*....|....*....|....*....|...
gi 1251574723 480 IRKPEIYIFDDSFSALD-------FKTDAKLRE 505
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLApiiiqqiFDTIEQLRE 185
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
340-539 |
7.88e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.82 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 340 EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVES--GVVKINGidvREMDQSSLRqKIGLVPQKAVLF--- 414
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN---RKPTKQILK-RTGFVTQDDILYphl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 415 ----TGTIASNMRYGKEDATDEeiwealRTAQAENFVSKLanGLgSRVEQG--GNNF----SGGQKQRLSIARSLIRKPE 484
Cdd:PLN03211 156 tvreTLVFCSLLRLPKSLTKQE------KILVAESVISEL--GL-TKCENTiiGNSFirgiSGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 485 IYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVA-QRITSVVNS--DQIIVMNEGK 539
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSSRVYQmfDSVLVLSEGR 284
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
346-559 |
1.04e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.64 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 346 DITFEANagETIAIIGSTGAGKSTLINMIPRFYDVESG-------VVKINGIDVREMDQssLRQKIGLVPQ--KAVLFTG 416
Cdd:PRK13645 31 SLTFKKN--KVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKEVKR--LRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 417 TIASNMRYGKED--ATDEEIWEALRTaqaenfVSKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSA 494
Cdd:PRK13645 107 TIEKDIAFGPVNlgENKQEAYKKVPE------LLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 495 LDFKTDA---KLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKESNQIYQEI 559
Cdd:PRK13645 181 LDPKGEEdfiNLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKI 248
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
326-549 |
1.18e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.14 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSfehVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKST-------LINMIPRfydVESGVVKINGIDVREMDQS 398
Cdd:PRK11022 8 KLS---VHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVsslaimgLIDYPGR---VMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 399 SLRQKIGlvPQKAVLFTGTIAS-NMRYgkedATDEEIWEALRTAQAENFVSK------LANGLG-----SRVEQGGNNFS 466
Cdd:PRK11022 82 ERRNLVG--AEVAMIFQDPMTSlNPCY----TVGFQIMEAIKVHQGGNKKTRrqraidLLNQVGipdpaSRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 467 GGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREAL-KAETTEAVTLIVAQRITSVV--NSDQIIVMNEGKIAGM 543
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLlELQQKENMALVLITHDLALVaeAAHKIIVMYAGQVVET 235
|
....*.
gi 1251574723 544 GTHEEL 549
Cdd:PRK11022 236 GKAHDI 241
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
319-556 |
2.15e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.65 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 319 KTSTPPAKLSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQS 398
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 399 SLRQKIGLVPQKAVLFTGTIASNM-------------RYGKEDAtdEEIWEALRTAQAENFVSKLANGLgsrveqggnnf 465
Cdd:PRK10575 82 AFARKVAYLPQQLPAAEGMTVRELvaigrypwhgalgRFGAADR--EKVEEAISLVGLKPLAHRLVDSL----------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 466 SGGQKQRLSIARSLIRKPEIYIFDDSFSALDFktdaklreALKAETTEAVTLIVAQRITSVVN-----------SDQIIV 534
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDI--------AHQVDVLALVHRLSQERGLTVIAvlhdinmaaryCDYLVA 220
|
250 260
....*....|....*....|....*
gi 1251574723 535 MNEGKIAGMGTHEELKES---NQIY 556
Cdd:PRK10575 221 LRGGEMIAQGTPAELMRGetlEQIY 245
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
11-302 |
3.56e-09 |
|
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: 58.23 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFGqVIGQLYLPTLMSNIIdkgvVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIFT 90
Cdd:cd18570 9 LLSLLITLLG-IAGSFFFQILIDDII----PSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 91 KVEDFSLQEFDKVGTSSLITRTtNDVVQIQNVL-YMMMRLMVMAPIMLLGGIIMAvgrdaKLSLIFVVVLPLLLLLVVIL 169
Cdd:cd18570 84 HLLKLPLSFFETRKTGEIISRF-NDANKIREAIsSTTISLFLDLLMVIISGIILF-----FYNWKLFLITLLIIPLYILI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 170 GGKAMPMFKSLQKKM----DKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNL 245
Cdd:cd18570 158 ILLFNKPFKKKNREVmesnAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 246 TSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18570 238 GSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
344-542 |
4.04e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.07 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 344 IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVE-SGVVKING--IDVREMDQSsLRQKI----------GLVPQK 410
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQA-IRAGIamvpedrkrhGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 411 AVLFTGTIASNMRYGKEDATDEE-----IWEALRTAQAENFVSKLANGlgsrveqggnNFSGGQKQRLSIARSLIRKPEI 485
Cdd:TIGR02633 355 GVGKNITLSVLKSFCFKMRIDAAaelqiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 486 YIFDDSFSALDFKTDAKLREALKAETTEAVTLIV-AQRITSVVN-SDQIIVMNEGKIAG 542
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVvSSELAEVLGlSDRVLVIGEGKLKG 483
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
14-302 |
5.78e-09 |
|
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: 57.55 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 14 VLVLTFGQVIGQLYLPTLMS---NIIDKGVVTGDTDYI---WSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDK 87
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGdlvNVISRSLKETNGDFIedlKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 88 IFTKVEDFSLQEFDKVGTSSLITRTTNDV------------------VQIQNV---LYMM-----MRLMVMAPIMLLGGI 141
Cdd:cd18574 81 LFSSLLRQDIAFFDTHRTGELVNRLTADVqefkssfkqcvsqglrsvTQTVGCvvsLYLIspkltLLLLVIVPVVVLVGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 142 IMAVG-RdaKLSlifvvvlplllllvvilggkampmfKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANAD 220
Cdd:cd18574 161 LYGSFlR--KLS-------------------------RRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 221 YATTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAE 300
Cdd:cd18574 214 AAKLNEKLGLGIGIFQGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGA 293
|
..
