|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-572 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 553.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 1 MENFKIILPYLKRYKKDVVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFA 79
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRiIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 80 AKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWW 159
Cdd:COG1132 86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 160 APVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFS 239
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 240 AIMPAFQMIAYTVIALIVYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRIREVLETEPDVK 319
Cdd:COG1132 246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 320 FVESG-SVAPLSGSVEFDHVSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI 398
Cdd:COG1132 326 DPPGAvPLPPVRGEIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 399 KDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQR 478
Cdd:COG1132 405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKT 558
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
570
....*....|....
gi 492039060 559 SLVYQEIFKTQKGK 572
Cdd:COG1132 565 GGLYARLYRLQFGE 578
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-569 |
1.17e-116 |
|
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: 361.84 E-value: 1.17e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 3 NFKIILPYLKRYKKDVVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQavlsdgiWLVVLGIIAIISGIFNV----- 76
Cdd:COG2274 143 GLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVvIDRVLPNQDLS-------TLWVLAIGLLLALLFEGllrll 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 77 --YFAAKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRL-----INDMNQVMNMMmqlfmqmlrLPILIVGSFIF 149
Cdd:COG2274 216 rsYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFrdvesIREFLTGSLLT---------ALLDLLFVLIF 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 150 CIVII---PRFWWAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQ 226
Cdd:COG2274 287 LIVLFfysPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 227 LNDYNI---VIGYWFSAIMPAFQMIAYTVI-ALIVYL-IGKNITAhPSDIAVVSpFVNYVLTLLFTIMiagMTLMQFSRA 301
Cdd:COG2274 367 YLNARFklrRLSNLLSTLSGLLQQLATVALlWLGAYLvIDGQLTL-GQLIAFNI-LSGRFLAPVAQLI---GLLQRFQDA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 302 NISLGRIREVLETEPDVKFVESGSVAP-LSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLI 380
Cdd:COG2274 442 KIALERLDDILDLPPEREEGRSKLSLPrLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 381 ARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSF 460
Cdd:COG2274 522 LGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 461 DHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILV 540
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIV 681
|
570 580
....*....|....*....|....*....
gi 492039060 541 LDDGKLVAQGTHEELLKTSLVYQEIFKTQ 569
Cdd:COG2274 682 LDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-569 |
1.67e-114 |
|
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: 352.10 E-value: 1.67e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 4 FKIILPYLKRYKKDVVCAIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLsdgiWLVVLGIIAI-----ISGIFNVYF 78
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVL----WWVPLVVIGLavlrgICSFVSTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 79 AAKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFW 158
Cdd:TIGR02203 78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 159 WAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWF 238
Cdd:TIGR02203 158 LIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 239 SAIMPAFQMIAYTVIALIVYLIGknitaHPSDIAVVSP--FVNYvltllFTIMIAGMT-LMQFSRANISLGR-------I 308
Cdd:TIGR02203 238 SISSPITQLIASLALAVVLFIAL-----FQAQAGSLTAgdFTAF-----ITAMIALIRpLKSLTNVNAPMQRglaaaesL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 309 REVLETEPDVkfvESGSVAP--LSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP 386
Cdd:TIGR02203 308 FTLLDSPPEK---DTGTRAIerARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 387 TKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGN-AQAKLHELQRAANMAQASEFIERYNDSFDHEVE 465
Cdd:TIGR02203 385 DSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 466 ERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGK 545
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
570 580
....*....|....*....|....
gi 492039060 546 LVAQGTHEELLKTSLVYQEIFKTQ 569
Cdd:TIGR02203 545 IVERGTHNELLARNGLYAQLHNMQ 568
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-564 |
2.06e-94 |
|
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: 299.76 E-value: 2.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 3 NFKIILPYLKRYKKDVVCAIIAILVSAFSGLyqpklleniqkALMAnqkqavLSdGiWLVVlgIIAIISGIFNVYFAA-- 80
Cdd:COG4987 2 DLLRLLRLLRPHRGRLLLGVLLGLLTLLAGI-----------GLLA------LS-G-WLIA--AAALAPPILNLFVPIvg 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 81 ----KIAQGV----------------VSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNqvmnmmmqlfmqmlRL- 139
Cdd:COG4987 61 vrafAIGRTVfrylerlvshdatlrlLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVD--------------ALd 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 140 --------PILI-VGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVL-----RQMNSLFTKFQEMMDRISNQAQETLQGVR 205
Cdd:COG4987 127 nlylrvllPLLVaLLVILAAVAFLAFFSPALALVLALGLLLAGLLLpllaaRLGRRAGRRLAAARAALRARLTDLLQGAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 206 VVKSFNQGPQEIKKFDQTSDQLNDYNIVIGyWFSAIMPAFQMIAYTVIALIVYLIGKNITAH----PSDIAVVspfvnyV 281
Cdd:COG4987 207 ELAAYGALDRALARLDAAEARLAAAQRRLA-RLSALAQALLQLAAGLAVVAVLWLAAPLVAAgalsGPLLALL------V 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 282 LTLL-----FTIMIAGMTLMQFSRAniSLGRIREVLETEPDVKFVESGSVAPLSGSVEFDHVSFTYPDGDDPTLKDISFK 356
Cdd:COG4987 280 LAALalfeaLAPLPAAAQHLGRVRA--AARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 357 IKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAK 436
Cdd:COG4987 358 LPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDAT 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 437 LHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHE 516
Cdd:COG4987 438 DEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA 517
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 492039060 517 LPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQE 564
Cdd:COG4987 518 LAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQ 565
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-558 |
5.33e-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: 290.89 E-value: 5.33e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 10 YLKRYKKDVVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQ-KQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVV 87
Cdd:COG4988 11 LARGARRWLALAVLLGLLSGLLIIAQAWLLASlLAGLIIGGApLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 88 SDLREDTYAKIQTFSFGNIKKFSAGSLTTRLIndmnqvmnmmmqlfmqmlR------------LPILIVGSFIFCIVIIP 155
Cdd:COG4988 91 RRLRRRLLEKLLALGPAWLRGKSTGELATLLT------------------EgvealdgyfaryLPQLFLAALVPLLILVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 156 RF---WWAPVVMVA---LIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLND 229
Cdd:COG4988 153 VFpldWLSGLILLVtapLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 230 ynivigywfsAIMP----AFQ------MIAYTVIALI-VY----LIGKNITahpsdiavvspfvnyVLTLLFTIMIAG-- 292
Cdd:COG4988 233 ----------RTMKvlrvAFLssavleFFASLSIALVaVYigfrLLGGSLT---------------LFAALFVLLLAPef 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 293 -MTLMQFS-----RANI--SLGRIREVLETEPDVKFVESGSVAPLSG-SVEFDHVSFTYPDGDdPTLKDISFKIKPGQMV 363
Cdd:COG4988 288 fLPLRDLGsfyhaRANGiaAAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGR-PALDGLSLTIPPGERV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 364 GIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRA 443
Cdd:COG4988 367 ALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 444 ANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTF 523
Cdd:COG4988 447 LEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVI 526
|
570 580 590
....*....|....*....|....*....|....*
gi 492039060 524 IIAEKIVSVINADTILVLDDGKLVAQGTHEELLKT 558
Cdd:COG4988 527 LITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
333-566 |
2.54e-90 |
|
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: 277.96 E-value: 2.54e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIF 566
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
162-556 |
6.66e-88 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 283.39 E-value: 6.66e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 162 VVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNI-VIGYWfsA 240
Cdd:PRK13657 163 VVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMpVLSWW--A 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 241 IMPAFQMIAYTVIALIVYLIGknITAHPSDIAVVSPFVNYVLtlLFTIMIAGMTLMQ--FSRANISLGRIREVLETEPDV 318
Cdd:PRK13657 241 LASVLNRAASTITMLAILVLG--AALVQKGQLRVGEVVAFVG--FATLLIGRLDQVVafINQVFMAAPKLEEFFEVEDAV 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 319 KFVE----SGSVAPLSGSVEFDHVSFTYpDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIG 394
Cdd:PRK13657 317 PDVRdppgAIDLGRVKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILID 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 395 GQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGG 474
Cdd:PRK13657 396 GTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGG 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 475 QKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEE 554
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDE 555
|
..
gi 492039060 555 LL 556
Cdd:PRK13657 556 LV 557
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-572 |
1.01e-86 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 280.37 E-value: 1.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 4 FKIILPYLKRYKKDVVCAIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLsdgIW--LVVLGIIAI--ISGIFNVYFA 79
Cdd:PRK11176 13 FRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVL---KWmpLVVIGLMILrgITSFISSYCI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 80 AKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFciviipRFW- 158
Cdd:PRK11176 90 SWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIM------MFYy 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 159 -W---------APVVMVALifgfgAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLN 228
Cdd:PRK11176 164 sWqlsliliviAPIVSIAI-----RVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 229 DYNIVIGYWFSAIMPAFQMIAYTVIALIVYLigkniTAHPSDIAVVSPfvnYVLTLLFTIMIAGMTLM--------QFSR 300
Cdd:PRK11176 239 QQGMKMVSASSISDPIIQLIASLALAFVLYA-----ASFPSVMDTLTA---GTITVVFSSMIALMRPLksltnvnaQFQR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 301 ---ANISLGRIREvLETEPDVKFVEsgsVAPLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLA 377
Cdd:PRK11176 311 gmaACQTLFAILD-LEQEKDEGKRV---IERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 378 QLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQG-NAQAKLHELQRAANMAQASEFIERY 456
Cdd:PRK11176 387 NLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAARMAYAMDFINKM 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 457 NDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINAD 536
Cdd:PRK11176 467 DNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKAD 546
|
570 580 590
....*....|....*....|....*....|....*.
gi 492039060 537 TILVLDDGKLVAQGTHEELLKTSLVYQEIFKTQKGK 572
Cdd:PRK11176 547 EILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
331-557 |
6.58e-85 |
|
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: 263.70 E-value: 6.58e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 331 GSVEFDHVSFTYpDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTV 410
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 491 ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLK 557
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
303-556 |
1.36e-82 |
|
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: 270.15 E-value: 1.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 303 ISLGRIREVLETEPDVKfvESGSVAPLS---GSVEFDHVSFTYpDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQL 379
Cdd:COG5265 327 ADMERMFDLLDQPPEVA--DAPDAPPLVvggGEVRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 380 IARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDS 459
Cdd:COG5265 404 LFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 460 FDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTIL 539
Cdd:COG5265 484 YDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEIL 563
|
250
....*....|....*..
gi 492039060 540 VLDDGKLVAQGTHEELL 556
Cdd:COG5265 564 VLEAGRIVERGTHAELL 580
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
333-569 |
8.31e-82 |
|
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: 255.93 E-value: 8.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDD-PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVS 411
Cdd:cd03249 1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIFKTQ 569
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
333-569 |
1.48e-81 |
|
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: 255.23 E-value: 1.48e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:cd03253 1 IEFENVTFAYDPGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIFKTQ 569
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
18-308 |
8.56e-79 |
|
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: 250.01 E-value: 8.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 18 VVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYA 96
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADiIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 97 KIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVL 176
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 177 RQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIALI 256
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 492039060 257 VYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18548 241 LWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
333-545 |
1.74e-77 |
|
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: 242.29 E-value: 1.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTIASNLrqgnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGK 545
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
333-569 |
1.58e-69 |
|
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: 224.29 E-value: 1.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTY-PDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVS 411
Cdd:cd03252 1 ITFEHVRFRYkPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIFKTQ 569
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
331-551 |
3.41e-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: 222.75 E-value: 3.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 331 GSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTV 410
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSGTIASNLRQGNaQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 491 ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGT 551
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
331-550 |
1.72e-68 |
|
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: 220.92 E-value: 1.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 331 GSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTV 410
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 491 ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQG 550
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-562 |
5.23e-67 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 230.76 E-value: 5.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 7 ILPYLKRYKKDVVCAIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLSDGIWLvvLGIIAIIS--------GIFNVYF 78
Cdd:TIGR00958 152 LLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFF--MCLLSIASsvsaglrgGSFNYTM 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 79 AAkiaqgVVSDLREDTYAKI--QTFSFGNIKKfsAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPR 156
Cdd:TIGR00958 230 AR-----INLRIREDLFRSLlrQDLGFFDENK--TGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPR 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 157 FWWAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYN----- 231
Cdd:TIGR00958 303 LTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNkrkal 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 232 IVIGY-WFSAIMPAFqmiaytVIALIVYLIGKNITAHPSDIAVVSPFVNYVLTL------LFTIMIAGMTLMQFSRanis 304
Cdd:TIGR00958 383 AYAGYlWTTSVLGML------IQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLgeavrvLSYVYSGMMQAVGASE---- 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 305 lgRIREVLETEPDVKfvESGSVAP--LSGSVEFDHVSFTYPD-GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIA 381
Cdd:TIGR00958 453 --KVFEYLDRKPNIP--LTGTLAPlnLEGLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 382 RLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFD 461
Cdd:TIGR00958 529 NLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYD 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 462 HEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHElpDTTTFIIAEKIVSVINADTILVL 541
Cdd:TIGR00958 609 TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA--SRTVLLIAHRLSTVERADQILVL 686
|
570 580
....*....|....*....|.
gi 492039060 542 DDGKLVAQGTHEELLKTSLVY 562
Cdd:TIGR00958 687 KKGSVVEMGTHKQLMEDQGCY 707
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
184-568 |
2.57e-65 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 223.61 E-value: 2.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 184 TKFQEMMDRISNqaqetlqgVRVVKSFNQGPQEIKKFDQ-TSDQLNDYNIVIGYWfsAIMPAFQMIAYTVIALIVYLIG- 261
Cdd:TIGR01192 193 NVFKHVSDSISN--------VSVVHSYNRIEAETSALKQfTNNLLSAQYPVLDWW--ALASGLNRMASTISMMCILVIGt 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 262 ---KNITAHPSDIAVVSPFVNYVLTLLfTIMIAGMTLMQFSRAnislgRIREVLETEPDVKFVE----SGSVAPLSGSVE 334
Cdd:TIGR01192 263 vlvIKGELSVGEVIAFIGFANLLIGRL-DQMSGFITQIFEARA-----KLEDFFDLEDSVFQREepadAPELPNVKGAVE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 335 FDHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVL 414
Cdd:TIGR01192 337 FRHITFEFANSSQ-GVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVF 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 415 QRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILIL 494
Cdd:TIGR01192 416 QDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVL 495
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 495 DDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIFKT 568
Cdd:TIGR01192 496 DEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
324-546 |
1.06e-64 |
|
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: 211.18 E-value: 1.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 324 GSVAP--LSGSVEFDHVSFTYPD-GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD 400
Cdd:cd03248 1 GSLAPdhLKGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 401 VTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLS 480
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 481 IARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
307-556 |
1.67e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 210.45 E-value: 1.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 307 RIREVLETEPDVKFVESGSVAPLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP 386
Cdd:PRK11160 313 RINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 387 TKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERyNDSFDHEVEE 466
Cdd:PRK11160 393 QQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 467 RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:PRK11160 472 GGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
250
....*....|
gi 492039060 547 VAQGTHEELL 556
Cdd:PRK11160 552 IEQGTHQELL 561
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
42-541 |
5.95e-59 |
|
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: 205.21 E-value: 5.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 42 IQKALMANQKQAVLSDG-------IWLVVLGIIAIISGIFnVYF----AAKIAQGVVSDLREDTYAKIQTFSFGNIKKFS 110
Cdd:TIGR02857 21 AQAWLLARVVDGLISAGeplaellPALGALALVLLLRALL-GWLqeraAARAAAAVKSQLRERLLEAVAALGPRWLQGRP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 111 AGSLTTRLINDMNQVMNMMMQLfmqmlrLPILI---VGSFIFCIVIIPRFWWAPVVMV---ALIFGFGAYVLRQMNSLFT 184
Cdd:TIGR02857 100 SGELATLALEGVEALDGYFARY------LPQLVlavIVPLAILAAVFPQDWISGLILLltaPLIPIFMILIGWAAQAAAR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 185 KFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIV---IGYWFSAIMPAFQMIAYTVIAliVYlIG 261
Cdd:TIGR02857 174 KQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRvlrIAFLSSAVLELFATLSVALVA--VY-IG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 262 KNITAHPSDIAvvspfvnyvlTLLFTIMIAG---MTLMQFS-----RAN--ISLGRIREVLETEPDVKFVESGSVAPLSG 331
Cdd:TIGR02857 251 FRLLAGDLDLA----------TGLFVLLLAPefyLPLRQLGaqyhaRADgvAAAEALFAVLDAAPRPLAGKAPVTAAPAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVS 411
Cdd:TIGR02857 321 SLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVL 541
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
163-570 |
6.76e-58 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 203.41 E-value: 6.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 163 VMVALIFGFGAyvlrQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIgywfSAIM 242
Cdd:PRK10789 149 VMAIMIKRYGD----QLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRV----ARID 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 243 PAFQMIAYTVIALIVYLI---GKNITAHPS-DIAVVSPFVNYvLTLLFTIMIAgMTLMqFS---RANISLGRIREVLETE 315
Cdd:PRK10789 221 ARFDPTIYIAIGMANLLAiggGSWMVVNGSlTLGQLTSFVMY-LGLMIWPMLA-LAWM-FNiveRGSAAYSRIRAMLAEA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 316 PDVKfVESGSVAPLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGG 395
Cdd:PRK10789 298 PVVK-DGSEPVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 396 QNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQ 475
Cdd:PRK10789 377 IPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQ 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 476 KQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQL 536
|
410
....*....|....*
gi 492039060 556 LKTSLVYQEIFKTQK 570
Cdd:PRK10789 537 AQQSGWYRDMYRYQQ 551
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
162-556 |
3.67e-57 |
|
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: 203.65 E-value: 3.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 162 VVMVALIFGFGAYVLRQMNslfTKFQEMMDRISNQAQETLQGV---RV----VKSFNQGPQ---EIKKFDQTSDQLNDYN 231
Cdd:TIGR03797 285 ALVAIAVTLVLGLLQVRKE---RRLLELSGKISGLTVQLINGIsklRVagaeNRAFARWAKlfsRQRKLELSAQRIENLL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 232 IVigywFSAIMPAFQMIAytVIALIVYLIGkniTAHPSdiavVSPFVNYvlTLLFTIMIAGMTlmQFSRANISL------ 305
Cdd:TIGR03797 362 TV----FNAVLPVLTSAA--LFAAAISLLG---GAGLS----LGSFLAF--NTAFGSFSGAVT--QLSNTLISIlavipl 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 306 -GRIREVLETEPDVkfvESGSVAP--LSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIAR 382
Cdd:TIGR03797 425 wERAKPILEALPEV---DEAKTDPgkLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLG 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 383 LYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLrQGNAQAKLHELQRAANMAQASEFIERYNDSFDH 462
Cdd:TIGR03797 502 FETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHT 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 463 EVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHElpDTTTFIIAEKIVSVINADTILVLD 542
Cdd:TIGR03797 581 VISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLD 658
|
410
....*....|....
gi 492039060 543 DGKLVAQGTHEELL 556
Cdd:TIGR03797 659 AGRVVQQGTYDELM 672
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
288-557 |
1.80e-50 |
|
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: 182.64 E-value: 1.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 288 IMIAGMTLM---------------QFSRANISLGRIREVLETEPDVKfvESGSVAPLSGSVEFDHVSFTYPDGDDPTLKD 352
Cdd:COG4618 273 AMIAASILMgralapieqaiggwkQFVSARQAYRRLNELLAAVPAEP--ERMPLPRPKGRLSVENLTVVPPGSKRPILRG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 353 ISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNL-RQG 431
Cdd:COG4618 351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 432 NAQAklHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQ 511
Cdd:COG4618 431 DADP--EKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA 508
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 492039060 512 ALEHeLPD--TTTFIIAEKiVSVIN-ADTILVLDDGKLVAQGTHEELLK 557
Cdd:COG4618 509 AIRA-LKArgATVVVITHR-PSLLAaVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
237-525 |
2.72e-49 |
|
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: 178.71 E-value: 2.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 237 WFSAIMPAFQMIAYTVIALIVYLIGKNITAH----PSDIAVVspfvnyVLTLL--FTIMIA-GMTLMQFSRANISLGRIR 309
Cdd:TIGR02868 235 AATALGAALTLLAAGLAVLGALWAGGPAVADgrlaPVTLAVL------VLLPLaaFEAFAAlPAAAQQLTRVRAAAERIV 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 310 EVLETEPDVKFVES---GSVAPLSGSVEFDHVSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP 386
Cdd:TIGR02868 309 EVLDAAGPVAEGSApaaGAVGLGKPTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 387 TKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEE 466
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGE 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 467 RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFII 525
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLI 526
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
318-555 |
2.61e-48 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 177.34 E-value: 2.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 318 VKFVESGSVAPLSGSVEFDH----------VSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLaqLIARL-YDP 386
Cdd:PRK11174 325 VTFLETPLAHPQQGEKELASndpvtieaedLEILSPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSL--LNALLgFLP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 387 TKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEE 466
Cdd:PRK11174 402 YQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGD 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 467 RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:PRK11174 482 QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
....*....