gi 1251574723 301 RI 302
Cdd:cd18574 294 RV 295
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
22-300 |
7.07e-09 |
|
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: 57.35 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 22 VIGQLYLPTLMSNIIDkgVVTGDTDyiwstgmkmlLISFASVILSVIVVYLASRISMG------------FGKELRDKIF 89
Cdd:cd18590 9 VICETFIPYYTGRVID--ILGGEYQ----------HNAFTSAIGLMCLFSLGSSLSAGlrgglfmctlsrLNLRLRHQLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 90 TKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVIL 169
Cdd:cd18590 77 SSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 170 GGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIA 249
Cdd:cd18590 157 NTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 250 IVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVF-IMIPRAGASAE 300
Cdd:cd18590 237 MLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYgDMLSNVGAAAK 288
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
340-551 |
7.35e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.72 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 340 EKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIP--RFYDVESGVVKINGIDVREMD-QSSLRQKIGLVPQKAV---- 412
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVeipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 413 ----LFTGTIASNMR-YGKEDATDEEIWEALRTAQAEnFVSKLANGLGSRVEQGgnnFSGGQKQRLSIARSLIRKPEIYI 487
Cdd:PRK09580 93 vsnqFFLQTALNAVRsYRGQEPLDRFDFQDLMEEKIA-LLKMPEDLLTRSVNVG---FSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 488 FDDSFSALD---FKTDAKLREALKAETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAGMGTHEELKE 551
Cdd:PRK09580 169 LDESDSGLDidaLKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQ 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
343-553 |
8.85e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.02 E-value: 8.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 343 VIEDITFEANAGETIAIIGSTGAGKSTLIN-----MIP----------------RFYDVESGVVKIN--GIDVREMDQ-S 398
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnalLLPdtgtiewifkdeknkkKTKEKEKVLEKLViqKTRFKKIKKiK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 399 SLRQKIGLVPQKA--VLFTGTIASNMRYGKED-ATDEEiwEALRTAQAenfVSKLANGLGSRVEQGGNNFSGGQKQRLSI 475
Cdd:PRK13651 102 EIRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSmGVSKE--EAKKRAAK---YIELVGLDESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 476 ARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLI-VAQRITSVVN-SDQIIVMNEGKIAGMG-THEELKES 552
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIIlVTHDLDNVLEwTKRTIFFKDGKIIKDGdTYDILSDN 256
|
.
gi 1251574723 553 N 553
Cdd:PRK13651 257 K 257
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
317-567 |
1.10e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 317 NPKTSTPPAKLSFE--HVTFRYEGAekpvIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVR- 393
Cdd:PRK09700 254 KENVSNLAHETVFEvrNVTSRDRKK----VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISp 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 394 --EMDqsSLRQKIGLVPQK----AVLFTGTIASNMRYGK--EDATDEEIW------EALRTAQAENfvsKLANGLGSRVE 459
Cdd:PRK09700 330 rsPLD--AVKKGMAYITESrrdnGFFPNFSIAQNMAISRslKDGGYKGAMglfhevDEQRTAENQR---ELLALKCHSVN 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 460 QGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQ----RITSVVnsDQIIVM 535
Cdd:PRK09700 405 QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSselpEIITVC--DRIAVF 482
|
250 260 270
....*....|....*....|....*....|...
gi 1251574723 536 NEGKIAGMGTH-EELKEsnqiyQEIMRSQLSEE 567
Cdd:PRK09700 483 CEGRLTQILTNrDDMSE-----EEIMAWALPQE 510
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
334-551 |
1.22e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.63 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 334 FRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMI-----PrfydvESGVVKINGIDVREmDQSSLRQKIGLV- 407
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtgilvP-----TSGEVRVLGYVPFK-RRKEFARRIGVVf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 408 PQKAVLftgtiasnmrygkedatdeeIW-----EALR---------TAQAENFVSKLAN--GLGSRVEQGGNNFSGGQKQ 471
Cdd:COG4586 102 GQRSQL--------------------WWdlpaiDSFRllkaiyripDAEYKKRLDELVEllDLGELLDTPVRQLSLGQRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 472 RLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEA-VTLIVA----QRITSVvnSDQIIVMNEGKIAGMGTH 546
Cdd:COG4586 162 RCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTshdmDDIEAL--CDRVIVIDHGRIIYDGSL 239
|
....*
gi 1251574723 547 EELKE 551
Cdd:COG4586 240 EELKE 244
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
35-302 |
1.28e-08 |
|
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: 56.81 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 35 IIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIFTKVEDFSLQEFDKVGTSSLITRTTN 114
Cdd:cd18565 40 VPASLGPADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 115 DVVQIQNVLYMMMRLMVMAPIMLLG-GIIMAVgRDAKLSLIFVVVLPLLLLLVVILGGKAMPMFKSLQKKMDKLNRVIRE 193
Cdd:cd18565 120 DVNQLERFLDDGANSIIRVVVTVLGiGAILFY-LNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLEN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 194 GLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIGSIFIGNG------DMQVGD 267
Cdd:cd18565 199 NLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGT 278
|
250 260 270
....*....|....*....|....*....|....*
gi 1251574723 268 LMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18565 279 LVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
313-569 |
1.31e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.34 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 313 LNPENPKTSTPPAKLSFEHVTFRyEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDV 392
Cdd:COG3845 244 LRVEKAPAEPGEVVLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 393 -----REMDQSSL------RQKIGLVPqkavlfTGTIASNM---RYGKEDATDeeiWEALRTAQAENFVSKL-------A 451
Cdd:COG3845 323 tglspRERRRLGVayipedRLGRGLVP------DMSVAENLilgRYRRPPFSR---GGFLDRKAIRAFAEELieefdvrT 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 452 NGLGSRVEqggnNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTE--AVTLIVA--QRITSVv 527
Cdd:COG3845 394 PGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgaAVLLISEdlDEILAL- 468
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1251574723 528 nSDQIIVMNEGKIAGmgtheelkesnqiyqEIMRSQLSEEEI 569
Cdd:COG3845 469 -SDRIAVMYEGRIVG---------------EVPAAEATREEI 494
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
14-271 |
1.36e-08 |
|
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: 56.45 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 14 VLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIFTKVE 93
Cdd:cd18782 7 VLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 94 DFSLQEFDKVGTSSLITR-----------TTNDVVQIQNVLYMMMRLMVMAPI-MLLGGIIMAVgrdaklslifvvvlpl 161
Cdd:cd18782 87 RLPLGFFDKRPVGELSTRiseldtirgflTGTALTTLLDVLFSVIYIAVLFSYsPLLTLVVLAT---------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 162 llllvvilggkaMPMF--------KSLQKKMDKLN--------RVIrEGLTGIRVVRSFNRNEDELEKFEEANADYATTA 225
Cdd:cd18782 151 ------------VPLQllltflfgPILRRQIRRRAeasaktqsYLV-ESLTGIQTVKAQNAELKARWRWQNRYARSLGEG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1251574723 226 IKVNRLLSLMSPLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAF 271
Cdd:cd18782 218 FKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAF 263
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
321-549 |
1.51e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 321 STPPAKLSFEHVTFRYEGAekPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSL 400
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGV--EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 401 RQ-KIGLVPQKAVLFTG-TIASNMRYGKEdatdeeiwealRTAQAENFVSKLANGLGSRVE---QGGnNFSGGQKQRLSI 475
Cdd:PRK15439 84 HQlGIYLVPQEPLLFPNlSVKENILFGLP-----------KRQASMQKMKQLLAALGCQLDldsSAG-SLEVADRQIVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 476 ARSLIRKPEIYIFDDSFSALD-FKTDA---KLREALKaettEAVTLI-VAQRITSVVN-SDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTpAETERlfsRIRELLA----QGVGIVfISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
14-302 |
1.56e-08 |
|
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: 56.33 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 14 VLVLTFGQVIGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILS----VIVVYLASRISmgfgKELRDKIF 89
Cdd:cd18589 1 VLGLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEfvcdLIYNITMSRIH----SRLQGLVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 90 TKVEDFSLQEFDKVGT---SSLITRTTNDVVQI--QNVLYMM---MRLMVMAPIMLLGGIimavgrdaKLSLIFVVVLPL 161
Cdd:cd18589 77 AAVLRQEIAFFDSNQTgdiVSRVTTDTEDMSESlsENLSLLMwylARGLFLFIFMLWLSP--------KLALLTALGLPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 162 LLLLVVILGGKAMPMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATtaikVNRLLSLMSPLMML 241
Cdd:cd18589 149 LLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYR----LNKKEAAAYAVSMW 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251574723 242 LMNLTSIA----IVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18589 225 TSSFSGLAlkvgILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
327-550 |
1.83e-08 |
|
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: 57.72 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVReMDQSSLRQKIGL 406
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 407 VPQKAVLftgtiaSNMRYGKEDATdeeIWEALRTAQAENfVSKLAN------GLGSRVEQGGNNFSGGQKQRLSIARSLI 480
Cdd:TIGR01257 2017 CPQFDAI------DDLLTGREHLY---LYARLRGVPAEE-IEKVANwsiqslGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 481 RKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNS--DQIIVMNEGKIAGMGTHEELK 550
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAlcTRLAIMVKGAFQCLGTIQHLK 2158
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
7-302 |
2.31e-08 |
|
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: 55.64 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 7 YWLSITAVLVltfgQVIGqLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRD 86
Cdd:cd18568 5 AEILLASLLL----QLLG-LALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 87 KIFTKVEDFSLQEFDKVGTSSLITR-TTNDVVQI---QNVLYMMMRLMvMAPIMLlggIIMAVgRDAKLSLIFVVVLPLL 162
Cdd:cd18568 80 DFYKHLLSLPLSFFASRKVGDIITRfQENQKIRRfltRSALTTILDLL-MVFIYL---GLMFY-YNLQLTLIVLAFIPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 163 LLLVVIlggkAMPMFKSLQKKM----DKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPL 238
Cdd:cd18568 155 VLLTLL----SSPKLKRNSREIfqanAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLI 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 239 MMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18568 231 SSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
342-548 |
5.04e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 342 PVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMD-QSSLRQKI----------GLVPQK 410
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIvyisedrkrdGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 411 AVLFTGTIASnMRY-----GKEDATDEEIwealrtaQAENFVsKLANGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEI 485
Cdd:PRK10762 346 SVKENMSLTA-LRYfsragGSLKHADEQQ-------AVSDFI-RLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251574723 486 YIFDDSFSALDF---KTDAKLREALKAETTEAVtlIVAQRITSVVN-SDQIIVMNEGKIAGMGTHEE 548
Cdd:PRK10762 417 LILDEPTRGVDVgakKEIYQLINQFKAEGLSII--LVSSEMPEVLGmSDRILVMHEGRISGEFTREQ 481
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
343-508 |
5.38e-08 |
|
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: 55.91 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 343 VIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvremdqsslRQKIGLVPQKAVLFTGTIASNM 422
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 423 RY--GKED-----ATDEEIWEALRTAQAENFVSKlaNGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSAL 495
Cdd:TIGR00954 536 IYpdSSEDmkrrgLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170
....*....|...