gi 492039060 547 VAQGTHEEL 555
Cdd:PRK11174 562 VQQGDYAEL 570
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
333-557 |
5.81e-48 |
|
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: 166.74 E-value: 5.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAV--LFSGTIAS-------NLRQGNAQAKlhelQRAANMAQASEfIERYndsfdhevEERSANF-SGGQKQRLSIA 482
Cdd:COG1122 80 VFQNPDdqLFAPTVEEdvafgpeNLGLPREEIR----ERVEEALELVG-LEHL--------ADRPPHElSGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 483 RGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDT-TTFIIA----EKIVSVinADTILVLDDGKLVAQGTHEELLK 557
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELL-KRLNKEgKTVIIVthdlDLVAEL--ADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
328-551 |
6.22e-48 |
|
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: 166.05 E-value: 6.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 328 PLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALR 407
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQRAVLFSGTIASNLrqgnaqaklhelqraanmaqasefiERYNDSFDHE------VEERSANFSGGQKQRLSI 481
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNL-------------------------DPFDEYSDEEiygalrVSEGGLNLSQGQRQLLCL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGT 551
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
199-566 |
3.61e-47 |
|
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: 175.70 E-value: 3.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 199 ETLQGVRVVKSFNQgpqEIKKFDQTSDQLNDY------NIVIGYWFSAIMPAFQMIAYTVI--ALIVYLIGKNITAhpSD 270
Cdd:TIGR01193 339 EDLNGIETIKSLTS---EAERYSKIDSEFGDYlnksfkYQKADQGQQAIKAVTKLILNVVIlwTGAYLVMRGKLTL--GQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 271 IAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANIslgRIREVLETepDVKFVESGSVAPLS---GSVEFDHVSFTYPDGDd 347
Cdd:TIGR01193 414 LITFNALLSYFLTPLENIINLQPKLQAARVANN---RLNEVYLV--DSEFINKKKRTELNnlnGDIVINDVSYSYGYGS- 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASN 427
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILEN 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 428 LRQGNAQ-AKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESE 506
Cdd:TIGR01193 568 LLLGAKEnVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE 647
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 507 KKVQQALEHeLPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIF 566
Cdd:TIGR01193 648 KKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
333-566 |
3.81e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 162.16 E-value: 3.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKtVSF 412
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRqgnAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:COG1131 78 VPQEPALYPDlTVRENLR---FFARLYGLPRKEARERIDELLELFG--LTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHELPDTTTFII-------AEKIvsvinADTILVLDDGKLVAQGTHEELLKTSLvyQE 564
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAEGKTVLLsthyleeAERL-----CDRVAIIDKGRIVADGTPDELKARLL--ED 225
|
..
gi 492039060 565 IF 566
Cdd:COG1131 226 VF 227
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
328-569 |
6.81e-45 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 167.97 E-value: 6.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 328 PL-SGSVEFDHVSFTYPDgDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL 406
Cdd:PRK10790 335 PLqSGRIDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 407 RKTVSFVLQRAVLFSGTIASNLRQGNAQAKlHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLI 486
Cdd:PRK10790 414 RQGVAMVQQDPVVLADTFLANVTLGRDISE-EQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 487 AKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIF 566
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY 572
|
...
gi 492039060 567 KTQ 569
Cdd:PRK10790 573 QLQ 575
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
141-557 |
6.91e-45 |
|
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: 171.28 E-value: 6.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 141 ILIVGSFIFCIVIIPRfwwapVVMVALIFGFGAYVLRQMNSLftkfqEMMDR--ISNQAQETLQGVRVVKSFNqgpqEIK 218
Cdd:TIGR00957 1099 VILLATPIAAVIIPPL-----GLLYFFVQRFYVASSRQLKRL-----ESVSRspVYSHFNETLLGVSVIRAFE----EQE 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 219 KFDQTSDQLNDYN-------IVIGYWFsAIMPAFQMIAYTVIALIVYLIGKnitaHPSDIAVVSPFVNYVLTLLFTI--M 289
Cdd:TIGR00957 1165 RFIHQSDLKVDENqkayypsIVANRWL-AVRLECVGNCIVLFAALFAVISR----HSLSAGLVGLSVSYSLQVTFYLnwL 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 290 IAGMTLMQfsrANI-SLGRIREVLETEPDVKFVESGSVAPLS----GSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVG 364
Cdd:TIGR00957 1240 VRMSSEME---TNIvAVERLKEYSETEKEAPWQIQETAPPSGwpprGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVG 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 365 IVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLrQGNAQAKLHELQRAA 444
Cdd:TIGR00957 1317 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL-DPFSQYSDEEVWWAL 1395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 445 NMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFI 524
Cdd:TIGR00957 1396 ELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLT 1475
|
410 420 430
....*....|....*....|....*....|...
gi 492039060 525 IAEKIVSVINADTILVLDDGKLVAQGTHEELLK 557
Cdd:TIGR00957 1476 IAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
334-545 |
2.06e-44 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 156.86 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFV 413
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQ--RAVLFSGTIASNLRQG--NAQAKLHELQRAANMAqasefIERYNDSfdhEVEERS-ANFSGGQKQRLSIARGLIAK 488
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGleNLGLPEEEIEERVEEA-----LELVGLE---GLRDRSpFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 489 APILILDDSTSALDAESEKKVQQALeHELPDT-TTFIIAEKIVSVIN--ADTILVLDDGK 545
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELL-KKLKAEgKTIIIVTHDLDLLLelADRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
334-546 |
3.73e-44 |
|
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: 154.68 E-value: 3.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFV 413
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSGTIASNLrqgnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAPILI 493
Cdd:cd03246 82 PQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492039060 494 LDDSTSALDAESEKKVQQALEH-ELPDTTTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
333-550 |
1.07e-43 |
|
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: 153.62 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVtEAALRKTVSF 412
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTIASNLrqgnaqaklhelqraanmaqasefieryndsfdheveerSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQG 550
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
328-556 |
2.73e-43 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 166.45 E-value: 2.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 328 PLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALR 407
Cdd:PLN03130 1233 PSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQRAVLFSGTIASNLRQGNAQ--AKLHE-LQRAanmaQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARG 484
Cdd:PLN03130 1313 KVLGIIPQAPVLFSGTVRFNLDPFNEHndADLWEsLERA----HLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARA 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELL 556
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
159-556 |
1.09e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 161.68 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 159 WApvVMVALIFGFGAYVLRQMNSLFTKFQEMMDR--ISNQAQETLQG---VRVVKSFNQGPQEIKKFDQTSDQLNDYNIV 233
Cdd:PLN03232 1054 WA--IMPLLILFYAAYLYYQSTSREVRRLDSVTRspIYAQFGEALNGlssIRAYKAYDRMAKINGKSMDNNIRFTLANTS 1131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 234 IGYWFSAIMPAFQMIAYTVIALIVYLIGKNITAHPSDIAVVSPFVNYvlTLLFTIMIAGMtLMQFSRANISLGRIREV-- 311
Cdd:PLN03232 1132 SNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAGFASTMGLLLSY--TLNITTLLSGV-LRQASKAENSLNSVERVgn 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 312 ---LETE-PDV-KFVESGSVAPLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP 386
Cdd:PLN03232 1209 yidLPSEaTAIiENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVEL 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 387 TKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLhELQRAANMAQASEFIERYNDSFDHEVEE 466
Cdd:PLN03232 1289 EKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDA-DLWEALERAHIKDVIDRNPFGLDAEVSE 1367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 467 RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:PLN03232 1368 GGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
410
....*....|
gi 492039060 547 VAQGTHEELL 556
Cdd:PLN03232 1448 LEYDSPQELL 1457
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
333-555 |
5.98e-41 |
|
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: 147.71 E-value: 5.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD-----PTKGKVKIGGQNI--KDVTEAA 405
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQRAVLFSGTIASNLRQGnaqAKLHELQRAANMAQASEFIERYNDSFDhEVEERSA--NFSGGQKQRLSIAR 483
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYG---LRLHGIKLKEELDERVEEALRKAALWD-EVKDRLHalGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 484 GLIAKAPILILDDSTSALDAESEKKVQQALeHELPDTTTFII-------AEKIvsvinADTILVLDDGKLVAQGTHEEL 555
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELI-AELKKEYTIVIvthnmqqAARV-----ADRTAFLLNGRLVEFGPTEQI 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
334-546 |
1.03e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.50 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFV 413
Cdd:COG4619 2 ELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSGTIASNLRQGNAQAklhelQRAANMAQASEFIERYNdsFDHEVEERSA-NFSGGQKQRLSIARGLIAKAPIL 492
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLR-----ERKFDRERALELLERLG--LPPDILDKPVeRLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHEL--PDTTTFII------AEKIvsvinADTILVLDDGKL 546
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVshdpeqIERV-----ADRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
350-499 |
1.36e-40 |
|
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: 144.33 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSG-TIASNL 428
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 429 RQGnaqAKLHELQRAANMAQASEFIERYNDSF--DHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
270-556 |
1.48e-40 |
|
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: 154.29 E-value: 1.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 270 DIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRIrEVLETEPDVKFVESGSVAPLsgsVEFDHVSFTYPDGDDPT 349
Cdd:COG1123 202 DLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAV-PRLGAARGRAAPAAAAAEPL---LEVRNLSKRYPVRGKGG 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 ---LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALRKTVSFVLQ-------- 415
Cdd:COG1123 278 vraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRRRVQMVFQdpysslnp 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 -----RAVLFSGTIASNLRQGNAQAKLHELQRAANMaqASEFIERYndsfDHEveersanFSGGQKQRLSIARGLIAKAP 490
Cdd:COG1123 358 rmtvgDIIAEPLRLHGLLSRAERRERVAELLERVGL--PPDLADRY----PHE-------LSGGQRQRVAIARALALEPK 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 491 ILILDDSTSALDAESEKKVQQALEH---ELPDTTTFI-----IAEKIvsvinADTILVLDDGKLVAQGTHEELL 556
Cdd:COG1123 425 LLILDEPTSALDVSVQAQILNLLRDlqrELGLTYLFIshdlaVVRYI-----ADRVAVMYDGRIVEDGPTEEVF 493
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
333-556 |
5.04e-40 |
|
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: 152.75 E-value: 5.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPT---KGKVKIGGQNIKDVTEAALRKT 409
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQ--RAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEF--IERYNDSFDHEveersanFSGGQKQRLSIARGL 485
Cdd:COG1123 85 IGMVFQdpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAvgLERRLDRYPHQ-------LSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 486 IAKAPILILDDSTSALDAESEKKVQQALEHELPDT-TTFIIAEKIVSVI--NADTILVLDDGKLVAQGTHEELL 556
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgTTVLLITHDLGVVaeIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
334-557 |
6.57e-40 |
|
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: 145.39 E-value: 6.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKtVSFV 413
Cdd:COG4555 3 EVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSG-TIASNLRqgnAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:COG4555 80 PDERGLYDRlTVRENIR---YFAELYGLFDEELKKRIEELIELLG--LEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINA--DTILVLDDGKLVAQGTHEELLK 557
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlcDRVVILHKGKVVAQGSLDELRE 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
333-557 |
8.64e-40 |
|
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: 146.04 E-value: 8.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD---VTEaaLRKT 409
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDeenLWE--IRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVL-----QravlFSGTIAS--------NLrqGNAQAKLHEL-QRAANMAQASEFIeryndsfDHEveerSANFSGGQ 475
Cdd:TIGR04520 79 VGMVFqnpdnQ----FVGATVEddvafgleNL--GVPREEMRKRvDEALKLVGMEDFR-------DRE----PHLLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 476 KQRLSIArGLIAKAP-ILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTH 552
Cdd:TIGR04520 142 KQRVAIA-GVLAMRPdIIILDEATSMLDPKGRKEVLETIRklNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTP 220
|
....*
gi 492039060 553 EELLK 557
Cdd:TIGR04520 221 REIFS 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-570 |
2.65e-39 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 154.42 E-value: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 3 NFKIILPYLKRYKKDVVCAIIAILVSAfsGLYqPKLleniqkALMANQKQAVLSD-----------GIWLVVLGIIAIIS 71
Cdd:PTZ00265 812 NLRIVYREIFSYKKDVTIIALSILVAG--GLY-PVF------ALLYAKYVSTLFDfanleansnkySLYILVIAIAMFIS 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 72 GIFNVYFAAKIAQGVVSDLREDTYAKI--QTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLfmqmlrlpILIVGSFI- 148
Cdd:PTZ00265 883 ETLKNYYNNVIGEKVEKTMKRRLFENIlyQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNN--------IVIFTHFIv 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 149 -FCIVIIPRFWWAPVVMVALIFGFGAYVL----------------RQMNS-----LFTKFQEMMDRISNQAQETLQGVRV 206
Cdd:PTZ00265 955 lFLVSMVMSFYFCPIVAAVLTGTYFIFMRvfairarltankdvekKEINQpgtvfAYNSDDEIFKDPSFLIQEAFYNMNT 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 207 VksFNQGPQE-----IKKFDQTSDQLNDYNIVIgywfSAIMPAFQMIAYTVIALIVYLIGKNITAHPSdiAVVSPFVNYV 281
Cdd:PTZ00265 1035 V--IIYGLEDyfcnlIEKAIDYSNKGQKRKTLV----NSMLWGFSQSAQLFINSFAYWFGSFLIRRGT--ILVDDFMKSL 1106
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 282 LTLLFTIMIAG--MTLMQFSR-ANISLGRIREVLETEPDVKFVESGSVA-----PLSGSVEFDHVSFTYPDGDD-PTLKD 352
Cdd:PTZ00265 1107 FTFLFTGSYAGklMSLKGDSEnAKLSFEKYYPLIIRKSNIDVRDNGGIRiknknDIKGKIEIMDVNFRYISRPNvPIYKD 1186
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 353 ISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD----------------------------------------------- 385
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggs 1266
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 386 -------PTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYND 458
Cdd:PTZ00265 1267 gedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPN 1346
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 459 SFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAEKIVSVINAD 536
Cdd:PTZ00265 1347 KYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASIKRSD 1426
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 492039060 537 TILVLDD----GKLV-AQGTHEELLKTSL-VYQEIFKTQK 570
Cdd:PTZ00265 1427 KIVVFNNpdrtGSFVqAHGTHEELLSVQDgVYKKYVKLAK 1466
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
18-308 |
1.14e-38 |
|
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: 143.73 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 18 VVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAvlsdgIWLVVLGII--AIISGIFN---VYFAAKIAQGVVSDLR 91
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRiIDSVIGGGLREL-----LWLLALLILgvALLRGVFRylqGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 92 EDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGF 171
Cdd:cd18542 76 NDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 172 GAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYT 251
Cdd:cd18542 156 SYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 252 VIALIVYL-----IGKNITahpsdIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18542 236 QIVLVLWVggylvINGEIT-----LGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
333-549 |
3.16e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 140.56 E-value: 3.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---- 406
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 407 RKTVSFVLQRAVLFSG-TIASNLRqgnAQAKLHELQRAANMAQASEFIERYNdsfdheVEERSANF----SGGQKQRLSI 481
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVA---LPLLLAGVSRKERRERARELLERVG------LGDRLDHRpsqlSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDT--TTFIIA---EKIVSVinADTILVLDDGKLVAQ 549
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELL-RELNRElgTTIVMVthdPELAAR--ADRVIRLRDGRIVSD 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
334-545 |
1.26e-37 |
|
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: 136.22 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDGddPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFV 413
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQravlfsgtiasnlrqgnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAPILI 493
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492039060 494 LDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGK 545
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAElaADRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
333-546 |
2.13e-37 |
|
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: 138.01 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---- 406
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 407 RKTVSFVLQRAVLFSG-TIASNLRQGnaqAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGL 485
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLERVG--LGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 486 IAKAPILILDDSTSALDAESEKKVQQALE--HELPDTTTFI------IAEKivsvinADTILVLDDGKL 546
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVvthdpeLAEY------ADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
333-550 |
3.43e-37 |
|
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: 137.64 E-value: 3.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALR 407
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQ---RAVLFSGTIASNLR---QGNAQAKLHELQRAANMAQASEFI--ERYNDSFDHEveersanFSGGQKQRL 479
Cdd:cd03257 82 KEIQMVFQdpmSSLNPRMTIGEQIAeplRIHGKLSKKEARKEAVLLLLVGVGlpEEVLNRYPHE-------LSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 480 SIARGLIAKAPILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAE--KIVSVInADTILVLDDGKLVAQG 550
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHdlGVVAKI-ADRVAVMYAGKIVEEG 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-545 |
4.26e-37 |
|
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: 136.45 E-value: 4.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDD---PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqnikdvteaalrkT 409
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVLFSGTIASNLRQGnaqaklhelqraanmaqaSEF-IERYN------------DSFDH----EVEERSANFS 472
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFG------------------KPFdEERYEkvikacalepdlEILPDgdltEIGEKGINLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 473 GGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKV-QQALEHELPDTTTFIIAEKIVSVI-NADTILVLDDGK 545
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLLLNNKTRILVTHQLQLLpHADQIVVLDNGR 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
333-556 |
5.96e-37 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 137.43 E-value: 5.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:cd03295 1 IEFENVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLrqgNAQAKLHELQRAANMAQASEFIE-------RYNDSFDHEVeersanfSGGQKQRLSIARG 484
Cdd:cd03295 80 VIQQIGLFPHmTVEENI---ALVPKLLKWPKEKIRERADELLAlvgldpaEFADRYPHEL-------SGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQA---LEHELPDTTTFI---IAEKIVSvinADTILVLDDGKLVAQGTHEELL 556
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEfkrLQQELGKTIVFVthdIDEAFRL---ADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
18-308 |
9.79e-37 |
|
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: 138.45 E-value: 9.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 18 VVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYA 96
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLlIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 97 KIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVL 176
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 177 RQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIALI 256
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 492039060 257 VYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
333-558 |
1.29e-36 |
|
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: 136.86 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDD--PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTV 410
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQ------------RAVLfsGTIASNLRQGNAQAKLHELQRAANMAqaSEFIERYndsfDHEVeersanfSGGQKQR 478
Cdd:COG1124 82 QMVFQdpyaslhprhtvDRIL--AEPLRIHGLPDREERIAELLEQVGLP--PSFLDRY----PHQL-------SGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQAL-----EHELpdttTFIiaekIVS----VIN--ADTILVLDDGKLV 547
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLkdlreERGL----TYL----FVShdlaVVAhlCDRVAVMQNGRIV 218
|
250
....*....|.