gi 1251574723 496 DFKTDAKLREALK 508
Cdd:TIGR00954 614 SVDVEGYMYRLCR 626
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
334-549 |
5.51e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.24 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 334 FRYEgaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKING--IDVREMDQSSLRQKIGLV---P 408
Cdd:PRK13638 9 FRYQ--DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVfqdP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 409 QKAVLFT---GTIASNMR-YG-KEDATDEEIWEALRTAQAENFVsklanglgsrvEQGGNNFSGGQKQRLSIARSLIRKP 483
Cdd:PRK13638 87 EQQIFYTdidSDIAFSLRnLGvPEAEITRRVDEALTLVDAQHFR-----------HQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 484 EIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVN--SDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYeiSDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
333-561 |
7.26e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.86 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 333 TFRYEGAEKPVieDITFEAnaGETIAIIGSTGAGKSTLI----NMIPRFYDVESGV------VKINGIDVREMDQSslRQ 402
Cdd:PRK09984 13 TFNQHQALHAV--DLNIHH--GEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIellgrtVQREGRLARDIRKS--RA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 403 KIGLVPQKAVLFTG-TIASNMRYGKEDATdeEIWEA----LRTAQAENFVSKLAN-GLGSRVEQGGNNFSGGQKQRLSIA 476
Cdd:PRK09984 87 NTGYIFQQFNLVNRlSVLENVLIGALGST--PFWRTcfswFTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 477 RSLIRKPEIYIFDDSFSALDFKTDAKLREALK-AETTEAVTLIVA--QRITSVVNSDQIIVMNEGKI--AGMGTHEELKE 551
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRdINQNDGITVVVTlhQVDYALRYCERIVALRQGHVfyDGSSQQFDNER 244
|
250
....*....|
gi 1251574723 552 SNQIYQEIMR 561
Cdd:PRK09984 245 FDHLYRSINR 254
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
318-496 |
8.89e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 318 PKTSTPPAkLSFEHVTFRYEgaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQ 397
Cdd:PRK13543 4 PLHTAPPL-LAAHALAFSRN--EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 398 SSLRQKIGLVPQ-KAVLFTgtiASNMRY-----GKedatdeeiwEALRTAQAENFVSKLANGLGSRVEQggnnFSGGQKQ 471
Cdd:PRK13543 81 SRFMAYLGHLPGlKADLST---LENLHFlcglhGR---------RAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKK 144
|
170 180
....*....|....*....|....*
gi 1251574723 472 RLSIARSLIRKPEIYIFDDSFSALD 496
Cdd:PRK13543 145 RLALARLWLSPAPLWLLDEPYANLD 169
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
324-551 |
1.62e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 324 PAKLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIP----RFYDVESGVVKINGIDVREMdqss 399
Cdd:TIGR00956 57 ILTRGFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEI---- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 400 LRQKIGLV----------PQKAVLFTGTIASNMR--YGKEDATDEEIWEALRTAqaenfVSKLANGLG-SRVEQGGNNF- 465
Cdd:TIGR00956 133 KKHYRGDVvynaetdvhfPHLTVGETLDFAARCKtpQNRPDGVSREEYAKHIAD-----VYMATYGLShTRNTKVGNDFv 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 466 ---SGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKA-----ETTEAVTLI-VAQRITSVVnsDQIIVMN 536
Cdd:TIGR00956 208 rgvSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTsanilDTTPLVAIYqCSQDAYELF--DKVIVLY 285
|
250
....*....|....*
gi 1251574723 537 EGKIAGMGTHEELKE 551
Cdd:TIGR00956 286 EGYQIYFGPADKAKQ 300
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
324-551 |
2.10e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 324 PAKLSFEHVTFRYEGAEkpVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvREMDQSSLR-- 401
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTTaa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 402 ---------QKIGLVPQKAV---LFTGTIASnmRYGkedatdeeiWEALRTAQAEnfVSKLANGLGSRV--EQGGNNFSG 467
Cdd:PRK11288 77 laagvaiiyQELHLVPEMTVaenLYLGQLPH--KGG---------IVNRRLLNYE--AREQLEHLGVDIdpDTPLKYLSI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 468 GQKQRLSIARSLIRKPEIYIFDD---SFSALDFKTDAKLREALKAETTeaVTLIVAQRITSVVN-SDQIIVMNEGKIAgm 543
Cdd:PRK11288 144 GQRQMVEIAKALARNARVIAFDEptsSLSAREIEQLFRVIRELRAEGR--VILYVSHRMEEIFAlCDAITVFKDGRYV-- 219
|
....*...
gi 1251574723 544 GTHEELKE 551
Cdd:PRK11288 220 ATFDDMAQ 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
315-490 |
2.97e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 315 PENPKTSTPPA--KLSFEHVTFRYEG---AEKPVieDITFEAnaGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKING 389
Cdd:PRK10522 309 AEFPRPQAFPDwqTLELRNVTFAYQDngfSVGPI--NLTIKR--GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 390 IDVREMDQSSLRQKIGLVPQKAVLFTGTIasnmryGKEDatdeeiwEALRTAQAENFVSKLanGLGSRVEQGGN-----N 464
Cdd:PRK10522 385 KPVTAEQPEDYRKLFSAVFTDFHLFDQLL------GPEG-------KPANPALVEKWLERL--KMAHKLELEDGrisnlK 449
|
170 180
....*....|....*....|....*.
gi 1251574723 465 FSGGQKQRLSIARSLIRKPEIYIFDD 490
Cdd:PRK10522 450 LSKGQKKRLALLLALAEERDILLLDE 475
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
350-534 |
3.33e-07 |
|
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: 53.25 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 350 EANAGETIAIIGSTGAGKSTLINMIprfydveSGVVKINGIDVREmdqsslRQKIGLVPQkavlftgtiasnmrYGKEDa 429
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVDE------DLKISYKPQ--------------YISPD- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 430 TDEEIWEALRTAQAENFVSKLAN-------GLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAK 502
Cdd:COG1245 414 YDGTVEEFLRSANTDDFGSSYYKteiikplGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
170 180 190
....*....|....*....|....*....|....*.
gi 1251574723 503 LREALK--AETTEAVTLIVAQRITsVVN--SDQIIV 534
Cdd:COG1245 494 VAKAIRrfAENRGKTAMVVDHDIY-LIDyiSDRLMV 528
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
23-302 |
3.51e-07 |
|
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: 51.93 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 23 IGQLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVI--------LSVIVVYLASRIsmgfgkelRDKIFTKVED 94
Cdd:cd18784 10 VGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVaagirgglFTLAMARLNIRI--------RNLLFRSIVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 95 FSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSLIFVVVLPLLLLLVVILGGKAM 174
Cdd:cd18784 82 QEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 175 PMFKSLQKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIG 254
Cdd:cd18784 162 KLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1251574723 255 SIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18784 242 GHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
334-496 |
3.97e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 334 FRYEgaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREmDQSSLRQKIGLVPQKavl 413
Cdd:PRK13540 9 FDYH--DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 414 fTG-----TIASNMRYG-KEDATDEEIWEALRTAQAENFVSkLANGLgsrveqggnnFSGGQKQRLSIARSLIRKPEIYI 487
Cdd:PRK13540 83 -SGinpylTLRENCLYDiHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWL 150
|
....*....
gi 1251574723 488 FDDSFSALD 496
Cdd:PRK13540 151 LDEPLVALD 159
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
322-528 |
4.61e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.73 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 322 TPPAKLSFEHVTFRYEGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFY--DVESGVVKINGIDvremdqss 399
Cdd:COG2401 24 SERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 400 lrqkiglVPQKAVLFTgtiasnmRYGKEDATDEEIwEALRTA---QAENFVSKLAnglgsrveqggnNFSGGQKQRLSIA 476
Cdd:COG2401 96 -------FGREASLID-------AIGRKGDFKDAV-ELLNAVglsDAVLWLRRFK------------ELSTGQKFRFRLA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1251574723 477 RSLIRKPEIYIFDDSFSALDFKTdAKL--REALKAETTEAVTLIVAQRITSVVN 528
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQT-AKRvaRNLQKLARRAGITLVVATHHYDVID 201
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
327-545 |
7.06e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.98 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVT-FRYEGAekpVIEDITFEANAGETIAIIGSTGAGKSTLINMI---------PRFYDVeSGVVKINGIDVREMD 396
Cdd:PRK13547 2 LTADHLHvARRHRA---ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgggaPRGARV-TGDVTLNGEPLAAID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 397 QSSLRQKIGLVPQKA----------VLFTGTIASNMRYGKEDATDEEI-WEALRTAQAENFVSKLANGLgsrveqggnnf 465
Cdd:PRK13547 78 APRLARLRAVLPQAAqpafafsareIVLLGRYPHARRAGALTHRDGEIaWQALALAGATALVGRDVTTL----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 466 SGGQKQRLSIARSL---------IRKPEIYIFDDSFSALDFKTDAKLREALKAETTE---AVTLIVAQRITSVVNSDQII 533
Cdd:PRK13547 147 SGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnlGVLAIVHDPNLAARHADRIA 226
|
250
....*....|..
gi 1251574723 534 VMNEGKIAGMGT 545
Cdd:PRK13547 227 MLADGAIVAHGA 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
344-495 |
7.53e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 344 IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQS-SLRQKIGLVPQK-AVLFTGTIASN 421
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 422 MRYGKE--------DATDeeiWEALRTaQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFS 493
Cdd:PRK09700 101 LYIGRHltkkvcgvNIID---WREMRV-RAAMMLLRV--GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
..
gi 1251574723 494 AL 495
Cdd:PRK09700 175 SL 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
327-507 |
7.54e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.86 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEgaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKI-NGIDVREMDQSslrqKIG 405
Cdd:TIGR03719 323 IEAENLTKAFG--DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQS----RDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 406 LVPQKAVLftgtiasnmrygkedatdEEIWEALRTAQAENFVsklangLGSRVEQGGNNF------------SGGQKQRL 473
Cdd:TIGR03719 397 LDPNKTVW------------------EEISGGLDIIKLGKRE------IPSRAYVGRFNFkgsdqqkkvgqlSGGERNRV 452
|
170 180 190
....*....|....*....|....*....|....
gi 1251574723 474 SIARSLIRKPEIYIFDDSFSALDFKTDAKLREAL 507
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL 486
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
8-279 |
1.91e-06 |
|
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: 49.89 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 8 WLSITAVLVLTFGQVIGqLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDK 87
Cdd:cd18566 2 PLLPQVLLASLFINILA-LATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 88 IFTKVEDFSLQEFDKVGTSSLITRTtNDVVQIQNVLYMMMRLMVM-AP--------IMLLGGIIMAVgrdaklslifvvv 158
Cdd:cd18566 81 AFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLdLPfvliflglIWYLGGKLVLV------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 159 lplLLLLVVILGGKAMPMFKSLQKKMDKLNR-------VIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRL 231
Cdd:cd18566 147 ---PLVLLGLFVLVAILLGPILRRALKERSRaderrqnFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKI 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 232 LSLMSPLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAF----------IQYAMQIM 279
Cdd:cd18566 224 NAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIACtmlsgrvlqpLQRAFGLW 281
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
11-302 |
2.47e-06 |
|
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: 49.43 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 11 ITAVLVLTFG-QVIGqLYLPTLMSNIIDKGVVTGDTDYIWSTGMKMLLISFASVILSVIVVYLASRISMGFGKELRDKIF 89
Cdd:cd18555 4 LISILLLSLLlQLLT-LLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 90 TKVEDFSLQEFDKVGTSSLITRTtNDVVQIQNVL-------------------YMMMRLMVMAPIMLLGGIIMAVgrdak 150
Cdd:cd18555 83 EHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILsnqvisliidllllviyliYMLYYSPLLTLIVLLLGLLIVL----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 151 LSLIfvvvlplllllvvilggkAMPMFKSLQKK----MDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAI 226
Cdd:cd18555 157 LLLL------------------TRKKIKKLNQEeivaQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFK 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 227 KVNRLLSLMSPLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAMQIMMSFMMLSAVFIMIPRAGASAERI 302
Cdd:cd18555 219 KKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
347-480 |
2.95e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 48.68 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 347 ITFEANAGETIAIIGSTGAGKSTLINMIPRFYDvESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLftgtiASNMR--- 423
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLSQQQSP-----PFAMPvfq 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 424 Y---GKEDATDEEIWEALRTAQAENFvsKLANGLGSRVEQggnnFSGGQKQRLSIARSLI 480
Cdd:COG4138 89 YlalHQPAGASSEAVEQLLAQLAEAL--GLEDKLSRPLTQ----LSGGEWQRVRLAAVLL 142
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
318-561 |
5.34e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 318 PKTSTP-PAKLSFEHVTfryeGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGidvREMD 396
Cdd:PRK10982 241 DKENKPgEVILEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG---KKIN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 397 QSSL--------------RQKIGLVPQKAVLFTGTIaSNMRYGKEDatdeeiWEALRTAQAENFVSKLANGLgsRVEQGG 462
Cdd:PRK10982 314 NHNAneainhgfalvteeRRSTGIYAYLDIGFNSLI-SNIRNYKNK------VGLLDNSRMKSDTQWVIDSM--RVKTPG 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 463 N-----NFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALK--AETTEAVTLIVAQRITSVVNSDQIIVM 535
Cdd:PRK10982 385 HrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAelAKKDKGIIIISSEMPELLGITDRILVM 464
|
250 260
....*....|....*....|....*.