gi 492039060 548 AQGTHEELLKT 558
Cdd:COG1124 219 EELTVADLLAG 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
333-556 |
1.81e-36 |
|
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: 135.79 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPD--GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---R 407
Cdd:cd03258 2 IELKNVSKVFGDtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQRAVLFSG-TIASNLrqgnAQA-KLHELQRAANMAQASEFIERYNDSfdHEVEERSANFSGGQKQRLSIARGL 485
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENV----ALPlEIAGVPKAEIEERVLELLELVGLE--DKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 486 IAKAPILILDDSTSALDAESE-------KKVQQALehelpDTTTFIIAEKIvSVIN--ADTILVLDDGKLVAQGTHEELL 556
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTqsilallRDINREL-----GLTIVLITHEM-EVVKriCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
11-495 |
2.12e-36 |
|
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: 143.01 E-value: 2.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 11 LKRYKKDVVCAIIAILVSAFSGLYqpkLLENIQKALMANQkQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDL 90
Cdd:COG4615 8 LRESRWLLLLALLLGLLSGLANAG---LIALINQALNATG-AALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 91 REDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMqlfmqmlRLPILIVGSFIFCIVIIPRFWWAP----VVMVA 166
Cdd:COG4615 84 RLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-------RLPELLQSVALVLGCLAYLAWLSPplflLTLVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 167 LIFGFGAYVL--RQMNSLFTKFQEMMDRISNQAQETLQGVRVVK-------SFNQgpqeiKKFDQTSDQLNDYNIVIGYW 237
Cdd:COG4615 157 LGLGVAGYRLlvRRARRHLRRAREAEDRLFKHFRALLEGFKELKlnrrrrrAFFD-----EDLQPTAERYRDLRIRADTI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 238 FSAIMPAFQMIAYTVIALIVYLIGkniTAHPSDIAVVSpfvNYVLTLLFTI----MIAGMTLMqFSRANISLGRIREV-- 311
Cdd:COG4615 232 FALANNWGNLLFFALIGLILFLLP---ALGWADPAVLS---GFVLVLLFLRgplsQLVGALPT-LSRANVALRKIEELel 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 312 -LETEPDVKFVESGSVAPLS-GSVEFDHVSFTYPDGDDP---TLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP 386
Cdd:COG4615 305 aLAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 387 TKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSgtiasnlrqgnaqaKLHELQRAANMAQASEFIERYNdsFDHEVEE 466
Cdd:COG4615 385 ESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD--------------RLLGLDGEADPARARELLERLE--LDHKVSV 448
|
490 500 510
....*....|....*....|....*....|....
gi 492039060 467 RSANF-----SGGQKQRLSIARGLIAKAPILILD 495
Cdd:COG4615 449 EDGRFsttdlSQGQRKRLALLVALLEDRPILVFD 482
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
323-556 |
2.06e-35 |
|
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: 133.88 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 323 SGSVApLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVT 402
Cdd:cd03288 11 SGLVG-LGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 403 EAALRKTVSFVLQRAVLFSGTIASNLrqgNAQAKLHE--LQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLS 480
Cdd:cd03288 90 LHTLRSRLSIILQDPILFSGSIRFNL---DPECKCTDdrLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFC 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 481 IARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELL 556
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
333-565 |
3.47e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 133.77 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP---TKGKVKIGGQNIKDVTEAALRKT 409
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRA--VLFSGTIASNLRQG--NAQAKLHELQRAANMAQASEFIERYNDSfdheveeRSANFSGGQKQRLSIArGL 485
Cdd:PRK13640 86 VGIVFQNPdnQFVGATVGDDVAFGleNRAVPRPEMIKIVRDVLADVGMLDYIDS-------EPANLSGGQKQRVAIA-GI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 486 IAKAP-ILILDDSTSALDAESEKKVQQALEHELPDT--TTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVY 562
Cdd:PRK13640 158 LAVEPkIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
...
gi 492039060 563 QEI 565
Cdd:PRK13640 238 KEI 240
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
333-565 |
4.34e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.60 E-value: 4.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRA-VLFSGT-----IASNLRqgNAQAKLHELQRAANMAqasefIERYN--DSFDHEveerSANFSGGQKQRLSIArG 484
Cdd:PRK13635 86 VFQNPdNQFVGAtvqddVAFGLE--NIGVPREEMVERVDQA-----LRQVGmeDFLNRE----PHRLSGGQKQRVAIA-G 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 485 LIAKAP-ILILDDSTSALDAESEKKVQQALEH--ELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLV 561
Cdd:PRK13635 154 VLALQPdIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
....
gi 492039060 562 YQEI 565
Cdd:PRK13635 234 LQEI 237
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
333-558 |
5.20e-35 |
|
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: 131.86 E-value: 5.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALRKT 409
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVLFSG-TIASN----LRQgNAQAKLHELQRaanmaQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARG 484
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENvafpLRE-HTRLSEEEIRE-----IVLEKLEAVG--LRGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEELLKT 558
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
333-566 |
8.46e-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: 131.70 E-value: 8.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVL-FSGTIA----------SNLRQGNAQAKLHELQRAANMAQASEFIERYndsfdheVEErsanFSGGQKQRLSI 481
Cdd:COG1120 80 VPQEPPApFGLTVRelvalgryphLGLFGRPSAEDREAVEEALERTGLEHLADRP-------VDE----LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALEHelpdtttfIIAEK---IVSV---IN-----ADTILVLDDGKLVAQG 550
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRR--------LARERgrtVVMVlhdLNlaaryADRLVLLKDGRIVAQG 220
|
250
....*....|....*.
gi 492039060 551 THEELLKTSLVyQEIF 566
Cdd:COG1120 221 PPEEVLTPELL-EEVY 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
333-550 |
1.17e-34 |
|
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: 130.33 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVteAALRKTVSF 412
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRQGNAQAKLHELQRAANMAQASEFIEryndsFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03259 77 VFQDYALFPHlTVAENIAFGLKLRGVPKAEIRARVRELLELVG-----LEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 492 LILDDSTSALDAesekKVQQALEHELPDT-----TTFIIA----EKIVSVinADTILVLDDGKLVAQG 550
Cdd:cd03259 152 LLLDEPLSALDA----KLREELREELKELqrelgITTIYVthdqEEALAL--ADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
336-547 |
4.01e-33 |
|
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: 125.83 E-value: 4.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKdvtEAALRKTVSFVLQ 415
Cdd:cd03226 3 ENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 --RAVLFSGTIASNLRQGNAQAklhelqrAANMAQASEFIERYNDSFDHEVEERSanFSGGQKQRLSIARGLIAKAPILI 493
Cdd:cd03226 79 dvDYQLFTDSVREELLLGLKEL-------DAGNEQAETVLKDLDLYALKERHPLS--LSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 494 LDDSTSALDAESEKKVQQALEHELPDTTTFIIA----EKIVSVinADTILVLDDGKLV 547
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVIthdyEFLAKV--CDRVLLLANGAIV 205
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
333-556 |
5.08e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 129.04 E-value: 5.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---R 407
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQRAVLFSG-TIASN----LRqgnaQAKLHELQRAanmAQASEFIERyndsfdheV--EERSANF----SGGQK 476
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENvalpLE----IAGVPKAEIR---KRVAELLEL--------VglSDKADAYpsqlSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 477 QRLSIARGLIAKAPILILDDSTSALDaesekkvqqalehelPDTTTFI------IAEK----IV------SVIN--ADTI 538
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALD---------------PETTRSIldllkdINRElgltIVlithemDVVRriCDRV 211
|
250
....*....|....*...
gi 492039060 539 LVLDDGKLVAQGTHEELL 556
Cdd:COG1135 212 AVLENGRIVEQGPVLDVF 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
333-557 |
6.45e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.03 E-value: 6.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRA-VLFSGT-----IA-----SNLRQGNAQAKLHELQRAANMaqasefieryNDSFDHEveerSANFSGGQKQRLSI 481
Cdd:PRK13632 88 IFQNPdNQFIGAtveddIAfglenKKVPPKKMKDIIDDLAKKVGM----------EDYLDKE----PQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDTT--TFI-IAEKIVSVINADTILVLDDGKLVAQGTHEELLK 557
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIM-VDLRKTRkkTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
333-546 |
8.11e-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: 123.66 E-value: 8.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKtVSF 412
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRqgnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03230 78 LPEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHELPDTTTFII-------AEKIvsvinADTILVLDDGKL 546
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEGKTILLsshileeAERL-----CDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
333-545 |
8.29e-33 |
|
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: 123.84 E-value: 8.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE--AALRKTV 410
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSG-TIASNLRQGnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKA 489
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 490 PILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAEKIVSVIN-ADTILVLDDGK 545
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
334-550 |
1.08e-32 |
|
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: 123.70 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFV 413
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQravlfsgtiasnlrqgnaqaklhelqrAANMAQASEFIERYNDSfdheveersanFSGGQKQRLSIARGLIAKAPILI 493
Cdd:cd03214 79 PQ---------------------------ALELLGLAHLADRPFNE-----------LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 494 LDDSTSALDAESEKKVQQALeHELPDTTTFIIaekIVSV--IN-----ADTILVLDDGKLVAQG 550
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELL-RRLARERGKTV---VMVLhdLNlaaryADRVILLKDGRIVAQG 180
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
333-547 |
1.20e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.78 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE---AALRKT 409
Cdd:COG2884 2 IRFENVSKRYPGGR-EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreiPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQ--RaVLFSGTIASNLrqgnAQA-KLHELQRAANMAQASEFIERYN-----DSFDHEVeersanfSGGQKQRLSI 481
Cdd:COG2884 81 IGVVFQdfR-LLPDRTVYENV----ALPlRVTGKSRKEIRRRVREVLDLVGlsdkaKALPHEL-------SGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALEhELPDT-TTFIIA---EKIVSVINAdTILVLDDGKLV 547
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLE-EINRRgTTVLIAthdLELVDRMPK-RVLELEDGRLV 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
333-556 |
2.83e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.43 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVteaalRKTVSF 412
Cdd:COG1121 7 IELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRA------------VLFSGTIASNLRQGNAQAKLHEL-QRAANMAQASEFIERyndsfdheveeRSANFSGGQKQRL 479
Cdd:COG1121 80 VPQRAevdwdfpitvrdVVLMGRYGRRGLFRRPSRADREAvDEALERVGLEDLADR-----------PIGELSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 480 SIARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDTTTFIIaekIVS-----VI-NADTILVLDDGkLVAQGTHE 553
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELL-RELRREGKTIL---VVThdlgaVReYFDRVLLLNRG-LVAHGPPE 223
|
...
gi 492039060 554 ELL 556
Cdd:COG1121 224 EVL 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
333-558 |
6.03e-32 |
|
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: 123.55 E-value: 6.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALRKT 409
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVLFSG-TIASN----LRQgnaQAKL--HELQRAANMAQA----SEFIERYndsfdheveerSANFSGGQKQR 478
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENvafpLRE---HTDLseAEIRELVLEKLElvglPGAADKM-----------PSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQ---ALEHELpDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEE 554
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDElirELRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
....
gi 492039060 555 LLKT 558
Cdd:COG1127 229 LLAS 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
333-544 |
1.83e-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: 122.51 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqniKDVTEAALRktV 410
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG---KPVTGPGPD--R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFs-gTIASNLRQGnaqAKLHELQRAANMAQASEFIERYN-----DSFDHEVeersanfSGGQKQRLSIARG 484
Cdd:COG1116 83 GVVFQEPALLpwlTVLDNVALG---LELRGVPKAERRERARELLELVGlagfeDAYPHQL-------SGGMRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQALE---HELPDTTTFI---IAEkivSVINADTILVLDDG 544
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLrlwQETGKTVLFVthdVDE---AVFLADRVVVLSAR 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
333-541 |
2.41e-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: 121.04 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAalrktV 410
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFS-GTIASNLRQGnaqAKLHELQRAANMAQASEFIER-----YNDSFDHEVeersanfSGGQKQRLSIARG 484
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG---LELQGVPKAEARERAEELLELvglsgFENAYPHQL-------SGGMRQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQALE---HELPDTTTFI---IAEkivSVINADTILVL 541
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLdiwRETGKTVLLVthdIDE---AVFLADRVVVL 205
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
333-555 |
2.42e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 122.09 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRK---T 409
Cdd:COG3638 3 LELRNLSKRYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQ-----------RAVLfSGTIAsnlRQGNAQAKLHeLQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQR 478
Cdd:COG3638 82 IGMIFQqfnlvprlsvlTNVL-AGRLG---RTSTWRSLLG-LFPPEDRERALEALERVG--LADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHelpdtttfiIAE--KIVSVIN----------ADTILVLDDGKL 546
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRR---------IARedGITVVVNlhqvdlarryADRIIGLRDGRV 225
|
....*....
gi 492039060 547 VAQGTHEEL 555
Cdd:COG3638 226 VFDGPPAEL 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
198-543 |
1.55e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 127.84 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 198 QETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFS---AIMPAFQMIAY-------TVIalivyLIGKNITAH 267
Cdd:PTZ00265 240 EEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESlhiGMINGFILASYafgfwygTRI-----IISDLSNQQ 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 268 PSD----IAVVSPFVNYVLTL-LFTIMIAGMTlmQFSRANISLGRIREVLETEPDVKFVESGSVAPLSGSVEFDHVSFTY 342
Cdd:PTZ00265 315 PNNdfhgGSVISILLGVLISMfMLTIILPNIT--EYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHY 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 343 PDGDDPTL-KDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIG-GQNIKDVTEAALRKTVSFVLQRAVLF 420
Cdd:PTZ00265 393 DTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLF 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SGTIASNLR---------------------------------------------QGNAQAKLHELQRAANMAQASE---- 451
Cdd:PTZ00265 473 SNSIKNNIKyslyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsNTTDSNELIEMRKNYQTIKDSEvvdv 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 452 --------FIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHEL--PDTT 521
Cdd:PTZ00265 553 skkvlihdFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRI 632
|
410 420
....*....|....*....|..
gi 492039060 522 TFIIAEKIVSVINADTILVLDD 543
Cdd:PTZ00265 633 TIIIAHRLSTIRYANTIFVLSN 654
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
333-545 |
1.95e-30 |
|
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: 117.97 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAaLRKTVSF 412
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-YRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRqgnAQAKLHelQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:COG4133 80 LGHADGLKPElTVRENLR---FWAALY--GLRADREAIDEALEAVG--LAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGK 545
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGDFK 206
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
18-267 |
4.66e-30 |
|
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: 119.45 E-value: 4.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 18 VVCAIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLsdgiWLVVLGIIAI-----ISGIFNVYFAAKIAQGVVSDLRE 92
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEAL----LLVPLAIIGLfllrgLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 93 DTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFG 172
Cdd:cd18552 77 DLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 173 AYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTV 252
Cdd:cd18552 157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIA 236
|
250
....*....|....*
gi 492039060 253 IALIVYLIGKNITAH 267
Cdd:cd18552 237 IALVLWYGGYQVISG 251
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
331-572 |
4.73e-30 |
|
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: 119.19 E-value: 4.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 331 GSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDpTKGKVKIGGQNIKDVTEAALRKTV 410
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSGTIASNLrQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNL-DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 491 ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELL-KTSLVYQEIFKTQ 569
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLnEKSHFKQAISPSD 238
|
...
gi 492039060 570 KGK 572
Cdd:cd03289 239 RLK 241
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
331-555 |
6.81e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 120.56 E-value: 6.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 331 GSVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqniKDVTEAALRK-T 409
Cdd:COG3839 2 ASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVTDLPPKDrN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVLF-----SGTIASNLR-QGNAQAKLHE-LQRAANMAQASEFIERyndsfdheveeRSANFSGGQKQRLSIA 482
Cdd:COG3839 77 IAMVFQSYALYphmtvYENIAFPLKlRKVPKAEIDRrVREAAELLGLEDLLDR-----------KPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 483 RGLIAKAPILILDDSTSALDAE------SE-KKVQQALEhelpdtTTFII-------AEKIvsvinADTILVLDDGKLVA 548
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRLG------TTTIYvthdqveAMTL-----ADRIAVMNDGRIQQ 214
|
....*..
gi 492039060 549 QGTHEEL 555
Cdd:COG3839 215 VGTPEEL 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
350-556 |
1.24e-29 |
|
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: 117.74 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL----RKTVSFVLQRAVLFSG-TI 424
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 ASNLRQGNAQAKLHELQRAANMAQASEFI--ERYNDSFDHEVeersanfSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVglEGWEHKYPDEL-------SGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 503 AESEKKVQQ---ALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELL 556
Cdd:cd03294 193 PLIRREMQDellRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
332-555 |
3.84e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.66 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVtEAALRKtVS 411
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-PPEKRN-VG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSG-TIASN----LR-QGNAQAKLHEL-QRAANMAQASEFIERYndsfDHEVeersanfSGGQKQRLSIARG 484
Cdd:COG3842 81 MVFQDYALFPHlTVAENvafgLRmRGVPKAEIRARvAELLELVGLEGLADRY----PHQL-------SGGQQQRVALARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 485 LIAKAPILILDDSTSALDAE------SE-KKVQQALEhelpdtTTFIIA----EKIVSVinADTILVLDDGKLVAQGTHE 553
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKlreemrEElRRLQRELG------ITFIYVthdqEEALAL--ADRIAVMNDGRIEQVGTPE 221
|
..
gi 492039060 554 EL 555
Cdd:COG3842 222 EI 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
160-568 |
1.48e-28 |
|
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: 121.59 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 160 APVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVK------SFNQGPQEIKKFDQTSDQLNDYNIV 233
Cdd:TIGR00957 462 AGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKlyawelAFLDKVEGIRQEELKVLKKSAYLHA 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 234 IGYwFSAIMPAFqMIAYTVIALIVYLIGKNItahpsdIAVVSPFVNYVL--TLLFTIMIAGMTLMQFSRANISLGRIREV 311
Cdd:TIGR00957 542 VGT-FTWVCTPF-LVALITFAVYVTVDENNI------LDAEKAFVSLALfnILRFPLNILPMVISSIVQASVSLKRLRIF 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 312 L---ETEPDVkfVESGSVAPLSG-SVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPT 387
Cdd:TIGR00957 614 LsheELEPDS--IERRTIKPGEGnSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKV 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 388 KGKVKIGGqnikdvteaalrkTVSFVLQRAVLFSGTIASNLRQGNA-QAKLHE--LQRAANMAQasefIERYNDSFDHEV 464
Cdd:TIGR00957 692 EGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKAlNEKYYQqvLEACALLPD----LEILPSGDRTEI 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 465 EERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQAL---EHELPDTTTFIIAEKIVSVINADTILVL 541
Cdd:TIGR00957 755 GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVM 834
|
410 420
....*....|....*....|....*..
gi 492039060 542 DDGKLVAQGTHEELLKTSLVYQEIFKT 568
Cdd:TIGR00957 835 SGGKISEMGSYQELLQRDGAFAEFLRT 861
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
332-563 |
2.03e-28 |
|
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: 113.59 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikDVTEAALRK-TV 410
Cdd:cd03296 2 SIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE---DATDVPVQErNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSG-TIASNLRQG-------------NAQAKLHELQRaanMAQASEFIERYndsfdheveerSANFSGGQK 476
Cdd:cd03296 77 GFVFQHYALFRHmTVFDNVAFGlrvkprserppeaEIRAKVHELLK---LVQLDWLADRY-----------PAQLSGGQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 477 QRLSIARGLIAKAPILILDDSTSALDAESEKKVQ---QALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHE 553
Cdd:cd03296 143 QRVALARALAVEPKVLLLDEPFGALDAKVRKELRrwlRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPD 222
|
250
....*....|...