gi 1251574723 536 NEGKIAGMgthEELKESNQiyQEIMR 561
Cdd:PRK10982 465 SNGLVAGI---VDTKTTTQ--NEILR 485
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
343-567 |
1.03e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 343 VIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYD-VESGVVKING--IDVREMDQSsLRQKI----------GLVPQ 409
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNPQQA-IAQGIamvpedrkrdGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 410 KAVLFTGTIASNMRYGKEDATDEeiweALRTAQAENFVSKLANGLGSrVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFD 489
Cdd:PRK13549 356 MGVGKNITLAALDRFTGGSRIDD----AAELKTILESIQRLKVKTAS-PELAIARLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 490 DSFSALDFKTDAKLREALKAETTEAVTLIVaqrITS----VVN-SDQIIVMNEGKIAGMGTHEELKEsnqiyQEIMRSQL 564
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQLVQQGVAIIV---ISSelpeVLGlSDRVLVMHEGKLKGDLINHNLTQ-----EQVMEAAL 502
|
...
gi 1251574723 565 SEE 567
Cdd:PRK13549 503 RSE 505
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
193-277 |
1.05e-05 |
|
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: 47.46 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 193 EGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSPLMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFI 272
Cdd:cd18567 185 ETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFL 264
|
....*
gi 1251574723 273 QYAMQ 277
Cdd:cd18567 265 AYKDQ 269
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
352-515 |
1.15e-05 |
|
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: 47.02 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 352 NAGETIAIIGSTGAGKSTLINMIprfydveSGVVKINGIDVremdqSSLRQKIGLVPQKAVL-FTGTIASNMRYGKEDAT 430
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDI-----EIELDTVSYKPQYIKAdYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 431 DEEIWEalrtaqaenfvSKLANGLG--SRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFK-----TDAKL 503
Cdd:cd03237 91 THPYFK-----------TEIAKPLQieQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmaSKVIR 159
|
170
....*....|..
gi 1251574723 504 REALKAETTEAV 515
Cdd:cd03237 160 RFAENNEKTAFV 171
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
327-538 |
1.47e-05 |
|
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: 46.08 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRY--EGAEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRfyDVESGVVK----INGIDVREmdqsSL 400
Cdd:cd03232 4 LTWKNLNYTVpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITgeilINGRPLDK----NF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 401 RQKIGLVPQKAVLFTGtiaSNMRygkedatdeeiwEALRtaqaenfVSKLANGLGsrVEqggnnfsggQKQRLSIARSLI 480
Cdd:cd03232 78 QRSTGYVEQQDVHSPN---LTVR------------EALR-------FSALLRGLS--VE---------QRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251574723 481 RKPEIYIFDDSFSALDFKTDAKLREALK--AETTEAVTLIVAQRITSVVNS-DQIIVMNEG 538
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKklADSGQAILCTIHQPSASIFEKfDRLLLLKRG 185
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
327-386 |
1.72e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 1.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGaeKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVK 386
Cdd:PRK15064 320 LEVENLTKGFDN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
326-569 |
1.75e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 326 KLSFEHVTFRYEGAEKPV------------------IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKI 387
Cdd:PRK13545 4 KVKFEHVTKKYKMYNKPFdklkdlffrskdgeyhyaLNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 388 NGIDVREMDQSSLRQKIglvpqkavlfTGTIASNMRYGKEDATDEEIWEAlrTAQAENFVSklangLGSRVEQGGNNFSG 467
Cdd:PRK13545 84 KGSAALIAISSGLNGQL----------TGIENIELKGLMMGLTKEKIKEI--IPEIIEFAD-----IGKFIYQPVKTYSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 468 GQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVAQRITSVVNS--DQIIVMNEGKIAGMGT 545
Cdd:PRK13545 147 GMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSfcTKALWLHYGQVKEYGD 226
|
250 260 270
....*....|....*....|....*....|..
gi 1251574723 546 HEE--------LKESNQIYQEiMRSQLSEEEI 569
Cdd:PRK13545 227 IKEvvdhydefLKKYNQMSVE-ERKDFREEQI 257
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
354-496 |
1.91e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 354 GETIAIIGSTGAGKSTLIN-----MIPRFYDVESGVVKINGID----------VREMDQSSLR--QKIGLVPQKAVLFTG 416
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKilsgeLIPNLGDYEEEPSWDEVLKrfrgtelqnyFKKLYNGEIKvvHKPQYVDLIPKVFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 417 TIasnmrygKE--DATDEE-IWEALrtaqaenfVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFS 493
Cdd:PRK13409 179 KV-------REllKKVDERgKLDEV--------VERL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
...