gi 492039060 554 ELL---KTSLVYQ 563
Cdd:cd03296 223 EVYdhpASPFVYS 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
334-550 |
2.58e-28 |
|
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: 112.24 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVteaalRKTVSFV 413
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRA-------------VLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERyndsfdheveeRSANFSGGQKQRLS 480
Cdd:cd03235 74 PQRRsidrdfpisvrdvVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADR-----------QIGELSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 481 IARGLIAKAPILILDDSTSALDAESEKKVQQALEhELPDT--TTFIIAEKIVSVIN-ADTILVLdDGKLVAQG 550
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR-ELRREgmTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
334-555 |
3.32e-28 |
|
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: 113.05 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---RKTV 410
Cdd:cd03256 2 EVENLSKTYPNGK-KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQ-----------RAVLfSGTIA--SNLRQGNAQAKLHELQRAAnmaqasEFIERYNdsFDHEVEERSANFSGGQKQ 477
Cdd:cd03256 81 GMIFQqfnlierlsvlENVL-SGRLGrrSTWRSLFGLFPKEEKQRAL------AALERVG--LLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 478 RLSIARGLIAKAPILILDDSTSALDAESEKKVQQAL-----EHELpdttTFIIAEKIVSVI--NADTILVLDDGKLVAQG 550
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrinrEEGI----TVIVSLHQVDLAreYADRIVGLKDGRIVFDG 227
|
....*
gi 492039060 551 THEEL 555
Cdd:cd03256 228 PPAEL 232
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
21-308 |
8.65e-28 |
|
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: 113.28 E-value: 8.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 21 AIIAILVSAFSGLYQPKLLENIQKALmanQKQAVLSDGIWLVVLGI--IAIISGIFNV---YFAAKIAQGVVSDLREDTY 95
Cdd:cd18541 4 GILFLILVDLLQLLIPRIIGRAIDAL---TAGTLTASQLLRYALLIllLALLIGIFRFlwrYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 96 AKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYV 175
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 176 LRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIAL 255
Cdd:cd18541 161 GKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 492039060 256 IVYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18541 241 VLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
333-556 |
9.08e-28 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 111.62 E-value: 9.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI--KDVTEAALRKTV 410
Cdd:COG1126 2 IEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSG-TIASNLRQgnAQAKLHELQRAANMAQASEFIERYN--DSFDHeveeRSANFSGGQKQRLSIARGLIA 487
Cdd:COG1126 80 GMVFQQFNLFPHlTVLENVTL--APIKVKKMSKAEAEERAMELLERVGlaDKADA----YPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 488 KAPILILDDSTSALDAESEKKVQQALEhELPDT-TTFII-------AEKIvsvinADTILVLDDGKLVAQGTHEELL 556
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMR-DLAKEgMTMVVvthemgfAREV-----ADRVVFMDGGRIVEEGPPEEFF 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
333-555 |
1.20e-27 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 110.67 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAlRKTVSF 412
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA-RQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRqgnAQAKLHELQRAANMAQASEFIERYNdSFDHEvEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03263 80 CPQFDALFDElTVREHLR---FYARLKGLPKSEIKEEVELLLRVLG-LTDKA-NKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHELPDTTtfII--------AEKIvsvinADTILVLDDGKLVAQGTHEEL 555
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKGRS--IIltthsmdeAEAL-----CDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
333-550 |
2.26e-27 |
|
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: 109.59 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdpTLKDISFKIKPGqMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEaALRKTVSF 412
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTIAsnLRQGNAQAKLHELQRAANMAQASEFIERYNdSFDHEvEERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03264 77 LPQEFGVYPNFTV--REFLDYIAWLKGIPSKEVKARVDEVLELVN-LGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 493 ILDDSTSALDAESEKKVQQALEhELPDTTTFIIAEKIVSVI--NADTILVLDDGKLVAQG 550
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLS-ELGEDRIVILSTHIVEDVesLCNQVAVLNKGKLVFEG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
333-546 |
2.99e-27 |
|
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: 109.54 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAA--LRKTV 410
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSG-TIASNLRQgnAQAKLHELQRAANMAQASEFIERYndSFDHEVEERSANFSGGQKQRLSIARGLIAKA 489
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENITL--APIKVKGMSKAEAEERALELLEKV--GLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 490 PILILDDSTSALDAESEKKVQQALEHELPDTTTFII-------AEKIvsvinADTILVLDDGKL 546
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVvthemgfAREV-----ADRVIFMDDGRI 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
165-567 |
2.99e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 117.38 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 165 VALIFG---------FGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVK------SFNQGPQEIKkfdqtSDQLNd 229
Cdd:PLN03232 441 VASLFGslilfllipLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKcyawekSFESRIQGIR-----NEELS- 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 230 ynivigyWF--SAIMPAFQMIAYTVIALIVYLIGKNI-TAHPSDIAVVSPFVNYVL--TLLFTIMIAGMTLMQFSRANIS 304
Cdd:PLN03232 515 -------WFrkAQLLSAFNSFILNSIPVVVTLVSFGVfVLLGGDLTPARAFTSLSLfaVLRSPLNMLPNLLSQVVNANVS 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 305 LGRIREVLETEPDVkFVESGSVAPLSGSVEFDHVSFTYPDG-DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIarl 383
Cdd:PLN03232 588 LQRIEELLLSEERI-LAQNPPLQPGAPAISIKNGYFSWDSKtSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM--- 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 384 ydptkgkvkIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGnAQAKLHELQRAANMAQASEFIERYNDSFDHE 463
Cdd:PLN03232 664 ---------LGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFG-SDFESERYWRAIDVTALQHDLDLLPGRDLTE 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 464 VEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKV-QQALEHELPDTTTFIIAEKIVSVINADTILVLD 542
Cdd:PLN03232 734 IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVS 813
|
410 420
....*....|....*....|....*
gi 492039060 543 DGKLVAQGTHEELLKTSLVYQEIFK 567
Cdd:PLN03232 814 EGMIKEEGTFAELSKSGSLFKKLME 838
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
106-572 |
3.04e-27 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 117.32 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 106 IKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSfIFCIVIIPRFWWAPVVMVALIF-GFGAYVLRQMNSLFT 184
Cdd:TIGR01271 976 LNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGA-IFVVSVLQPYIFIAAIPVAVIFiMLRAYFLRTSQQLKQ 1054
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 185 KFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTsdqlndYNIVIGYWFS--AIMPAFQM----------IAYTV 252
Cdd:TIGR01271 1055 LESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKA------LNLHTANWFLylSTLRWFQMridiifvfffIAVTF 1128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 253 IALIVYLIGknitahPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRaniSLGRIREVLETEP---------------D 317
Cdd:TIGR01271 1129 IAIGTNQDG------EGEVGIILTLAMNILSTLQWAVNSSIDVDGLMR---SVSRVFKFIDLPQeeprpsggggkyqlsT 1199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 318 VKFVESGSVA---PLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDpTKGKVKIG 394
Cdd:TIGR01271 1200 VLVIENPHAQkcwPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQID 1278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 395 GQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLrQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGG 474
Cdd:TIGR01271 1279 GVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL-DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNG 1357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 475 QKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEE 554
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQK 1437
|
490
....*....|....*....
gi 492039060 555 LL-KTSLVYQEIFKTQKGK 572
Cdd:TIGR01271 1438 LLnETSLFKQAMSAADRLK 1456
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
18-288 |
3.86e-27 |
|
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: 110.81 E-value: 3.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 18 VVCAIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLSDGIWLVVLGIIAIISGIFN---VYFAAKIAQGVVSDLREDT 94
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSflqSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 95 YAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAY 174
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 175 VLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIA 254
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 492039060 255 LIVYLIGKNITAHPSDIAVVSPFVNYVLTLLFTI 288
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
325-566 |
3.88e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 117.19 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 325 SVAP---LSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDV 401
Cdd:PTZ00243 1298 SAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 402 TEAALRKTVSFVLQRAVLFSGTIASNLrQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSI 481
Cdd:PTZ00243 1378 GLRELRRQFSMIPQDPVLFDGTVRQNV-DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCM 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 482 ARGLIAKAPILIL-DDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSl 560
Cdd:PTZ00243 1457 ARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR- 1535
|
....*.
gi 492039060 561 vyQEIF 566
Cdd:PTZ00243 1536 --QSIF 1539
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
333-555 |
9.08e-27 |
|
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: 108.48 E-value: 9.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVteAALRKTVSF 412
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL--PPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRQGNAQAKLHELQRAANMAQASEFI--ERYNDSFDHEVeersanfSGGQKQRLSIARGLIAKA 489
Cdd:cd03300 77 VFQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALDLVqlEGYANRKPSQL-------SGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 490 PILILDDSTSALDAESEKKVQ---QALEHELpdTTTFIIA----EKIVSVinADTILVLDDGKLVAQGTHEEL 555
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQlelKRLQKEL--GITFVFVthdqEEALTM--SDRIAVMNKGKIQQIGTPEEI 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
333-556 |
1.21e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 109.31 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE-AALRKTVS 411
Cdd:PRK13644 2 IRLENVSYSYPDGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRA-VLFSG-TIASNLRQGNAQAKLH--ELQRAANMAQASEFIERYndsfdhevEERS-ANFSGGQKQRLSIArGLI 486
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKY--------RHRSpKTLSGGQGQCVALA-GIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 487 AKAP-ILILDDSTSALDAESEKKVQQALE--HELPDTTTFiIAEKIVSVINADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK13644 152 TMEPeCLIFDEVTSMLDPDSGIAVLERIKklHEKGKTIVY-ITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
300-532 |
1.64e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 113.75 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 300 RANIS-LGRIREVLETEPDVKFVESGSVAPLSGSVEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQ 378
Cdd:COG4178 329 RATVDrLAGFEEALEAADALPEAASRIETSEDGALALEDLTLRTPDGR-PLLEDLSLSLKPGERLLITGPSGSGKSTLLR 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 379 LIARLYDPTKGKVkiggqnikDVTEAAlrkTVSFVLQRAVLFSGTIASNLR--QGNAQAKLHELQRAANMAQASEFIERY 456
Cdd:COG4178 408 AIAGLWPYGSGRI--------ARPAGA---RVLFLPQRPYLPLGTLREALLypATAEAFSDAELREALEAVGLGHLAERL 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 457 ndsfdHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTtfiiaekIVSV 532
Cdd:COG4178 477 -----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTT-------VISV 540
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
333-550 |
1.67e-26 |
|
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: 107.30 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRktVSF 412
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR--IGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRqgnAQAKLHELQRAANMaqasEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03268 77 LIEAPGFYPNlTARENLR---LLARLLGIRKKRID----EVLDVVG--LKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 492 LILDDSTSALDAESEKKVQQALeHELPDT-TTFIIAEKIVSVIN--ADTILVLDDGKLVAQG 550
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELI-LSLRDQgITVLISSHLLSEIQkvADRIGIINKGKLIEEG 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
337-557 |
1.68e-26 |
|
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: 110.14 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 337 HVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP---TKGKVKIGGQNIKDVTEAALRK----- 408
Cdd:COG0444 8 KVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 409 ----------------TVSFVLQRAVLFSGtiasNLRQGNAQAKLHELQRAANMAQASEFIERYndsfDHEveersanFS 472
Cdd:COG0444 88 iqmifqdpmtslnpvmTVGDQIAEPLRIHG----GLSKAEARERAIELLERVGLPDPERRLDRY----PHE-------LS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 473 GGQKQRLSIARGLIAKAPILILDDSTSALDAEsekkVQ-QALE------HELpDTTT-FI-----IAEKIvsvinADTIL 539
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVT----IQaQILNllkdlqREL-GLAIlFIthdlgVVAEI-----ADRVA 222
|
250
....*....|....*...
gi 492039060 540 VLDDGKLVAQGTHEELLK 557
Cdd:COG0444 223 VMYAGRIVEEGPVEELFE 240
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
352-502 |
1.72e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 110.21 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 352 DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---RKTVSFVLQ------------- 415
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQdpyaslnprmtvg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 RAVLFSGTIASNLRQGNAQAKLHELqraanMAQ---ASEFIERYndsfDHEveersanFSGGQKQRLSIARGLIAKAPIL 492
Cdd:COG4608 116 DIIAEPLRIHGLASKAERRERVAEL-----LELvglRPEHADRY----PHE-------FSGGQRQRIGIARALALNPKLI 179
|
170
....*....|
gi 492039060 493 ILDDSTSALD 502
Cdd:COG4608 180 VCDEPVSALD 189
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
333-555 |
1.94e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.01 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL--RKTV 410
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRA--VLFSGTIASNLRQG--NAQAKLHELQRAANMAQASEFIERYNDSFDHeveersaNFSGGQKQRLSIArGLI 486
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEALKAVGMEGFENKPPH-------HLSGGQKKRVAIA-GIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 487 AKAP-ILILDDSTSALDAESEKKVQQALeHELPDT-TTFIIAEKIVSV--INADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK13639 153 AMKPeIIVLDEPTSGLDPMGASQIMKLL-YDLNKEgITIIISTHDVDLvpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
164-565 |
7.12e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 113.29 E-value: 7.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 164 MVALIFGFGAYVLRQMNSLfTK--FQEMMDRISnQAQETLQGVRVVK------SFNQGPQEIKkfdqtSDQLNdynivig 235
Cdd:PLN03130 449 MLVLMFPIQTFIISKMQKL-TKegLQRTDKRIG-LMNEVLAAMDTVKcyawenSFQSKVQTVR-----DDELS------- 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 236 yWF--SAIMPAFQM-------IAYTVIALIVY-LIGKNITahPSDiAVVSPFVNYVLTL-LFtiMIAGMtLMQFSRANIS 304
Cdd:PLN03130 515 -WFrkAQLLSAFNSfilnsipVLVTVVSFGVFtLLGGDLT--PAR-AFTSLSLFAVLRFpLF--MLPNL-ITQAVNANVS 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 305 LGRIREVLETEPDVkFVESGSVAPLSGSVEFDHVSFTY-PDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARL 383
Cdd:PLN03130 588 LKRLEELLLAEERV-LLPNPPLEPGLPAISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGE 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 384 YDPTKGkvkiggqnikdvTEAALRKTVSFVLQRAVLFSGTIASNLRQGnaqaklhelqraanmaqaSEF-IERYNDSFD- 461
Cdd:PLN03130 667 LPPRSD------------ASVVIRGTVAYVPQVSWIFNATVRDNILFG------------------SPFdPERYERAIDv 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 462 ---------------HEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKV-QQALEHELPDTTTFII 525
Cdd:PLN03130 717 talqhdldllpggdlTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLV 796
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 492039060 526 AEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEI 565
Cdd:PLN03130 797 TNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
334-556 |
7.97e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.99 E-value: 7.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDgddpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDvTEAALRKtVSFV 413
Cdd:COG3840 3 RLDDLTYRYGD----FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAERP-VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSG-TIASNLRQG-NAQAKLHELQRaanmAQASEFIERYNDSfdhEVEER-SANFSGGQKQRLSIARGLIAKAP 490
Cdd:COG3840 77 FQENNLFPHlTVAQNIGLGlRPGLKLTAEQR----AQVEQALERVGLA---GLLDRlPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 491 ILILDDSTSALDaesekkvqQALEHELPDTTTFIIAEKIVSVIN-----------ADTILVLDDGKLVAQGTHEELL 556
Cdd:COG3840 150 ILLLDEPFSALD--------PALRQEMLDLVDELCRERGLTVLMvthdpedaariADRVLLVADGRIAADGPTAALL 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
333-551 |
9.39e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 108.35 E-value: 9.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKT- 409
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 --VSFVLQRAVLFSG-TIASN----LRQGNA-----QAKLHELqraANMAQASEFIERYndsfdheveerSANFSGGQKQ 477
Cdd:PRK11153 82 rqIGMIFQHFNLLSSrTVFDNvalpLELAGTpkaeiKARVTEL---LELVGLSDKADRY-----------PAQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 478 RLSIARGLIAKAPILILDDSTSALDAESEKKVQQALE---HELPDTTTFIIAEkiVSVIN--ADTILVLDDGKLVAQGT 551
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKdinRELGLTIVLITHE--MDVVKriCDRVAVIDAGRLVEQGT 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
344-558 |
9.65e-26 |
|
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: 105.88 E-value: 9.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 344 DGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqniKDVTE-AALRKTVSFVLQRAVLFSG 422
Cdd:cd03299 9 DWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG---KDITNlPPEKRDISYVPQNYALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 -TIASNLRQGNAQAKLHELQRAANMAQASEFIeryndSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSAL 501
Cdd:cd03299 86 mTVYKNIAYGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 502 DAESEKKVQQALE--HELPDTTTFIIAEKIVSV-INADTILVLDDGKLVAQGTHEELLKT 558
Cdd:cd03299 161 DVRTKEKLREELKkiRKEFGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
332-555 |
1.10e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.63 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikDVTEAALR-KTV 410
Cdd:PRK10851 2 SIEIANIKKSF--GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLHARdRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSG-TIASNLRQG----------NAQAKLHELQRAANMAQASEFIERYndsfdheveerSANFSGGQKQRL 479
Cdd:PRK10851 77 GFVFQHYALFRHmTVFDNIAFGltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRY-----------PAQLSGGQKQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 480 SIARGLIAKAPILILDDSTSALDAESEKKVQ---QALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRrwlRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
333-565 |
1.34e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 106.37 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpDGDDP-TLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVS 411
Cdd:PRK13648 8 IVFKNVSFQY-QSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAV-LFSGTI-----ASNLRqgNAQAKLHELQRAANmaQASEFIERYNDSfDHEVEersaNFSGGQKQRLSIArGL 485
Cdd:PRK13648 87 IVFQNPDnQFVGSIvkydvAFGLE--NHAVPYDEMHRRVS--EALKQVDMLERA-DYEPN----ALSGGQKQRVAIA-GV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 486 IAKAP-ILILDDSTSALDAESEKKVQQALEH--ELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVY 562
Cdd:PRK13648 157 LALNPsVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
...
gi 492039060 563 QEI 565
Cdd:PRK13648 237 TRI 239
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
348-509 |
1.74e-25 |
|
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: 104.82 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKI--GGQNIkDVTEA------ALRK-TVSFVLQ--R 416
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWV-DLAQAspreilALRRrTIGYVSQflR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 417 AVLFSGTI---ASNLRQgnaqaklHELQRAANMAQASEFIERYNdsfdheVEER-----SANFSGGQKQRLSIARGLIAK 488
Cdd:COG4778 104 VIPRVSALdvvAEPLLE-------RGVDREEARARARELLARLN------LPERlwdlpPATFSGGEQQRVNIARGFIAD 170
|
170 180
....*....|....*....|.
gi 492039060 489 APILILDDSTSALDAESEKKV 509
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVV 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
334-548 |
2.62e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 110.58 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL----R 407
Cdd:PRK10535 6 ELKDIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQRAVLFSG-TIASNLRqgnAQAKLHELQRAANMAQASEFIERYndSFDHEVEERSANFSGGQKQRLSIARGLI 486
Cdd:PRK10535 86 EHFGFIFQRYHLLSHlTAAQNVE---VPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 487 AKAPILILDDSTSALDAESEKKVqQALEHELPDT--TTFIIAEKIVSVINADTILVLDDGKLVA 548
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEV-MAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
333-557 |
3.41e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.49 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdP----TLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---- 404
Cdd:PRK13634 3 ITFQKVEHRYQYKT-PferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 405 ALRKTVSFVLQ--RAVLFSGTIASNLRQG-------NAQAKlhelqraanmAQASEFIERYndSFDHEVEERSA-NFSGG 474
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGpmnfgvsEEDAK----------QKAREMIELV--GLPEELLARSPfELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 475 QKQRLSIArGLIAKAP-ILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQG 550
Cdd:PRK13634 150 QMRRVAIA-GVLAMEPeVLVLDEPTAGLDPKGRKEMMEMFYklHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQG 228
|
....*..
gi 492039060 551 THEELLK 557
Cdd:PRK13634 229 TPREIFA 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
350-556 |
3.86e-25 |
|
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: 109.39 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLyDPTKGKVKIGGQNIKDVTEAALRKtvsfvLQRA--VLF------- 420
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRP-----LRRRmqVVFqdpfgsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 ------SGTIASNLRqgnaqakLHEL-----QRAANMAQA-------SEFIERYndsfDHEveersanFSGGQKQRLSIA 482
Cdd:COG4172 376 sprmtvGQIIAEGLR-------VHGPglsaaERRARVAEAleevgldPAARHRY----PHE-------FSGGQRQRIAIA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 483 RGLIAKAPILILDDSTSALDAESEKKV-------QQalEHELpdTTTFIIAEkiVSVINA--DTILVLDDGKLVAQGTHE 553
Cdd:COG4172 438 RALILEPKLLVLDEPTSALDVSVQAQIldllrdlQR--EHGL--AYLFISHD--LAVVRAlaHRVMVMKDGKVVEQGPTE 511
|
...
gi 492039060 554 ELL 556
Cdd:COG4172 512 QVF 514
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
332-550 |
5.43e-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: 102.24 E-value: 5.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYPDGDDPT----LKDISFKIKPGQMVGIVGATGAGKSTLAQLIA--RLYDPTKGKVKIGGQNIKDVTeaa 405
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKRS--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQRAVLFSG-TIASNLRqgnAQAKLHELqraanmaqasefieryndsfdheveersanfSGGQKQRLSIARG 484
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLM---FAAKLRGL-------------------------------SGGERKRVSIALE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFII-----AEKIVSVinADTILVLDDGKLVAQG 550
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICsihqpSSEIFEL--FDKLLLLSQGRVIYFG 194
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
336-563 |
7.88e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 103.66 E-value: 7.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKtvsfvlQ 415
Cdd:COG4559 5 ENLSVRL--GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELAR------R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 RAVL---------FS-------GTIAsnlrQGNAQAKLHELQRAAnMAQA--SEFIER-YNDsfdheveersanFSGGQK 476
Cdd:COG4559 77 RAVLpqhsslafpFTveevvalGRAP----HGSSAAQDRQIVREA-LALVglAHLAGRsYQT------------LSGGEQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 477 QRLSIARGLI-------AKAPILILDDSTSALDaesekkvqqaLEHELpdtTTFII----AEKIVSVI------N----- 534
Cdd:COG4559 140 QRVQLARVLAqlwepvdGGPRWLFLDEPTSALD----------LAHQH---AVLRLarqlARRGGGVVavlhdlNlaaqy 206
|
250 260
....*....|....*....|....*....