gi 1251574723 494 ALD 496
Cdd:PRK13409 242 YLD 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
335-542 |
1.97e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 335 RYEGAEKPVIE----------DITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSlRQKI 404
Cdd:PRK15439 260 RQQAAGAPVLTvedltgegfrNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLAR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 405 GLV--P---QKAVLFtgtIASNMRYGKEDATDEEIWEALRTAQAENFVSKLANGLG---SRVEQGGNNFSGGQKQRLSIA 476
Cdd:PRK15439 339 GLVylPedrQSSGLY---LDAPLAWNVCALTHNRRGFWIKPARENAVLERYRRALNikfNHAEQAARTLSGGNQQKVLIA 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1251574723 477 RSLIRKPEIYIFDDSFSALDFKTDAKLREALK--AETTEAVTLIVAQRITSVVNSDQIIVMNEGKIAG 542
Cdd:PRK15439 416 KCLEASPQLLIVDEPTRGVDVSARNDIYQLIRsiAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISG 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
350-519 |
2.08e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 350 EANAGETIAIIGSTGAGKSTLINMIprfydveSGVVKINGIDVremdqsSLRQKIGLVPQkavlftgtiasnmrY--GKE 427
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLL-------AGVLKPDEGEV------DPELKISYKPQ--------------YikPDY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 428 DATDEEIWEALRTAQAENFV-SKLANGLG------SRVeqggNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTD 500
Cdd:PRK13409 414 DGTVEDLLRSITDDLGSSYYkSEIIKPLQlerlldKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
170 180
....*....|....*....|.
gi 1251574723 501 AKLREALK--AETTEAVTLIV 519
Cdd:PRK13409 490 LAVAKAIRriAEEREATALVV 510
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
339-553 |
2.55e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.08 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 339 AEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDvESGVVKINGIDVREMDQSSL-RQKIGLVPQKAVLFtgt 417
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 418 iasNMrygkedatdeEIWEAL--------RTAQAENFVSKLAN--GLGSRVEQGGNNFSGGQKQR-------LSIARSLI 480
Cdd:PRK03695 83 ---AM----------PVFQYLtlhqpdktRTEAVASALNEVAEalGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 481 RKPEIYIFDDSFSALDFKTDAKLREALKAetteavtlIVAQRITSVVNS----------DQIIVMNEGKIAGMGTHEE-L 549
Cdd:PRK03695 150 PAGQLLLLDEPMNSLDVAQQAALDRLLSE--------LCQQGIAVVMSShdlnhtlrhaDRVWLLKQGKLLASGRRDEvL 221
|
....
gi 1251574723 550 KESN 553
Cdd:PRK03695 222 TPEN 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
354-499 |
3.78e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 354 GETIAIIGSTGAGKSTLINMIPRFYD---VESGVVKINGidvREMDqSSLRQKIGLVPQKAV-LFTGTIASNMRYG---- 425
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNG---RPLD-SSFQRSIGYVQQQDLhLPTSTVRESLRFSaylr 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 426 ------KEDATD--EEIWEALRTAQAENFVSKLAnGLGSRVEqggnnfsggQKQRLSIARSLIRKPEIYIF-DDSFSALD 496
Cdd:TIGR00956 865 qpksvsKSEKMEyvEEVIKLLEMESYADAVVGVP-GEGLNVE---------QRKRLTIGVELVAKPKLLLFlDEPTSGLD 934
|
...
gi 1251574723 497 FKT 499
Cdd:TIGR00956 935 SQT 937
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
354-496 |
6.63e-05 |
|
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: 45.93 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 354 GETIAIIGSTGAGKSTLIN-----MIPRFYDVESGVVKINGID----------VREMDQSSLR-----QKIGLVPQkavL 413
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKilsgeLKPNLGDYDEEPSWDEVLKrfrgtelqdyFKKLANGEIKvahkpQYVDLIPK---V 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 414 FTGTIasnmrygKE--DATDEEiwealrtAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDS 491
Cdd:COG1245 176 FKGTV-------REllEKVDER-------GKLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
....*
gi 1251574723 492 FSALD 496
Cdd:COG1245 240 SSYLD 244
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
354-423 |
2.72e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 2.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 354 GETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMDQSSLRQKIGLVPQKAVLFTGTIASNMR 423
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLAL 71
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
354-535 |
2.72e-04 |
|
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: 42.74 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 354 GETIAIIGSTGAGKSTLIN-----MIPRFYDVES-----GVVK-INGI-------DVREMDQSSLR--QKIGLVPQKavl 413
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKilagkLKPNLGKFDDppdwdEILDeFRGSelqnyftKLLEGDVKVIVkpQYVDLIPKA--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 414 FTGTIASNMrygkeDATDEeiwealrTAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFS 493
Cdd:cd03236 103 VKGKVGELL-----KKKDE-------RGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1251574723 494 ALDFKTDAKLREALKAETTEAVTLIVAQRITSVVN--SDQIIVM 535
Cdd:cd03236 169 YLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDylSDYIHCL 212
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
441-550 |
4.98e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.41 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 441 AQAENFVSKLAngLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLIVA 520
Cdd:NF000106 123 ARADELLERFS--LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLT 200
|
90 100 110
....*....|....*....|....*....|..
gi 1251574723 521 QRITSVVN--SDQIIVMNEGKIAGMGTHEELK 550
Cdd:NF000106 201 TQYMEEAEqlAHELTVIDRGRVIADGKVDELK 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
339-549 |
5.26e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.99 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 339 AEKPVIEDITFEANAGETIAIIGSTGAGKS----TLINMIPrfydveSGVVKING---IDVREMDQSSLR-QKIGLV--- 407
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILP------AGVRQTAGrvlLDGKPVAPCALRgRKIATImqn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 408 PQKAVLFTGTIASNMR-----YGKEdATDEEIWEALRTAQAENfvsklanglGSRVEQG-GNNFSGGQKQRLSIARSLIR 481
Cdd:PRK10418 88 PRSAFNPLHTMHTHARetclaLGKP-ADDATLTAALEAVGLEN---------AARVLKLyPFEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1251574723 482 KPEIYIFDDSFSALDFKTDAK---LREALKAETTEAVtLIVAQRITSVVN-SDQIIVMNEGKIAGMGTHEEL 549
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARildLLESIVQKRALGM-LLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
82-297 |
7.63e-04 |
|
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: 41.88 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 82 KELRDKIFTKVEDFSLQEFDKVGTSSLITRTTNDVVQIQNVLYMMMRLMVMAPIMLLGGIIMAVGRDAKLSlifvVVLPL 161
Cdd:cd18558 92 KKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLT----LVILA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 162 LLLLVVILGGKAMPMFKSL----QKKMDKLNRVIREGLTGIRVVRSFNRNEDELEKFEEANADYATTAIKVNRLLSLMSP 237
Cdd:cd18558 168 ISPVLGLSAVVWAKILSGFtdkeKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMG 247
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 238 LMMLLMNLTSIAIVWIGSIFIGNGDMQVGDLMAFIQYAmqIMMSFMMLSAVFIMIPRAGA 297
Cdd:cd18558 248 AAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSV--LIGAFSAGQQVPSIEAFANA 305
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
327-561 |
8.15e-04 |
|
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: 42.12 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 327 LSFEHVTFRYEGAEkpVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYD---------VESGVVKINGI-DVREMD 396
Cdd:TIGR02633 2 LEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeiyWSGSPLKASNIrDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 397 QSSLRQKIGLVPQKAVlftgtiASNMRYGKEDATDEEIWE-ALRTAQAENFVSKLANGLgSRVEQGGNNFSGGQKQRLSI 475
Cdd:TIGR02633 80 IVIIHQELTLVPELSV------AENIFLGNEITLPGGRMAyNAMYLRAKNLLRELQLDA-DNVTRPVGDYGGGQQQLVEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 476 ARSLIRKPEIYIFDDSFSALDFKTDAKLREALKAETTEAVTLI-VAQRITSVVN-SDQIIVMNEGKIAGMGTHEELKESN 553
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVyISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSEDD 232
|
....*...
gi 1251574723 554 QIYQEIMR 561
Cdd:TIGR02633 233 IITMMVGR 240
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
331-374 |
9.17e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 9.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1251574723 331 HVTFRYEgaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMI 374
Cdd:PRK10938 265 NGVVSYN--DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI 306
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
344-539 |
9.87e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.84 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 344 IEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVES--GVVKINGID-----VREMDQSS---LRQKIGLVPQKavl 413
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEElqasnIRDTERAGiaiIHQELALVKEL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 414 ftgTIASNMRYGKEDATDEEI-WEALrTAQAENFVSKLanGLGSRVEQGGNNFSGGQKQRLSIARSLIRKPEIYIFDDSF 492
Cdd:PRK13549 98 ---SVLENIFLGNEITPGGIMdYDAM-YLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1251574723 493 SALDFKTDAKLREALKAETTEAVTLI-VAQRITSVVN-SDQIIVMNEGK 539
Cdd:PRK13549 172 ASLTESETAVLLDIIRDLKAHGIACIyISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
446-538 |
1.33e-03 |
|
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: 40.00 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 446 FVSKL----ANGLGS-RVEQGGNNFSGGQKQRLSIARSLIRKPE--IYIFDDSFSALDFKTDAKLREALKAETTEAVTLI 518
Cdd:cd03238 64 FIDQLqfliDVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVI 143
|
90 100
....*....|....*....|.
gi 1251574723 519 VAQRITSVVN-SDQIIVMNEG 538
Cdd:cd03238 144 LIEHNLDVLSsADWIIDFGPG 164
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
354-372 |
1.34e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 1.34e-03
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
285-464 |
1.57e-03 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 41.12 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 285 LSAVFIMIPRAgasAERINEVLDMNAEILNPENP-------KTSTPPAK-LSFEHVTFRYEGAEKPVieDITFEANAGET 356
Cdd:PRK06793 84 LIAEDVVIPRG---NHLLGKVLSANGEVLNEEAEniplqkiKLDAPPIHaFEREEITDVFETGIKSI--DSMLTIGIGQK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 357 IAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVREMdQSSLRQKIGLVP-QKAVLFTGTiasnmrygkedaTDEEIW 435
Cdd:PRK06793 159 IGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREV-KDFIRKELGEEGmRKSVVVVAT------------SDESHL 225
|
170 180
....*....|....*....|....*....
gi 1251574723 436 EALRTAqaenfvsKLANGLGSRVEQGGNN 464
Cdd:PRK06793 226 MQLRAA-------KLATSIAEYFRDQGNN 247
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
353-374 |
1.84e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.07 E-value: 1.84e-03
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
353-560 |
2.18e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.76 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 353 AGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKINGIDVR--------EMDQSSLRQKIGLVPQKavlftgTIASNMRY 424
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqEAGIGIIHQELNLIPQL------TIAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251574723 425 GKEDAT-----DeeiWEALRtAQAENFVSKLANGLGSRVEQGgnNFSGGQKQRLSIARSLIRKPEIYIFDDSFSAL-DFK 498
Cdd:PRK10762 103 GREFVNrfgriD---WKKMY-AEADKLLARLNLRFSSDKLVG--ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1251574723 499 TDA---KLREaLKAETTEAVtlIVAQRITSVVN-SDQIIVMNEGKIAGMGTHEELKESNQIyqEIM 560
Cdd:PRK10762 177 TESlfrVIRE-LKSQGRGIV--YISHRLKEIFEiCDDVTVFRDGQFIAEREVADLTEDSLI--EMM 237
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
353-374 |
2.43e-03 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 40.10 E-value: 2.43e-03
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
329-387 |
2.83e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 2.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 329 FEHVTFRYEgaEKPVIEDITFEANAGETIAIIGSTGAGKSTLINMIPRFYDVESGVVKI 387
Cdd:PRK11819 327 AENLSKSFG--DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
14-78 |
5.06e-03 |
|
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: 38.96 E-value: 5.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251574723 14 VLVLTFGQVIgQLYLPTLMSNIIDKGVVTGDTDYIWS--TGMKMLLISFASV--ILSVIVVYLASRISM 78
Cdd:cd18571 8 LLGLLLGSLL-QLIFPFLTQSIVDKGINNKDLNFIYLilIAQLVLFLGSTSIefIRSWILLHISSRINI 75
|
|
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