gi 492039060 535 ADTILVLDDGKLVAQGTHEELLKTSLVYQ 563
Cdd:COG4559 207 ADRILLLHQGRLVAQGTPEEVLTDELLER 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
333-547 |
1.02e-24 |
|
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: 102.33 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVtEAALRKtVSF 412
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL-PPKDRD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRQGNAQAKLHE------LQRAANMAQASEFIERYndsfdheveerSANFSGGQKQRLSIARGL 485
Cdd:cd03301 77 VFQNYALYPHmTVYDNIAFGLKLRKVPKdeiderVREVAELLQIEHLLDRK-----------PKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 486 IAKAPILILDDSTSALDAE------SE-KKVQQALEHelpdTTTFIIAEKIVSVINADTILVLDDGKLV 547
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKlrvqmrAElKRLQQRLGT----TTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
345-556 |
1.19e-24 |
|
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: 102.13 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDV-TEAALRKTVSFVLQRAVLFSG- 422
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERARAGIGYVPEGRRIFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 TIASNLRQGnAQAKLHElQRAANMAQASEFI----ERYNdsfdheveERSANFSGGQKQRLSIARGLIAKAPILILDDST 498
Cdd:cd03224 91 TVEENLLLG-AYARRRA-KRKARLERVYELFprlkERRK--------QLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 499 SALdaeSEKKVQQALE--HELPDT-TTFIIAEKIVSVI--NADTILVLDDGKLVAQGTHEELL 556
Cdd:cd03224 161 EGL---APKIVEEIFEaiRELRDEgVTILLVEQNARFAleIADRAYVLERGRVVLEGTAAELL 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
332-557 |
1.33e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.97 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYPDG---DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI--KDVTEAAL 406
Cdd:PRK13637 2 SIKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 407 RKTVSFVLQ--RAVLFSGTIASNLRQGNAQAKLHE------LQRAANMAQASefIERYNDSFDHEVeersanfSGGQKQR 478
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIEKDIAFGPINLGLSEeeienrVKRAMNIVGLD--YEDYKDKSPFEL-------SGGQKRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIArGLIAKAP-ILILDDSTSALDAESEKKV--QQALEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEE 554
Cdd:PRK13637 153 VAIA-GVVAMEPkILILDEPTAGLDPKGRDEIlnKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
...
gi 492039060 555 LLK 557
Cdd:PRK13637 232 VFK 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
350-557 |
1.79e-24 |
|
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: 102.13 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL-RKTVSFVLQRAVLFSG-TIASN 427
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 428 LRQGnAQAKLHEL--------QRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:cd03219 96 VMVA-AQARTGSGlllararrEEREARERAEELLERVG--LADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 500 ALDAESEKKVQQALEhELPDT-TTFIIAE---KIVSVInADTILVLDDGKLVAQGTHEELLK 557
Cdd:cd03219 173 GLNPEETEELAELIR-ELRERgITVLLVEhdmDVVMSL-ADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
333-555 |
1.85e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 102.81 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD--P---TKGKVKIGGQNI--KDVTEAA 405
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQRAVLFSGTIASNLRQGnaqAKLHELQRAANMAqasEFIERyndS------FDhEVEER---SA-NFSGGQ 475
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNVAYG---LRLHGIKSKSELD---EIVEE---SlrkaalWD-EVKDRlkkSAlGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 476 KQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDTTTFII-------AEKIvsvinADTILVLDDGKLVA 548
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELI-LELKKDYTIVIvthnmqqAARV-----SDYTAFFYLGELVE 233
|
....*..
gi 492039060 549 QGTHEEL 555
Cdd:COG1117 234 FGPTEQI 240
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
332-559 |
2.14e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.37 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYPDG---DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---- 404
Cdd:PRK13641 2 SIKFENVDYIYSPGtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 405 ALRKTVSFVLQ--RAVLFSGTIASNLRQGNAQAKLHElQRAANmaQASEFIERYndSFDHEVEERSA-NFSGGQKQRLSI 481
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE-DEAKE--KALKWLKKV--GLSEDLISKSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 482 ArGLIAKAP-ILILDDSTSALDAESEKKVQQA-LEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK13641 157 A-GVMAYEPeILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSD 235
|
.
gi 492039060 559 S 559
Cdd:PRK13641 236 K 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
333-559 |
2.26e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.09 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD--VTEAALRKTV 410
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSGTIA-SNLRQGNAQAKlhELQRAANMAQASEFIERYNdsfdheVEERSANF----SGGQKQRLSIARGL 485
Cdd:PRK09493 80 GMVFQQFYLFPHLTAlENVMFGPLRVR--GASKEEAEKQARELLAKVG------LAERAHHYpselSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 486 IAKAPILILDDSTSALDAESEK---KVQQALEHElpdTTTFII-------AEKIVSvinadTILVLDDGKLVAQGTHEEL 555
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHevlKVMQDLAEE---GMTMVIvtheigfAEKVAS-----RLIFIDKGRIAEDGDPQVL 223
|
....
gi 492039060 556 LKTS 559
Cdd:PRK09493 224 IKNP 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
333-550 |
2.67e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 101.03 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTlkDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikDVTEA-ALRKTVS 411
Cdd:cd03298 1 VRLDKIRFSY--GEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTAApPADRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSG-TIASNLRQG-NAQAKLHELQRAANMAQASEFieryndSFDHEVEERSANFSGGQKQRLSIARGLIAKA 489
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGlSPGLKLTAEDRQAIEVALARV------GLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 490 PILILDDSTSALDAesekkvqqALEHELPDTTTFIIAEKIVSVIN-----------ADTILVLDDGKLVAQG 550
Cdd:cd03298 148 PVLLLDEPFAALDP--------ALRAEMLDLVLDLHAETKMTVLMvthqpedakrlAQRVVFLDNGRIAAQG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
350-550 |
3.32e-24 |
|
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: 100.83 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIK---PGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDvTEAAL-----RKTVSFVLQRAVLFS 421
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD-SRKKInlppqQRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 G-TIASNLRQGnaqakLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:cd03297 89 HlNVRENLAFG-----LKRKRNREDRISVDELLDLLG--LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 501 LDAESEKKVQQALEH---ELPDTTTFII-----AEKIvsvinADTILVLDDGKLVAQG 550
Cdd:cd03297 162 LDRALRLQLLPELKQikkNLNIPVIFVThdlseAEYL-----ADRIVVMEDGRLQYIG 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
323-548 |
3.33e-24 |
|
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: 101.36 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 323 SGSVAPLsgsVEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD 400
Cdd:COG4181 2 SSSSAPI---IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 401 VTE---AALR-KTVSFVLQRAVLFSGTIAsnLRqgNAQAKLhELQRAAN-MAQASEFIERY--NDSFDHeveeRSANFSG 473
Cdd:COG4181 79 LDEdarARLRaRHVGFVFQSFQLLPTLTA--LE--NVMLPL-ELAGRRDaRARARALLERVglGHRLDH----YPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 474 GQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEhELPDT--TTFII-------AEKivsvinADTILVLDDG 544
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLF-ELNRErgTTLVLvthdpalAAR------CDRVLRLRAG 222
|
....
gi 492039060 545 KLVA 548
Cdd:COG4181 223 RLVE 226
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
21-308 |
3.82e-24 |
|
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: 102.85 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 21 AIIAILVSAFSGLYQPKLLEN-IQKALMANQK--QAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYAK 97
Cdd:cd18544 4 ALLLLLLATALELLGPLLIKRaIDDYIVPGQGdlQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 98 IQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLR 177
Cdd:cd18544 84 IQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 178 QMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIALIV 257
Cdd:cd18544 164 KSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 492039060 258 YLIGKNITAHPSDIAVVSPFVNYvLTLLFT--IMIAG-MTLMQfsRANISLGRI 308
Cdd:cd18544 244 WYGGGQVLSGAVTLGVLYAFIQY-IQRFFRpiRDLAEkFNILQ--SAMASAERI 294
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
354-556 |
6.08e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.43 E-value: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 354 SFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAalRKTVSFVLQRAVLFSG-TIASNLRQG- 431
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 432 NAQAKLHELQRAANMAQASE-FIERYNDSFDHEVeersanfSGGQKQRLSIARGLIAKAPILILDDSTSALDAesekkvq 510
Cdd:PRK10771 97 NPGLKLNAAQREKLHAIARQmGIEDLLARLPGQL-------SGGQRQRVALARCLVREQPILLLDEPFSALDP------- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 511 qALEHELPDTTTFIIAEK-----IVS--VINADTI----LVLDDGKLVAQGTHEELL 556
Cdd:PRK10771 163 -ALRQEMLTLVSQVCQERqltllMVShsLEDAARIaprsLVVADGRIAWDGPTDELL 218
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
350-553 |
9.59e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.14 E-value: 9.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIA--RLYDPTKGKVKIGGQNIKD--VTEAAlRKTVSFVLQRAVLFSG-TI 424
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILElsPDERA-RAGIFLAFQYPVEIPGvSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 ASNLRQGNAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSAN--FSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:COG0396 95 SNFLRTALNARRGEELSAREFLKLLKEKMKELG--LDEDFLDRYVNegFSGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492039060 503 AESEKKVQQALEHEL-PDTTTFIIA--EKIVSVINADTILVLDDGKLVAQGTHE 553
Cdd:COG0396 173 IDALRIVAEGVNKLRsPDRGILIIThyQRILDYIKPDFVHVLVDGRIVKSGGKE 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
333-546 |
1.48e-23 |
|
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: 99.02 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAA---LRKT 409
Cdd:cd03292 1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVLfsgtiasnlrqgnaqakLHELQRAANMAQASEFI--------ERYNDSFD-----HEVEERSANFSGGQK 476
Cdd:cd03292 80 IGVVFQDFRL-----------------LPDRNVYENVAFALEVTgvppreirKRVPAALElvglsHKHRALPAELSGGEQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 477 QRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADT--ILVLDDGKL 546
Cdd:cd03292 143 QRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
21-281 |
2.00e-23 |
|
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: 100.56 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 21 AIIAILVSAFSGLYQPKLLENI--QKALMANQKQAVLSDGIW--LVVLGIIAIISGIFNV---YFAAKIAQGVVSDLRED 93
Cdd:cd18547 4 VIILAIISTLLSVLGPYLLGKAidLIIEGLGGGGGVDFSGLLriLLLLLGLYLLSALFSYlqnRLMARVSQRTVYDLRKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 94 TYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGA 173
Cdd:cd18547 84 LFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 174 YVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMI---AY 250
Cdd:cd18547 164 FIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFInnlGY 243
|
250 260 270
....*....|....*....|....*....|...
gi 492039060 251 TVIALI--VYLIGKNITahpsdIAVVSPFVNYV 281
Cdd:cd18547 244 VLVAVVggLLVINGALT-----VGVIQAFLQYS 271
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
332-549 |
2.28e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.03 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAalRKTVS 411
Cdd:PRK11000 3 SVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSG-TIASNLRQGNAQAKLHELQRAANMAQASEFIEryndsFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:PRK11000 79 MVFQSYALYPHlSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQ-----LAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 491 ILILDDSTSALDAesEKKVQQALE----HE-LPDTTTFIIAEKIVSVINADTILVLDDGKlVAQ 549
Cdd:PRK11000 154 VFLLDEPLSNLDA--ALRVQMRIEisrlHKrLGRTMIYVTHDQVEAMTLADKIVVLDAGR-VAQ 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
350-554 |
2.69e-23 |
|
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: 99.34 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIK-----DVTEAALRKTvsFvlQRAVLFSG-T 423
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglpphRIARLGIART--F--QNPRLFPElT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 424 IASNLRQGnAQAKLHE-------------LQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:COG0411 96 VLENVLVA-AHARLGRgllaallrlprarREEREARERAEELLERVG--LADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 491 ILILDDSTSALDAEsEKKVQQALEHELPDT--TTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEE 554
Cdd:COG0411 173 LLLLDEPAAGLNPE-ETEELAELIRRLRDErgITILLIEHDMDLVMglADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
337-550 |
2.91e-23 |
|
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: 98.21 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 337 HVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQR 416
Cdd:cd03266 8 TKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 417 AVLFSGTIASNLRQgnaQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDD 496
Cdd:cd03266 88 GLYDRLTARENLEY---FAGLYGLKGDELTARLEELADRLG--MEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 497 STSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINA--DTILVLDDGKLVAQG 550
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlcDRVVVLHRGRVVYEG 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
350-561 |
3.98e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.79 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ--NIKDVTEAaLRKTVSFVLQRAVLFSG-TIAS 426
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvRFRSPRDA-QAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 NLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDheVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDaESE 506
Cdd:COG1129 99 NIFLGREPRRGGLIDWRAMRRRARELLARLGLDID--PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT-ERE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 507 KKVQQALEHELpdtttfiiAEKIVSVI-----------NADTILVLDDGKLVAQGTHEELLKTSLV 561
Cdd:COG1129 176 VERLFRIIRRL--------KAQGVAIIyishrldevfeIADRVTVLRDGRLVGTGPVAELTEDELV 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
345-555 |
9.30e-23 |
|
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: 96.67 E-value: 9.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI-KDVTEaaLRKTVSFVLQRAVLFSG- 422
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREPRE--VRRRIGIVFQDLSVDDEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 TIASNLRqgnAQAKLHELQRaanmAQASEFIERYNDSFD-HEVEER-SANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:cd03265 89 TGWENLY---IHARLYGVPG----AERRERIDELLDFVGlLEAADRlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 501 LDAESEKKVQQALE--HELPDTTTFII------AEKIvsvinADTILVLDDGKLVAQGTHEEL 555
Cdd:cd03265 162 LDPQTRAHVWEYIEklKEEFGMTILLTthymeeAEQL-----CDRVAIIDHGRIIAEGTPEEL 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
352-559 |
1.05e-22 |
|
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: 99.80 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 352 DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD----VTEAALRKTVSFVLQRAVLFSG-TIAS 426
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 NLRQGNAQAKLHelQRAANMAQASEFIeryndSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESE 506
Cdd:TIGR02142 95 NLRYGMKRARPS--ERRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 507 KKVQQALE--HELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEELLKTS 559
Cdd:TIGR02142 168 YEILPYLErlHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-505 |
1.30e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 335 FDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqnikdvteaalRKTVSFVL 414
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 415 QRAVLFSG-TIASNLRQGNA--QAKLHELQRA-ANMAQASEFIERYND-----------SFDHEVEE------------- 466
Cdd:COG0488 68 QEPPLDDDlTVLDTVLDGDAelRALEAELEELeAKLAEPDEDLERLAElqeefealggwEAEARAEEilsglgfpeedld 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492039060 467 -RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAES 505
Cdd:COG0488 148 rPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
333-563 |
1.47e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.50 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRA--VLFSGTIASNLRQG--NAQAKLHELQRAANMAQASEFIERYNDSFDHeveersaNFSGGQKQRLSIArGLIAK 488
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERRVEEALKAVRMWDFRDKPPY-------HLSYGQKKRVAIA-GVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 489 AP-ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELLKTSLVYQ 563
Cdd:PRK13647 156 DPdVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAewADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
333-561 |
1.52e-22 |
|
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: 97.08 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGK-VKIGGQNIKDVTEAALRKTVS 411
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FV---LQR----------AVLfSGTIASNLRQGNAQAKlhELQRAANMAQASEFIERYNDSFDHeveersanFSGGQKQR 478
Cdd:COG1119 82 LVspaLQLrfprdetvldVVL-SGFFDSIGLYREPTDE--QRERARELLELLGLAHLADRPFGT--------LSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQALEH--ELPDTTTFII---AEKIVSVINadTILVLDDGKLVAQGTHE 553
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVthhVEEIPPGIT--HVLLLKDGRVVAAGPKE 228
|
....*...
gi 492039060 554 ELLKTSLV 561
Cdd:COG1119 229 EVLTSENL 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
332-553 |
1.59e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGG------QNIKDVTEAA 405
Cdd:COG4161 2 SIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQRAVLFSG-TIASNLRQgnAQAKLHELQRAANMAQASEFIER-----YNDSFdheveerSANFSGGQKQRL 479
Cdd:COG4161 80 LRQKVGMVFQQYNLWPHlTVMENLIE--APCKVLGLSKEQAREKAMKLLARlrltdKADRF-------PLHLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 480 SIARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDT--TTFII------AEKIvsvinADTILVLDDGKLVAQGT 551
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEII-RELSQTgiTQVIVthevefARKV-----ASQVVYMEKGRIIEQGD 224
|
..
gi 492039060 552 HE 553
Cdd:COG4161 225 AS 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
334-515 |
1.60e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.32 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFV 413
Cdd:PRK10247 9 QLQNVGYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSGTIASNL------RqgnaqaklhelQRAANMAQASEFIERYNDSfDHEVEERSANFSGGQKQRLSIARGLIA 487
Cdd:PRK10247 87 AQTPTLFGDTVYDNLifpwqiR-----------NQQPDPAIFLDDLERFALP-DTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180
....*....|....*....|....*...
gi 492039060 488 KAPILILDDSTSALDAESEKKVQQALEH 515
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHR 182
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
350-563 |
2.91e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 96.38 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTvsfvlqRAVL-------FSG 422
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR------RAVLpqhsslsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 TI-------ASNLRQGNAQAKlhELQRAAnMAQA--SEFIERYNDSFdheveersanfSGGQKQRLSIARGLI------A 487
Cdd:PRK13548 92 TVeevvamgRAPHGLSRAEDD--ALVAAA-LAQVdlAHLAGRDYPQL-----------SGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 488 KAPILILDDSTSALDaesekkvqqaLEHELpdtTTFIIA-----EKIVSVI------N-----ADTILVLDDGKLVAQGT 551
Cdd:PRK13548 158 PPRWLLLDEPTSALD----------LAHQH---HVLRLArqlahERGLAVIvvlhdlNlaaryADRIVLLHQGRLVADGT 224
|
250
....*....|....*
gi 492039060 552 HEELLKTSL---VYQ 563
Cdd:PRK13548 225 PAEVLTPETlrrVYG 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
333-564 |
5.36e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.10 E-value: 5.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVteAALRKTVSF 412
Cdd:PRK09452 15 VELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV--PAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRQGNAQAKL--HELQR----AANMAQASEFIERyndsfdheveeRSANFSGGQKQRLSIARGL 485
Cdd:PRK09452 91 VFQSYALFPHmTVFENVAFGLRMQKTpaAEITPrvmeALRMVQLEEFAQR-----------KPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 486 IAKAPILILDDSTSALDAESEKKVQQ---ALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEllktslVY 562
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNelkALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE------IY 233
|
..
gi 492039060 563 QE 564
Cdd:PRK09452 234 EE 235
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
348-555 |
1.41e-21 |
|
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: 94.92 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikdvteaalrktVSFVLQRAVLFSGTIASN 427
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 428 LRQGNAQAKlHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEK 507
Cdd:cd03291 118 IIFGVSYDE-YRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492039060 508 KV-QQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEL 555
Cdd:cd03291 197 EIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
345-556 |
1.44e-21 |
|
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: 93.89 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDV-TEAALRKTVSFVLQRAVLFSG- 422
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLpPHRIARLGIGYVPEGRRIFPSl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 TIASNLRQGnAQAKLHELQRAANMAQASEFIERyndsfdheVEERSANF----SGGQKQRLSIARGLIAKAPILILDDST 498
Cdd:COG0410 94 TVEENLLLG-AYARRDRAEVRADLERVYELFPR--------LKERRRQRagtlSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 499 SALdaeSEKKVQQALE--HELPDT-TTFIIAEKIVSVI--NADTILVLDDGKLVAQGTHEELL 556
Cdd:COG0410 165 LGL---APLIVEEIFEiiRRLNREgVTILLVEQNARFAleIADRAYVLERGRIVLEGTAAELL 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
345-569 |
1.84e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.93 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTI 424
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 ASNL----RQ------GNAQAKLHEL-QRAANMAQASEFIERyndsfdheveeRSANFSGGQKQRLSIARGLIAKAPILI 493
Cdd:PRK11231 93 VRELvaygRSpwlslwGRLSAEDNARvNQAMEQTRINHLADR-----------RLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 494 LDDSTSALDAESEKKVqQALEHELPDTTTFIIAekIVSVIN-----ADTILVLDDGKLVAQGTHEELLKTSLVyQEIFKT 568
Cdd:PRK11231 162 LDEPTTYLDINHQVEL-MRLMRELNTQGKTVVT--VLHDLNqasryCDHLVVLANGHVMAQGTPEEVMTPGLL-RTVFDV 237
|
.
gi 492039060 569 Q 569
Cdd:PRK11231 238 E 238
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
333-568 |
2.29e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.61 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQravlfSGTIASNLR-------------QGNAQAKLHELqraanMAQASEFIE------RYNDSfdheveersanFSG 473
Cdd:COG4604 80 LRQ-----ENHINSRLTvrelvafgrfpysKGRLTAEDREI-----IDEAIAYLDledladRYLDE-----------LSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 474 GQKQRLSIARGLIAKAPILILDDSTSALD---AESEKKVQQALEHELPDTttfiiaekIVSV---IN-----ADTILVLD 542
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkhSVQMMKLLRRLADELGKT--------VVIVlhdINfascyADHIVAMK 210
|
250 260
....*....|....*....|....*.
gi 492039060 543 DGKLVAQGTHEELLkTSLVYQEIFKT 568
Cdd:COG4604 211 DGRVVAQGTPEEII-TPEVLSDIYDT 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
332-553 |
2.44e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.16 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGG------QNIKDVTEAA 405
Cdd:PRK11124 2 SIQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQRAVLFSG-TIASNLRQgnAQAKLHELQRAANMAQASEFIERYndsfdhEVEERSANF----SGGQKQRLS 480
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPHlTVQQNLIE--APCRVLGLSKDQALARAEKLLERL------RLKPYADRFplhlSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 481 IARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDT--TTFI------IAEKIvsvinADTILVLDDGKLVAQGTH 552
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSII-RELAETgiTQVIvtheveVARKT-----ASRVVYMENGHIVEQGDA 225
|
.
gi 492039060 553 E 553
Cdd:PRK11124 226 S 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
329-555 |
2.52e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.03 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 329 LSGSVEFDHVSFTY-PDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALR 407
Cdd:PRK13650 1 MSNIIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQRA-VLFSGT-----IASNLR-QGNAQAKLHE-LQRAANMAQASEFIERyndsfdheveeRSANFSGGQKQRL 479
Cdd:PRK13650 81 HKIGMVFQNPdNQFVGAtveddVAFGLEnKGIPHEEMKErVNEALELVGMQDFKER-----------EPARLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 480 SIArGLIAKAP-ILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK13650 150 AIA-GAVAMRPkIIILDEATSMLDPEGRLELIKTIKgiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
333-557 |
4.37e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 93.61 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT----LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA-ALR 407
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQR------AVLFSGTIA---SNL--RQGNAQAKLHELQRAANMAQasefierYNDSFDHEVeersanfSGGQK 476
Cdd:PRK13633 85 NKAGMVFQNpdnqivATIVEEDVAfgpENLgiPPEEIRERVDESLKKVGMYE-------YRRHAPHLL-------SGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 477 QRLSIArGLIAKAP-ILILDDSTSALDAESEKKVQQALEhELPDT---TTFIIAEKIVSVINADTILVLDDGKLVAQGTH 552
Cdd:PRK13633 151 QRVAIA-GILAMRPeCIIFDEPTAMLDPSGRREVVNTIK-ELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
....*
gi 492039060 553 EELLK 557
Cdd:PRK13633 229 KEIFK 233
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-308 |
6.32e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 93.34 E-value: 6.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 18 VVCAIIAILVSAFSGLYQPKLleniQKALM----ANQKQAVLSDGIWLVVLGIIAI-----ISGIFNVYFAAKIAQGVVS 88
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYL----TKILIddvlIQLGPGGNTSLLLLLVLGLAGAyvlsaLLGILRGRLLARLGERITA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 89 DLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIF---------CIVIIPrfww 159
Cdd:cd18563 77 DLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVlfslnwklaLLVLIP---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 160 APVVmVALIFGFGayvlRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFS 239
Cdd:cd18563 153 VPLV-VWGSYFFW----KKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 240 AIMPAFQMIAYTVIALIVYL-----IGKNITahpsdIAVVSPFVNYvLTLLFT-IMIAGMTLMQFSRANISLGRI 308
Cdd:cd18563 228 TFFPLLTFLTSLGTLIVWYFggrqvLSGTMT-----LGTLVAFLSY-LGMFYGpLQWLSRLNNWITRALTSAERI 296
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
333-558 |
7.30e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.40 E-value: 7.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikDVTEAALR-KTVS 411
Cdd:PRK11432 7 VVLKNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---DVTHRSIQqRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSG-TIASNLRQGNAQAKLHELQRAANMAQASE------FIERYNDsfdheveersaNFSGGQKQRLSIARG 484
Cdd:PRK11432 82 MVFQSYALFPHmSLGENVGYGLKMLGVPKEERKQRVKEALElvdlagFEDRYVD-----------QISGGQQQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 485 LIAKAPILILDDSTSALDA---ESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDAnlrRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
333-559 |
1.61e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.69 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTY-PDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVS 411
Cdd:PRK13642 5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRA--VLFSGTIASNLRQGNAQaklHELQRAANMAQASEFIERYNdSFDHEVEErSANFSGGQKQRLSIArGLIAKA 489
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMEN---QGIPREEMIKRVDEALLAVN-MLDFKTRE-PARLSGGQKQRVAVA-GIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 490 P-ILILDDSTSALDAESEKKVQQALeHELPDT---TTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTS 559
Cdd:PRK13642 159 PeIIILDESTSMLDPTGRQEIMRVI-HEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
333-556 |
2.06e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.45 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI----KDVTEaaLRK 408
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMK--LRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 409 TVSFVLQRA--VLFSGTIASNLRQG--NAQAKLHELQRAANMAQASEFIERYNDSFDHEVeersanfSGGQKQRLSIARG 484
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCL-------SFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQALEHELPDT-TTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELgLTIIIATHDIDIVPlyCDNVFVMKEGRVILQGNPKEVF 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
330-570 |
2.29e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.53 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 330 SGSVEFDHVSFTYPDGDDPT--------------------LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKG 389
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSrslkelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 390 KVKIGGqnikdvteaalrkTVSFVLQRAVLF----SGtiasnlRQgNA--QAKLHELQRA---ANMAQASEF--IERYnd 458
Cdd:COG1134 82 RVEVNG-------------RVSALLELGAGFhpelTG------RE-NIylNGRLLGLSRKeidEKFDEIVEFaeLGDF-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 459 sFDHEVEersaNFSGGQKQRL--SIArglIAKAP-ILILDDSTSALDAESEKKVQQALEHELPDTTTFIiaekIVS---- 531
Cdd:COG1134 140 -IDQPVK----TYSSGMRARLafAVA---TAVDPdILLVDEVLAVGDAAFQKKCLARIRELRESGRTVI----FVShsmg 207
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 492039060 532 VIN--ADTILVLDDGKLVAQGTHEELLKtslVYQEIFKTQK 570
Cdd:COG1134 208 AVRrlCDRAIWLEKGRLVMDGDPEEVIA---AYEALLAGRE 245
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
345-557 |
2.88e-20 |
|
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: 89.12 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARL--YDPTKGKVKIGGQNIKD--VTEAALRK-TVSFvlQRAVL 419
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDlpPEERARLGiFLAF--QYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 420 FSGTiasnlrqgnaqaKLHELQRAANMaqasefieryndsfdheveersaNFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:cd03217 89 IPGV------------KNADFLRYVNE-----------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 500 ALDAESEKKVQQALEHELPDTTTFIIA---EKIVSVINADTILVLDDGKLVAQGTHEELLK 557
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVLIIthyQRLLDYIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
333-524 |
3.11e-20 |
|
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: 87.98 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIggqnikdvteaALRKTVSF 412
Cdd:cd03223 1 IELENLSLATPDGR-VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTiasnLRQgnaqAKLHELQRAanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03223 69 LPQRPYLPLGT----LRE----QLIYPWDDV---------------------------LSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|..
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELpdtTTFI 524
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKELG---ITVI 142
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
333-549 |
3.92e-20 |
|
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: 87.48 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGddPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ--NIKDVTEaALRKTV 410
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRD-ARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQravlfsgtiasnlrqgnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAP 490
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 491 ILILDDSTSALDAESEKKVQQALeHELPDT-TTFI-IAEKIVSVIN-ADTILVLDDGKLVAQ 549
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVI-RRLRAQgVAVIfISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
18-308 |
3.93e-20 |
|
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: 90.99 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 18 VVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYA 96
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIaIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 97 KIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVL 176
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 177 RQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIALI 256
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 492039060 257 VYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18545 242 YWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
333-547 |
4.40e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIgGQNIKdvteaalrktVSF 412
Cdd:COG0488 316 LELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQ-RAVLFSG-TIASNLRQGNAQAKlhelqraanMAQASEFIERYNDSFDhEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:COG0488 383 FDQhQEELDPDkTVLDELRDGAPGGT---------EQEVRGYLGRFLFSGD-DAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 491 ILILDDSTSALDAESekkvQQALEHELPDTT-TFIiaekIVS----VIN--ADTILVLDDGKLV 547
Cdd:COG0488 453 VLLLDEPTNHLDIET----LEALEEALDDFPgTVL----LVShdryFLDrvATRILEFEDGGVR 508
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
343-555 |
4.85e-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: 94.98 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 343 PDGDD------------PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikdvteaalrktV 410
Cdd:TIGR01271 423 PNGDDglffsnfslyvtPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------I 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSGTIASNLRQGNAQAKlHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:TIGR01271 490 SFSPQTSWIMPGTIKDNIIFGLSYDE-YRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDAD 568
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 491 ILILDDSTSALDAESEKKV-QQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEL 555
Cdd:TIGR01271 569 LYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
350-560 |
5.16e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 94.85 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVkiggqnikdvteaALRKTVSFVLQRAVLFSGTIASNL- 428
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNIl 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 429 --RQGNAqAKLHELQRA----ANMAQASEFIERyndsfdhEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:PTZ00243 743 ffDEEDA-ARLADAVRVsqleADLAQLGGGLET-------EIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 503 AE-SEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSL 560
Cdd:PTZ00243 815 AHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTSL 873
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
350-555 |
5.21e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 91.18 E-value: 5.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD---VTEAALRKTVSFVLQRAVlfsgtiAS 426
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNPY------GS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 -NLRQGNAQ---------AKLHELQRAAN----MAQA---SEFIERYndsfDHEveersanFSGGQKQRLSIARGLIAKA 489
Cdd:PRK11308 105 lNPRKKVGQileepllinTSLSAAERREKalamMAKVglrPEHYDRY----PHM-------FSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 490 PILILDDSTSALDAESEKKVQQA---LEHELPDTTTFI-----IAEKIvsvinADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLmmdLQQELGLSYVFIshdlsVVEHI-----ADEVMVMYLGRCVEKGTKEQI 242
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
348-544 |
6.05e-20 |
|
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: 88.54 E-value: 6.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKV----KIGGQNIKDVTEAALRKTVSFVLQRAVLFSGT 423
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 424 IASNLRQGNAQAKlhelQRAANMAQASEF---IERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:cd03290 95 VEENITFGSPFNK----QRYKAVTDACSLqpdIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492039060 501 LDAE-SEKKVQQALEHELPDT--TTFIIAEKIVSVINADTILVLDDG 544
Cdd:cd03290 171 LDIHlSDHLMQEGILKFLQDDkrTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
334-513 |
6.53e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.54 E-value: 6.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikDVTEAALRKTVs 411
Cdd:COG4525 5 TVRHVSVRYPGGGQPQpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGADRGV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 fVLQRAVLFSG-TIASNLRQGnaqAKLHELQRAANMAQASEFIER-----YNDSFDHEVeersanfSGGQKQRLSIARGL 485
Cdd:COG4525 81 -VFQKDALLPWlNVLDNVAFG---LRLRGVPKAERRARAEELLALvgladFARRRIWQL-------SGGMRQRVGIARAL 149
|
170 180
....*....|....*....|....*...
gi 492039060 486 IAKAPILILDDSTSALDAESEKKVQQAL 513
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELL 177
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
18-308 |
9.77e-20 |
|
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: 89.80 E-value: 9.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 18 VVCAIIAILVSAFSGLYQPKLLENIQKALMANQkqavlSDGIWLVVLGIIAIISGIFNV---YFAAKIAQGVVSDLREDT 94
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGG-----SSGGLLALLVALFLLQAVLSAlssYLLGRTGERVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 95 YAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAY 174
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 175 VLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIA 254
Cdd:cd18551 156 LGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 492039060 255 LIVYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18551 236 VVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
323-557 |
1.39e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.28 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 323 SGSVAPLSGS-----VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQN 397
Cdd:PRK13536 27 SEAKASIPGSmstvaIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 398 IKDVTEAAlRKTVSFVLQRAVL-FSGTIASNLRQGNAQAKLHELQRAANMAQASEFIEryndsFDHEVEERSANFSGGQK 476
Cdd:PRK13536 105 VPARARLA-RARIGVVPQFDNLdLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFAR-----LESKADARVSDLSGGMK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 477 QRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEE 554
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAErlCDRLCVLEAGRKIAEGRPHA 258
|
...
gi 492039060 555 LLK 557
Cdd:PRK13536 259 LID 261
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
350-544 |
1.77e-19 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 87.52 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIkdvTEAALRKTVsfVLQRAVLFSGTIAsnlR 429
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI---TEPGPDRMV--VFQNYSLLPWLTV---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 430 QGNAQAkLHELQRAANMAQASEFIERYND--SFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEK 507
Cdd:TIGR01184 73 ENIALA-VDRVLPDLSKSERRAIVEEHIAlvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492039060 508 KVQQAL-----EHELpdtTTFIIAEKI-VSVINADTILVLDDG 544
Cdd:TIGR01184 152 NLQEELmqiweEHRV---TVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
21-292 |
1.77e-19 |
|
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: 89.08 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 21 AIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLsDGIWLVVLGIIAI--ISGIFNVYFAAKIAQGVVSDLREDTYAKI 98
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASL-NQIALLLLGLFLLqaVFSFFRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 99 QTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPR-----FWWAPVVMVALIFgFGA 173
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKltllmLATVPVVVLVAVL-FGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 174 YvLRQMNslfTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVI 253
Cdd:cd18576 159 R-IRKLS---KKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAI 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 492039060 254 ALIVYLIGKNITAHPSDIAVVSPFvnyvltLLFTIMIAG 292
Cdd:cd18576 235 VAVLWYGGRLVLAGELTAGDLVAF------LLYTLFIAG 267
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
336-513 |
2.11e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.56 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAA---LR-KT 409
Cdd:PRK11629 9 DNLCKRYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVL---FSG--TIASNLRQGN---AQAKlhelQRAANMAQASefieryndSFDHEVEERSANFSGGQKQRLSI 481
Cdd:PRK11629 89 LGFIYQFHHLlpdFTAleNVAMPLLIGKkkpAEIN----SRALEMLAAV--------GLEHRANHRPSELSGGERQRVAI 156
|
170 180 190
....*....|....*....|....*....|..
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQAL 513
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLL 188
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
332-565 |
2.72e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.26 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYPDG---DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI------KDVT 402
Cdd:PRK13649 2 GINLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 403 EaaLRKTVSFVLQ--RAVLFSGTIASNLRQG--NAQAKLHELQRAANMAQASEFIeryndsfDHEVEERSA-NFSGGQKQ 477
Cdd:PRK13649 82 Q--IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAREKLALVGI-------SESLFEKNPfELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 478 RLSIArGLIAKAP-ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIV-SVIN-ADTILVLDDGKLVAQGthee 554
Cdd:PRK13649 153 RVAIA-GILAMEPkILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANyADFVYVLEKGKLVLSG---- 227
|
250
....*....|.
gi 492039060 555 llKTSLVYQEI 565
Cdd:PRK13649 228 --KPKDIFQDV 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
350-556 |
4.18e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.11 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIkDVTEA---------ALRKTVSFVLQRAVLF 420
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI-DTARSlsqqkglirQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SG-TIASNLRQGNAQAKlhELQRAANMAQASEFIERYNDSFDHEVEERsaNFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:PRK11264 98 PHrTVLENIIEGPVIVK--GEPKEEATARARELLAKVGLAGKETSYPR--RLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 500 ALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdvADRAIFMDQGRIVEQGPAKALF 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
338-558 |
6.43e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 6.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 338 VSFtypdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRA 417
Cdd:PRK09536 11 VEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 418 VL-FSGTIASNLRQGNA----------QAKLHELQRAANMAQASEFIERYNDSfdheveersanFSGGQKQRLSIARGLI 486
Cdd:PRK09536 87 SLsFEFDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQFADRPVTS-----------LSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 487 AKAPILILDDSTSALDAesEKKVQQ-ALEHELPDTTTFIIAEkiVSVIN-----ADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK09536 156 QATPVLLLDEPTASLDI--NHQVRTlELVRRLVDDGKTAVAA--IHDLDlaaryCDELVLLADGRVRAAGPPADVLTA 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
350-550 |
9.01e-19 |
|
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: 85.28 E-value: 9.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikdVTeAALRKTVSFVLQ----RAVLFSGTIa 425
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR----VS-SLLGLGGGFNPEltgrENIYLNGRL- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 426 SNLRQGNAQAKLHELQraanmaqasEFIErYNDSFDHEVEersaNFSGGQKQRLSIARGLIAKAPILILDDSTSALDAES 505
Cdd:cd03220 112 LGLSRKEIDEKIDEII---------EFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492039060 506 EKKVQQALEHELPDTTTFIIAEKIVSVI--NADTILVLDDGKLVAQG 550
Cdd:cd03220 178 QEKCQRRLRELLKQGKTVILVSHDPSSIkrLCDRALVLEKGKIRFDG 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
344-555 |
1.57e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 87.58 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 344 DGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVteAALRKTVSFVLQRAVLFSG- 422
Cdd:PRK11607 30 DGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHm 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 TIASNLRQGNAQAKLHE---LQRAANM---AQASEFIERyndsfdheveeRSANFSGGQKQRLSIARGLIAKAPILILDD 496
Cdd:PRK11607 107 TVEQNIAFGLKQDKLPKaeiASRVNEMlglVHMQEFAKR-----------KPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 497 STSALDaeseKKVQQALEHELPD-------TTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK11607 176 PMGALD----KKLRDRMQLEVVDilervgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
333-545 |
2.42e-18 |
|
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: 81.73 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIgGQNIKdvteaalrktVSF 412
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQravlfsgtiasnlrqgnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03221 68 FEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 493 ILDDSTSALDAESekkvQQALEHELPDTT-TFIiaekIVS----VIN--ADTILVLDDGK 545
Cdd:cd03221 93 LLDEPTNHLDLES----IEALEEALKEYPgTVI----LVShdryFLDqvATKIIELEDGK 144
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
332-558 |
2.99e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.55 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVT--------- 402
Cdd:COG4152 1 MLELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 403 EAALRKTVSfVLQRAVLFsgtiasnlrqgnaqAKLHELQRAANMAQASEFIERYN--DSFDHEVEErsanFSGGQKQRLS 480
Cdd:COG4152 79 ERGLYPKMK-VGEQLVYL--------------ARLKGLSKAEAKRRADEWLERLGlgDRANKKVEE----LSKGNQQKVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 481 IARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDTTTFII--------AEKIvsvinADTILVLDDGKLVAQGTH 552
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVI-RELAAKGTTVIfsshqmelVEEL-----CDRIVIINKGRKVLSGSV 213
|
....*.
gi 492039060 553 EELLKT 558
Cdd:COG4152 214 DEIRRQ 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
345-507 |
3.24e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIkdvTEAALRKTVSFVLQR-AVLFSGT 423
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLGHRnAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 424 IASNLR-----QGNAQAKLHElqraanmaqASEFIERyndsfdHEVEERSANF-SGGQKQRLSIARGLIAKAPILILDDS 497
Cdd:PRK13539 90 VAENLEfwaafLGGEELDIAA---------ALEAVGL------APLAHLPFGYlSAGQKRRVALARLLVSNRPIWILDEP 154
|
170
....*....|
gi 492039060 498 TSALDAESEK 507
Cdd:PRK13539 155 TAALDAAAVA 164
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
348-555 |
3.93e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.38 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ--NIKDVTEA-----AL----RKTVSFVLQR 416
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAiragiAYvpedRKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 417 AVLFSGTIAsNLRQgnaQAKLHELQRAANMAQASEFIERYN---DSFDHEVeersANFSGGQKQRLSIARGLIAKAPILI 493
Cdd:COG1129 346 SIRENITLA-SLDR---LSRGGLLDRRRERALAEEYIKRLRiktPSPEQPV----GNLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 494 LDDSTSALD--AESEkkVQQALeHELpdtttfiiAEKIVSVI-----------NADTILVLDDGKLVAQGTHEEL 555
Cdd:COG1129 418 LDEPTRGIDvgAKAE--IYRLI-REL--------AAEGKAVIvisselpellgLSDRILVMREGRIVGELDREEA 481
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
350-547 |
3.99e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 84.74 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALRKTVSFVLQRAV-------L 419
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDSIsavnprkT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 420 FSGTIASNLRQgnaqakLHELQRAANMAQASEFIeRYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:PRK10419 108 VREIIREPLRH------LLSLDKAERLARASEML-RAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 500 ALDAESEKKVQQ---ALEHELPDTTTFI-----IAEKIvsvinADTILVLDDGKLV 547
Cdd:PRK10419 181 NLDLVLQAGVIRllkKLQQQFGTACLFIthdlrLVERF-----CQRVMVMDNGQIV 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
350-555 |
4.85e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.29 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGG------------------QNIKDVTEaaLRKTVS 411
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitnpysKKIKNFKE--LRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQ--RAVLFSGTIASNLRQGN---AQAKLHELQRAA----NMAQASEFIERynDSFDheveersanFSGGQKQRLSIA 482
Cdd:PRK13631 120 MVFQfpEYQLFKDTIEKDIMFGPvalGVKKSEAKKLAKfylnKMGLDDSYLER--SPFG---------LSGGQKRRVAIA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 483 rGLIAKAP-ILILDDSTSALDAESEKK-VQQALEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK13631 189 -GILAIQPeILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEI 263
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
333-555 |
4.97e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.47 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:PRK13652 4 IETRDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRA--VLFSGTIASNLRQGNAQAKLHELQRAANMAQASEF--IERYNDSFDHeveersaNFSGGQKQRLSIArGLIAK 488
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMlgLEELRDRVPH-------HLSGGEKKRVAIA-GVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 489 AP-ILILDDSTSALDAESEKKVQQALeHELPDT--TTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK13652 155 EPqVLVLDEPTAGLDPQGVKELIDFL-NDLPETygMTVIFSTHQLDLVPemADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
21-308 |
5.34e-18 |
|
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: 84.53 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 21 AIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLSDgiWLVVLGIIAIISGIFNV---YFAAKIAQGVVSDLREDTYAK 97
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNE--LALILLAIYLLQSVFTFvryYLFNIAGERIVARLRRDLFSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 98 IQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLR 177
Cdd:cd18557 79 LLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 178 QMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIALIV 257
Cdd:cd18557 159 YIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 492039060 258 YLIGKNITA-HPSDIAVVSpFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18557 239 WYGGYLVLSgQLTVGELTS-FILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
345-525 |
7.15e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.68 E-value: 7.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD--PT---KGKVKIGGQNI--KDVTEAALRKTVSFVLQRA 417
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 418 VLFSGTIASNLRQG----NAQAKLHEL-QRAanMAQASEFierynDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:PRK14243 101 NPFPKSIYDNIAYGarinGYKGDMDELvERS--LRQAALW-----DEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190
....*....|....*....|....*....|...
gi 492039060 493 ILDDSTSALDAESEKKVQQaLEHELPDTTTFII 525
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEE-LMHELKEQYTIII 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
345-567 |
8.45e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.39 E-value: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARL--YDPTKGKV-----------------KIGGQ--------- 396
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpsKVGEPcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 397 -------NIKDVTEAALRKTVSFVLQRAVLFSG--TIASNLRQGnaqakLHELQRAANMA--QASEFIERYNdsFDHEVE 465
Cdd:TIGR03269 91 peevdfwNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVLEA-----LEEIGYEGKEAvgRAVDLIEMVQ--LSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 466 ERSANFSGGQKQRLSIARGLiAKAPILIL-DDSTSALDAESEKKVQQALEHELPDT-TTFIIAEKIVSVIN--ADTILVL 541
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQL-AKEPFLFLaDEPTGTLDPQTAKLVHNALEEAVKASgISMVLTSHWPEVIEdlSDKAIWL 242
|
250 260
....*....|....*....|....*.
gi 492039060 542 DDGKLVAQGTHEELLKtslVYQEIFK 567
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVA---VFMEGVS 265
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
345-556 |
9.01e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.48 E-value: 9.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA-------------ALRKTVS 411
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSG-TIASNLRQGNAQAklhelqRAANMAQASEFIERYNDSFDheVEERS-----ANFSGGQKQRLSIARGL 485
Cdd:PRK10619 96 MVFQHFNLWSHmTVLENVMEAPIQV------LGLSKQEARERAVKYLAKVG--IDERAqgkypVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 486 IAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARhvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
350-556 |
9.13e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 85.47 E-value: 9.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL----RKTVSFVLQR-AVLFSGTI 424
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 ASNLRQGNAQAKL--HELQRAANMAQASEFIERYNDSFDHEVeersanfSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:PRK10070 124 LDNTAFGMELAGInaEERREKALDALRQVGLENYAHSYPDEL-------SGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 503 AESEKKVQQ---ALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK10070 197 PLIRTEMQDelvKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
21-257 |
1.35e-17 |
|
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: 83.35 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 21 AIIAILVSAFSGLYQPKLLENIQKALMANQKQAvlsDGIWLVVLGIIA--IISGIFN---VYFAAKIAQGVVSDLREDTY 95
Cdd:cd18778 4 TLLCALLSTLLGLVPPWLIRELVDLVTIGSKSL---GLLLGLALLLLGayLLRALLNflrIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 96 AKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLfmqmlrLPILIVGSFIFCIVIIPRFW--W-------APVVMVA 166
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADG------IPQGITNVLTLVGVAIILFSinPklalltlIPIPFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 167 LI-FGFGAYVLRqmnsLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAF 245
Cdd:cd18778 155 LGaWLYSKKVRP----RYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLM 230
|
250
....*....|....
gi 492039060 246 QMIAY--TVIALIV 257
Cdd:cd18778 231 EFLTSlgTVLVLGF 244
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
350-563 |
1.48e-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: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD--VTEAAlRKTVSFVLQRAVLFSG-TIAS 426
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpMHKRA-RLGIGYLPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 NLRqgnAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESE 506
Cdd:cd03218 95 NIL---AVLEIRGLSKKEREEKLEELLEEFH--ITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 507 KKVQQaLEHELPDTTTFII-----AEKIVSVInaDTILVLDDGKLVAQGTHEELLKTSLVYQ 563
Cdd:cd03218 170 QDIQK-IIKILKDRGIGVLitdhnVRETLSIT--DRAYIIYEGKVLAEGTPEEIAANELVRK 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
348-550 |
1.53e-17 |
|
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: 82.00 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqNIKDVTEAALRKTVSFVL-QRAvlfsgTIAS 426
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVFgQKT-----QLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 NLRQGNAQAKLHELQRAANmAQASEFIERYNDSFD--HEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAE 504
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPP-ARFKKRLDELSELLDleELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492039060 505 SEKKVQQALEHELPDT-TTFIIAEKIVSVIN--ADTILVLDDGKLVAQG 550
Cdd:cd03267 188 AQENIRNFLKEYNRERgTTVLLTSHYMKDIEalARRVLVIDKGRLLYDG 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
345-555 |
1.54e-17 |
|
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: 81.80 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI-KDVTEAALRKTVSFVLQRAVLFSG- 422
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItKLPPHERARAGIAYVPQGREIFPRl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 TIASNLRQGnaqaklhelqrAANMAQASEFI-ERYNDSFD--HEVEERSA-NFSGGQKQRLSIARGLIAKAPILILDDST 498
Cdd:TIGR03410 91 TVEENLLTG-----------LAALPRRSRKIpDEIYELFPvlKEMLGRRGgDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 499 SALDAESEKKVQQALehelpdttTFIIAEKIVSVI-----------NADTILVLDDGKLVAQGTHEEL 555
Cdd:TIGR03410 160 EGIQPSIIKDIGRVI--------RRLRAEGGMAILlveqyldfareLADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
17-300 |
1.70e-17 |
|
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: 83.27 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 17 DVVCAIIAilvsAFSGLYQPKLLENI-QKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTY 95
Cdd:cd18549 7 DLFCAVLI----AALDLVFPLIVRYIiDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 96 AKIQTFSFG---NIKkfsAGSLTTRLINDMNQVMNMMMqlfmqmlRLP-------ILIVGSFIFCIVIIPRFWWAPVVMV 165
Cdd:cd18549 83 EHLQKLSFSffdNNK---TGQLMSRITNDLFDISELAH-------HGPedlfisiITIIGSFIILLTINVPLTLIVFALL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 166 ALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQL----NDYNIVIGyWFSAI 241
Cdd:cd18549 153 PLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFleskKKAYKAMA-YFFSG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 242 MPAF-QMIAYTVIALIVYLIGKN-ITAhpSDIAVvspFVNYVLTLLFTImiagMTLMQFSR 300
Cdd:cd18549 232 MNFFtNLLNLVVLVAGGYFIIKGeITL--GDLVA---FLLYVNVFIKPI----RRLVNFTE 283
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
337-556 |
2.02e-17 |
|
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: 85.51 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 337 HVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP----TKGKVKIGGQNIKDVTEAALRK---- 408
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 409 TVSFVLQRAV-----LFS-GT-IASNLRqgnaqakLHE-LQRAANMAQASEFIERYN--------DSFDHEveersanFS 472
Cdd:COG4172 93 RIAMIFQEPMtslnpLHTiGKqIAEVLR-------LHRgLSGAAARARALELLERVGipdperrlDAYPHQ-------LS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 473 GGQKQRLSIARGLIAKAPILILDDSTSALDAesekKVQ-QALE-----------------HELPdtttfiiaekIVSVIn 534
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDllkdlqrelgmalllitHDLG----------VVRRF- 223
|
250 260
....*....|....*....|..
gi 492039060 535 ADTILVLDDGKLVAQGTHEELL 556
Cdd:COG4172 224 ADRVAVMRQGEIVEQGPTAELF 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
333-550 |
2.57e-17 |
|
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: 80.79 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqniKDVTEAALRKTVSF 412
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTIASNLRQgnaQAKLHELQRAANMAQASEFIERYNDSfDHEvEERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03269 76 PEERGLYPKMKVIDQLVY---LAQLKGLKKEEARRRIDEWLERLELS-EYA-NKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 493 ILDDSTSALDAESEKKVQQALEhELPDTTTFII--------AEKIvsvinADTILVLDDGKLVAQG 550
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIR-ELARAGKTVIlsthqmelVEEL-----CDRVLLLNKGRAVLYG 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
352-556 |
2.88e-17 |
|
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: 83.61 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 352 DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDvTEAAL-----RKTVSFVLQRAVLFSG-TIA 425
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD-SARGIflpphRRRIGYVFQEARLFPHlSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 426 SNLRQGNAQAKLHElqRAANMAQASEF--IEryndsfdHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDA 503
Cdd:COG4148 96 GNLLYGRKRAPRAE--RRISFDEVVELlgIG-------HLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 504 ES--E-----KKVQQalEHELPdtttfIIaekIVS-----VIN-ADTILVLDDGKLVAQGTHEELL 556
Cdd:COG4148 167 ARkaEilpylERLRD--ELDIP-----IL---YVShsldeVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
11-318 |
3.06e-17 |
|
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: 82.88 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 11 LKRYKKDVVCAIIAILVSAFSGLYQP-------KLLENIQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIA 83
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPvfailfsKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 84 QGVVSDLREDTYAKI--QTFSFGNIKKFSAGSLTTRLINDmnqvmnMMMQLFMQMLRLPILI--VGSFIFCIVIIPRFWW 159
Cdd:cd18578 81 ERLTRRLRKLAFRAIlrQDIAWFDDPENSTGALTSRLSTD------ASDVRGLVGDRLGLILqaIVTLVAGLIIAFVYGW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 160 --APVVMVALIFGFGAYVLRQMnsLFTKFQEMMDRI----SNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIv 233
Cdd:cd18578 155 klALVGLATVPLLLLAGYLRMR--LLSGFEEKNKKAyeesSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGL- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 234 IGYWFSAIMPAF-QMIAYTVIALIVYLIGKNITAHPSDIAVVspFVNYVLtLLFTIMIAGMTLM---QFSRANISLGRIR 309
Cdd:cd18578 232 RRALISGLGFGLsQSLTFFAYALAFWYGGRLVANGEYTFEQF--FIVFMA-LIFGAQSAGQAFSfapDIAKAKAAAARIF 308
|
....*....
gi 492039060 310 EVLETEPDV 318
Cdd:cd18578 309 RLLDRKPEI 317
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
332-557 |
3.42e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.13 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYPDG---DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI----KDVTEA 404
Cdd:PRK13646 2 TIRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 405 ALRKTVSFVLQ--RAVLFSGTIASNLRQGNAQAKLhELQRAANMAqaseFIERYNDSFDHEVEERSA-NFSGGQKQRLSI 481
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKM-NLDEVKNYA----HRLLMDLGFSRDVMSQSPfQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALEH-ELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELLK 557
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENKTIILVSHDMNEVAryADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
349-555 |
3.99e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.83 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 349 TLK---DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALRKTVSFVLQR--AVL- 419
Cdd:PRK15079 33 TLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDplASLn 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 420 ----FSGTIASNLRQGNAQAKLHEL-QRAANMAQA----SEFIERYndsfDHEveersanFSGGQKQRLSIARGLIAKAP 490
Cdd:PRK15079 113 prmtIGEIIAEPLRTYHPKLSRQEVkDRVKAMMLKvgllPNLINRY----PHE-------FSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 491 ILILDDSTSALDAESEKKV---QQALEHELPDTTTFIIAEkiVSVIN--ADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVvnlLQQLQREMGLSLIFIAHD--LAVVKhiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
324-560 |
4.62e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.16 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 324 GSVAPLsgsvEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE 403
Cdd:PRK13537 3 MSVAPI----DFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 404 AAlRKTVSFVLQRAVL---FsgTIASNLRQGNAQAKLHELQRAANMAQASEFiERYNDSFDHEVEErsanFSGGQKQRLS 480
Cdd:PRK13537 77 HA-RQRVGVVPQFDNLdpdF--TVRENLLVFGRYFGLSAAAARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 481 IARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFII-------AEKIvsvinADTILVLDDGKLVAQGTHE 553
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPH 223
|
....*..
gi 492039060 554 ELLKTSL 560
Cdd:PRK13537 224 ALIESEI 230
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
138-546 |
4.73e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 84.25 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 138 RLP------ILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQG-------- 203
Cdd:PRK10522 124 RLPelvqgiILTLGSAAYLAWLSPKMLLVTAIWMAVTIWGGFVLVARVYKHMATLRETEDKLYNDYQTVLEGrkeltlnr 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 204 VRVVKSFNQGPQE-IKKFDQTSDQLNDYNIVIGYWfSAIMpafqMIAytVIALIVYLIGKNITAhpsDIAVVSpfvNYVL 282
Cdd:PRK10522 204 ERAEYVFENEYEPdAQEYRHHIIRADTFHLSAVNW-SNIM----MLG--AIGLVFYMANSLGWA---DTNVAA---TYSL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 283 TLLF--TIMIAGM----TLMQfsrANISLGRIREvLETEPDVKFVESGSVAPLSGSVEFDHVSFTYPDGDDpTLKDISFK 356
Cdd:PRK10522 271 TLLFlrTPLLSAVgalpTLLS---AQVAFNKLNK-LALAPYKAEFPRPQAFPDWQTLELRNVTFAYQDNGF-SVGPINLT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 357 IKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASnlrQGnaqak 436
Cdd:PRK10522 346 IKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGP---EG----- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 437 lhelqRAANMAQASEFIERYNDSFDHEVEE---RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQAL 513
Cdd:PRK10522 418 -----KPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVL 492
|
410 420 430
....*....|....*....|....*....|....*
gi 492039060 514 EHELPDT--TTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:PRK10522 493 LPLLQEMgkTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
350-558 |
4.97e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.37 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPTKGKVKIGGQNIKDVTEAAL---RKTVSFVLQR---------A 417
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDpnsslnprlN 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 418 VLfsGTIASNLRQgnAQAKLHELQRAANMAQASEFIeryndSFDHEVEER-SANFSGGQKQRLSIARGLIAKAPILILDD 496
Cdd:PRK15134 381 VL--QIIEEGLRV--HQPTLSAAQREQQVIAVMEEV-----GLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 497 STSALDAESE-------KKVQQalEHELpdttTFIIAEKIVSVINA--DTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK15134 452 PTSSLDKTVQaqilallKSLQQ--KHQL----AYLFISHDLHVVRAlcHQVIVLRQGEVVEQGDCERVFAA 516
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
350-509 |
5.00e-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: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVL---FSGTIAS 426
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPSMTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 NLRQGNAQAKLHELQRAANMAQASEFIERYNdSFDHEVEER----SANFSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:COG1101 102 NLALAYRRGKRRGLRRGLTKKRRELFRELLA-TLGLGLENRldtkVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
....*..
gi 492039060 503 AESEKKV 509
Cdd:COG1101 181 PKTAALV 187
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
333-565 |
7.09e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.32 E-value: 7.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTY-PDGD--DPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE----AA 405
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQ--RAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIeryndSFDHEVEERSA-NFSGGQKQRLSIA 482
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV-----GLADEFWEKSPfELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 483 rGLIAKAP-ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEEllkts 559
Cdd:PRK13643 157 -GILAMEPeVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVAdyADYVYLLEKGHIISCGTPSD----- 230
|
....*.
gi 492039060 560 lVYQEI 565
Cdd:PRK13643 231 -VFQEV 235
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-261 |
7.17e-17 |
|
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: 81.37 E-value: 7.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 18 VVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVlsdgIWLVVLGI-IAIISGIFNV---YFAAKIAQGVVSDLRE 92
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREiIDDALPQGDLGLL----VLLALGMVaVAVASALLGVvqtYLSARIGQGVMYDLRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 93 DTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFI-----------FCIVIIPRFWWaP 161
Cdd:cd18550 77 QLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVamlaldwrlalLSLVLLPLFVL-P 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 162 VVMVAlifgfgayvlRQMNSLFTKFQEMMDRISNQAQETL--QGVRVVKSFNQGPQEIKKFDQTSDQLNDYNI---VIGY 236
Cdd:cd18550 156 TRRVG----------RRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARRSRELRDLGVrqaLAGR 225
|
250 260
....*....|....*....|....*
gi 492039060 237 WFSAIMpafqMIAYTVIALIVYLIG 261
Cdd:cd18550 226 WFFAAL----GLFTAIGPALVYWVG 246
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-558 |
7.20e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.48 E-value: 7.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ------NIKDVTEAALRKTVSFVLQRAVL 419
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 420 FS-----GTIASNLRQGNAQAKlHELQRAanMAQASEFIERYNDSFDhEVEERSANFSGGQKQRLSIARGLIAKAPILIL 494
Cdd:PRK14246 102 FPhlsiyDNIAYPLKSHGIKEK-REIKKI--VEECLRKVGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 495 DDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
332-514 |
9.36e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 9.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD-----PTKGKVKIGGQNI--KDVTEA 404
Cdd:PRK14258 7 AIKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 405 ALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARG 484
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190
....*....|....*....|....*....|
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQALE 514
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQ 194
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
345-525 |
9.47e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 80.20 E-value: 9.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD-----PTKGKVKIGGQNI----KDVTEaaLRKTVSFVLQ 415
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysprTDTVD--LRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 RAVLFSGTIASNLRQG---NAQAKLHELQRAA--NMAQAS---EFIERYNDSfdheveerSANFSGGQKQRLSIARGLIA 487
Cdd:PRK14239 94 QPNPFPMSIYENVVYGlrlKGIKDKQVLDEAVekSLKGASiwdEVKDRLHDS--------ALGLSGGQQQRVCIARVLAT 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 492039060 488 KAPILILDDSTSALDAESEKKVQQALeHELPDTTTFII 525
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETL-LGLKDDYTMLL 202
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
18-308 |
1.28e-16 |
|
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: 80.60 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 18 VVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYA 96
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRaIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 97 KIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQlfmqmlrLPILIVGSFIFCIVIIPRFWWAP------VVMVALIFG 170
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-------GPFLLGNLLTLVVGLVVMLVLSPplalvaLASLPPLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 171 FGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAY 250
Cdd:cd18543 154 VARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 251 TVIALIVyLIGKNITAHPS-DIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18543 234 LGLAAVL-ALGGWLVANGSlTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
345-546 |
1.45e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.72 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIkdvteAALRKTVSFVLQRAVLFS-GT 423
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAREDTRLMFQDARLLPwKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 424 IASN----LRqGNAQAKLHELQRAANMAqasefiERYNdsfdheveERSANFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:PRK11247 98 VIDNvglgLK-GQWRDAALQALAAVGLA------DRAN--------EWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492039060 500 ALDAESEKKVQQALE-----HELpdttTFIIAEKIVS--VINADTILVLDDGKL 546
Cdd:PRK11247 163 ALDALTRIEMQDLIEslwqqHGF----TVLLVTHDVSeaVAMADRVLLIEEGKI 212
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
353-555 |
1.71e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 79.65 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 353 ISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL-RKTVSFVLQRAVLF-SGTIASNL-- 428
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLFrEMTVIENLlv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 429 ---RQGNAQAkLHEL---------QRAAnMAQASEFIERYNDSfdhEVEERSA-NFSGGQKQRLSIARGLIAKAPILILD 495
Cdd:PRK11300 104 aqhQQLKTGL-FSGLlktpafrraESEA-LDRAATWLERVGLL---EHANRQAgNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 496 DSTSALDAEsEKKVQQALEHELPD---TTTFIIAE--KIVSVInADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK11300 179 EPAAGLNPK-ETKELDELIAELRNehnVTVLLIEHdmKLVMGI-SDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-558 |
1.72e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.75 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 322 ESGSVAPLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKG-----KVKIGGQ 396
Cdd:PRK14271 9 QSGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 397 NI---KDVTEaaLRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSG 473
Cdd:PRK14271 89 SIfnyRDVLE--FRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 474 GQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTH 552
Cdd:PRK14271 167 GQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPT 246
|
....*.
gi 492039060 553 EELLKT 558
Cdd:PRK14271 247 EQLFSS 252
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
341-514 |
1.72e-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: 78.17 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 341 TYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEaalrktvsfVLQRAVLF 420
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD---------EPHENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SG---------TIASNLR-----QGNAQAKLHELQRAANMAQAsefieryndsfdhevEERSANF-SGGQKQRLSIARGL 485
Cdd:TIGR01189 78 LGhlpglkpelSALENLHfwaaiHGGAQRTIEDALAAVGLTGF---------------EDLPAAQlSAGQQRRLALARLW 142
|
170 180
....*....|....*....|....*....
gi 492039060 486 IAKAPILILDDSTSALDAESEKKVQQALE 514
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLR 171
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
330-559 |
2.41e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.88 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 330 SGSVEFDHVSFTYPDGDdpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIK-DVTEAALRK 408
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 409 TVSFVLQRAVLFSG-TIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSanFSGGQKQRLSIARGLIA 487
Cdd:PRK11288 80 GVAIIYQELHLVPEmTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY--LSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 488 KAPILILDDSTSALDAEsEKKVQQALEHELPDTTTFII-----AEKIVSVinADTILVLDDGKLVAqgTHEELLKTS 559
Cdd:PRK11288 158 NARVIAFDEPTSSLSAR-EIEQLFRVIRELRAEGRVILyvshrMEEIFAL--CDAITVFKDGRYVA--TFDDMAQVD 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
350-546 |
3.15e-16 |
|
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: 76.70 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIK-DVTEAALRKTVSFV----LQRAVLFSGTI 424
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrRSPRDAIRAGIAYVpedrKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 ASNLrqgnaqaklhelqraanmaqaseFIERYndsfdheveersanFSGGQKQRLSIARGLIAKAPILILDDSTSALDAE 504
Cdd:cd03215 96 AENI-----------------------ALSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492039060 505 SEKKVQQALeHELPDTTTFIIaekIVS------VINADTILVLDDGKL 546
Cdd:cd03215 139 AKAEIYRLI-RELADAGKAVL---LISseldelLGLCDRILVMYEGRI 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
350-565 |
4.27e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPT---KGKVKIGGQ-----NIKDvTEaalRKTVSFVLQRAVLFS 421
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEelqasNIRD-TE---RAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 G-TIASNLRQGNAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:PRK13549 96 ElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLK--LDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 501 LdAESEKKVQQALEHELP--DTTTFIIAEKI--VSVInADTILVLDDGKLV----AQGTHEELLKTSLVYQEI 565
Cdd:PRK13549 174 L-TESETAVLLDIIRDLKahGIACIYISHKLneVKAI-SDTICVIRDGRHIgtrpAAGMTEDDIITMMVGREL 244
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
345-557 |
4.57e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.35 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD-----PTKGKVKIGGQNI--KDVTEAALRKTVSFVLQRA 417
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 418 VLFSG-TIASNLRQG-------NAQAKLHELQRAA--NMAQASEFIERYNDsfdheveeRSANFSGGQKQRLSIARGLIA 487
Cdd:PRK14267 95 NPFPHlTIYDNVAIGvklnglvKSKKELDERVEWAlkKAALWDEVKDRLND--------YPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 488 KAPILILDDSTSALDAESEKKVQQALeHELPDTTTFII-------AEKIvsvinADTILVLDDGKLVAQGTHEELLK 557
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELL-FELKKEYTIVLvthspaqAARV-----SDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
350-555 |
7.38e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.46 E-value: 7.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ--NIKDvTEAALRKTVSFVLQRAVLFSG-TIAS 426
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRS-PRDAIALGIGMVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 NLRQGNAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSAL-DAES 505
Cdd:COG3845 100 NIVLGLEPTKGGRLDRKAARARIRELSERYG--LDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 506 EkkvqqalehELpdtttFIIAEKIV----SVI-----------NADTILVLDDGKLVAQG-----THEEL 555
Cdd:COG3845 178 D---------EL-----FEILRRLAaegkSIIfithklrevmaIADRVTVLRRGKVVGTVdtaetSEEEL 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
350-503 |
7.62e-16 |
|
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: 76.93 E-value: 7.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP---TKGKVKIGGQNIKdvtEAALRKTVSFVLQRAVLFSG-TIA 425
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK---PDQFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 426 SNLRQgNAQAKLHELQRAANMAQASEfIERYNDSFDHEV-EERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDA 503
Cdd:cd03234 100 ETLTY-TAILRLPRKSSDAIRKKRVE-DVLLRDLALTRIgGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
309-548 |
3.56e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 309 REVLETEPDVKfVESGSVAplsgsVEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTK 388
Cdd:COG3845 240 REVLLRVEKAP-AEPGEVV-----LEVENLSVRDDRGV-PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 389 GKVKIGGQNIKDVTEAALRKT-VSFV----LQRAVLFSGTIASNL---RQGNAQ-AKLHELQRAANMAQASEFIERYN-- 457
Cdd:COG3845 313 GSIRLDGEDITGLSPRERRRLgVAYIpedrLGRGLVPDMSVAENLilgRYRRPPfSRGGFLDRKAIRAFAEELIEEFDvr 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 458 -DSFDHEVeersANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALehelpdtttfiIAEK-------I 529
Cdd:COG3845 393 tPGPDTPA----RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL-----------LELRdagaavlL 457
|
250 260
....*....|....*....|....*
gi 492039060 530 VS-----VIN-ADTILVLDDGKLVA 548
Cdd:COG3845 458 ISedldeILAlSDRIAVMYEGRIVG 482
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
333-547 |
4.39e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.53 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI---KDVTEAALRKT 409
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQ-RAVLFSGTIASNLRQG--NAQAKLHELQRaanmaqasefieRYNDSFDH-EVEERSANF----SGGQKQRLSI 481
Cdd:PRK10908 81 IGMIFQdHHLLMDRTVYDNVAIPliIAGASGDDIRR------------RVSAALDKvGLLDKAKNFpiqlSGGEQQRVGI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADT--ILVLDDGKLV 547
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyrMLTLSDGHLH 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
329-556 |
5.39e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.81 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 329 LSGSVEFDHVSFTYPDG---DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGG----QNIKDV 401
Cdd:PRK13645 3 FSKDIILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 402 TEAA-LRKTVSFVLQ--RAVLFSGTIASNLRQGnaqaklhELQRAANMAQASEFIERYND--SFDHEVEERSA-NFSGGQ 475
Cdd:PRK13645 83 KEVKrLRKEIGLVFQfpEYQLFQETIEKDIAFG-------PVNLGENKQEAYKKVPELLKlvQLPEDYVKRSPfELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 476 KQRLSIArGLIA-KAPILILDDSTSALDAESEKKVQQALEHELPDTTTFII-----AEKIVSVinADTILVLDDGKLVAQ 549
Cdd:PRK13645 156 KRRVALA-GIIAmDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIImvthnMDQVLRI--ADEVIVMHEGKVISI 232
|
....*..
gi 492039060 550 GTHEELL 556
Cdd:PRK13645 233 GSPFEIF 239
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
348-550 |
7.33e-15 |
|
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: 73.45 E-value: 7.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPT---KGKVKIGGQNIKDVTEAAlRKTVSFVLQRAVLFsgti 424
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKY-PGEIIYVSEEDVHF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 asnlrqgnAQAKLHELQRAANMAQASEFIEryndsfdheveersaNFSGGQKQRLSIARGLIAKAPILILDDSTSALDAE 504
Cdd:cd03233 96 --------PTLTVRETLDFALRCKGNEFVR---------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492039060 505 SE---KKVQQALEHELPDTTTFII---AEKIVSVInaDTILVLDDGKLVAQG 550
Cdd:cd03233 153 TAleiLKCIRTMADVLKTTTFVSLyqaSDEIYDLF--DKVLVLYEGRQIYYG 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
348-555 |
8.15e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA-ALRKTVSFVLQRAVLFSG-TIA 425
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkAHQLGIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 426 SNLRQGNAqaklhelQRAANMAQASEFIERYNDSFDHEVEERSANFSggQKQRLSIARGLIAKAPILILDDSTSALD-AE 504
Cdd:PRK15439 105 ENILFGLP-------KRQASMQKMKQLLAALGCQLDLDSSAGSLEVA--DRQIVEILRGLMRDSRILILDEPTASLTpAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492039060 505 SEKKVQQALEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK15439 176 TERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
334-513 |
1.04e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.35 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDgdDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDvtEAALRKTVsfV 413
Cdd:PRK11248 3 QISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--PGAERGVV--F 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSGTIASNLRQGnaqAKLHELQRAANMAQASEFIERYN-DSFDHeveERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFG---LQLAGVEKMQRLEIAHQMLKKVGlEGAEK---RYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180
....*....|....*....|.
gi 492039060 493 ILDDSTSALDAESEKKVQQAL 513
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLL 171
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
333-561 |
1.44e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.37 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD-VTEAALRKTVS 411
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQ-RAVLFSGTIASNLRQGNAQAKLHELQraanmaqasEFIERYNDSFDHEVE---ERSANFSGGQKQRLSIARGLIA 487
Cdd:PRK11614 84 IVPEgRRVFSRMTVEENLAMGGFFAERDQFQ---------ERIKWVYELFPRLHErriQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 488 KAPILILDDSTSALDA----ESEKKVQQALEHELpdtTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEELLKTSLV 561
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPiiiqQIFDTIEQLREQGM---TIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
353-556 |
1.53e-14 |
|
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: 76.38 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 353 ISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIG-GQNIKDVTEAAL------RKTVSFVLQRAVLFS-GTI 424
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPdgrgraKRYIGILHQEYDLYPhRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 ASNLRQGNAQAKLHEL--QRAANMAQASEFIERYNDSFdheVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:TIGR03269 383 LDNLTEAIGLELPDELarMKAVITLKMVGFDEEKAEEI---LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 503 AESEKKVQQALEH---ELPDttTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELL 556
Cdd:TIGR03269 460 PITKVDVTHSILKareEMEQ--TFIIVSHDMDFVLdvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
22-308 |
1.84e-14 |
|
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: 74.43 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 22 IIAILVSAFSGLYQP-------KLLENIQKALMANQKQAVLSDGI-----WLVVLGIIAIISGIFNVYFAAKIAQGVVSD 89
Cdd:cd18577 2 IIGLLAAIAAGAALPlmtivfgDLFDAFTDFGSGESSPDEFLDDVnkyalYFVYLGIGSFVLSYIQTACWTITGERQARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 90 LREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQlfmqmlRLPILI--VGSFIFCIVIIprFWWAP---VVM 164
Cdd:cd18577 82 IRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGE------KLGLLIqsLSTFIAGFIIA--FIYSWkltLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 165 VA---LIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAI 241
Cdd:cd18577 154 LAtlpLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 242 MPAFQMIAYTVIALIVYLIGKNITAHPSDIAVvspfvnyVLTLLFTIMIAGMTLMQ-------FSRANISLGRI 308
Cdd:cd18577 234 LGLLFFIIFAMYALAFWYGSRLVRDGEISPGD-------VLTVFFAVLIGAFSLGQiapnlqaFAKARAAAAKI 300
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
346-505 |
1.94e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 72.29 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDvTEAALRKTVSFVLQRavlfSGtIA 425
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR----SG-IN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 426 SNLRQgnAQAKLHELQRAANMAQASEFIERYndSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAES 505
Cdd:PRK13540 87 PYLTL--RENCLYDIHFSPGAVGITELCRLF--SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
350-557 |
2.16e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIArLYDPTKgkVKIGGQ---NIKDVTEAALRKTVSFVLQRAvLFSGT--- 423
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKG--VKGSGSvllNGMPIDAKEMRAISAYVQQDD-LFIPTltv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 424 -----IASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDheVEERSANFSGGQKQRLSIARGLIAKAPILILDDST 498
Cdd:TIGR00955 117 rehlmFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIG--VPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 499 SALDAESEKKVQQALEHelpdtttfiIAEKIVSVI------------NADTILVLDDGKLVAQGTHEELLK 557
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKG---------LAQKGKTIIctihqpsselfeLFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
345-556 |
2.46e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.02 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD-----PTKGKVKIGGQNIKDVTEAALRKTVSFVLQ-RAV 418
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 419 LFSGTIASNLRQGnaqAKLHELQRAAnmaqaSEFIERYNDSFD-----HEVEER----SANFSGGQKQRLSIARGLIAKA 489
Cdd:PRK14247 94 IPNLSIFENVALG---LKLNRLVKSK-----KELQERVRWALEkaqlwDEVKDRldapAGKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 490 PILILDDSTSALDAESEKKVqQALEHELPDTTTFII-------AEKIvsvinADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKI-ESLFLELKKDMTIVLvthfpqqAARI-----SDYVAFLYKGQIVEWGPTREVF 233
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
352-515 |
2.61e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 352 DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAalrktvsfvLQRAVLFSG--------- 422
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---------YHQDLLYLGhqpgiktel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 TIASNLRqgnAQAKLHELQRAANMAQASEFI--ERYNDSFDHeveersaNFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:PRK13538 90 TALENLR---FYQRLHGPGDDEALWEALAQVglAGFEDVPVR-------QLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170
....*....|....*
gi 492039060 501 LDAESEKKVQQALEH 515
Cdd:PRK13538 160 IDKQGVARLEALLAQ 174
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
346-556 |
3.31e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.12 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA--ALRKTVSFVLQ---RAVLF 420
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQdpeQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 S---GTIASNLRQ-GNAQAKL-HELQRAANMAQASEFIERYNDSFDHeveersanfsgGQKQRLSIARGLIAKAPILILD 495
Cdd:PRK13638 93 TdidSDIAFSLRNlGVPEAEItRRVDEALTLVDAQHFRHQPIQCLSH-----------GQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 496 DSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYeiSDAVYVLRQGQILTHGAPGEVF 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
337-555 |
3.72e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.61 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 337 HVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP---TKGKVKIGGQNIKDVTEAALRKTVSfv 413
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKLRA-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSGTIAS-N--LRQGNAQAKLHELQRAANMAQASEFIERYNDS------------FDHEveersanFSGGQKQR 478
Cdd:PRK09473 97 EQISMIFQDPMTSlNpyMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAvkmpearkrmkmYPHE-------FSGGMRQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPD--TTTFIIAEKIVSVINA--DTILVLDDGKLVAQGTHEE 554
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLL-NELKRefNTAIIMITHDLGVVAGicDKVLVMYAGRTMEYGNARD 248
|
.
gi 492039060 555 L 555
Cdd:PRK09473 249 V 249
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
350-546 |
5.46e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.73 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE---AALR-KTVSFVLQRAVLFSGTIA 425
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRaKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 426 snlrQGNAQakLHELQRAAN----MAQASEFIERYN--DSFDHeveeRSANFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:PRK10584 106 ----LENVE--LPALLRGESsrqsRNGAKALLEQLGlgKRLDH----LPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492039060 500 ALDAESEKKVQQ---ALEHELpDTTTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:PRK10584 176 NLDRQTGDKIADllfSLNREH-GTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
353-513 |
8.03e-14 |
|
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: 70.60 E-value: 8.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 353 ISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAalrktvsfvLQRAVLFSGTIASNLRQGN 432
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS---------IARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 433 AQAKLHELQRAANMAQASEFIERYN-DSFDHEVeerSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQ 511
Cdd:cd03231 90 VLENLRFWHADHSDEQVEEALARVGlNGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
..
gi 492039060 512 AL 513
Cdd:cd03231 167 AM 168
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
333-514 |
1.16e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.82 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGgqnikdvteaalrKTV-- 410
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG-------------ETVkl 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQ-RAVLFSG-TIASNLRQGNAQAKL--HELQ-RAanmaqaseFIERYNdsF---DHevEERSANFSGGQKQRLSIA 482
Cdd:TIGR03719 388 AYVDQsRDALDPNkTVWEEISGGLDIIKLgkREIPsRA--------YVGRFN--FkgsDQ--QKKVGQLSGGERNRVHLA 455
|
170 180 190
....*....|....*....|....*....|..
gi 492039060 483 RGLIAKAPILILDDSTSALDAESEKKVQQALE 514
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
325-563 |
2.00e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.79 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 325 SVAPLSGsvefDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA 404
Cdd:PRK10253 4 SVARLRG----EQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 405 ALRKTVSFVLQRAVLFSGTIASNL--RQGNAQAKL-----HELQRAANMA-QASEFIERYNDSFDheveersaNFSGGQK 476
Cdd:PRK10253 78 EVARRIGLLAQNATTPGDITVQELvaRGRYPHQPLftrwrKEDEEAVTKAmQATGITHLADQSVD--------TLSGGQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 477 QRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEhELPDTTTFIIAeKIVSVIN-----ADTILVLDDGKLVAQGT 551
Cdd:PRK10253 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLS-ELNREKGYTLA-AVLHDLNqacryASHLIALREGKIVAQGA 227
|
250
....*....|..
gi 492039060 552 HEELLKTSLVYQ 563
Cdd:PRK10253 228 PKEIVTAELIER 239
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
350-557 |
2.51e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.89 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA------------------------A 405
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkekekvleklviqktrfkkikkikE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQRA--VLFSGTIASNLRQGNAQ---AKLHELQRAAnmaqasEFIERYNdsFDHEVEERSA-NFSGGQKQRL 479
Cdd:PRK13651 103 IRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSmgvSKEEAKKRAA------KYIELVG--LDESYLQRSPfELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 480 SIArGLIAKAP-ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADT--ILVLDDGKLVAQGTHEELL 556
Cdd:PRK13651 175 ALA-GILAMEPdFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTkrTIFFKDGKIIKDGDTYDIL 253
|
.
gi 492039060 557 K 557
Cdd:PRK13651 254 S 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
332-557 |
4.36e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ----------NIKDV 401
Cdd:PRK10261 14 AVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 402 TEAALRKT----VSFVLQRAVLFSGTIASNLRQGNAQAKLHE-LQRAANMAQASEFIERYNDSFDHEVEERSAN-FSGGQ 475
Cdd:PRK10261 94 SAAQMRHVrgadMAMIFQEPMTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEAQTILSRYPHqLSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 476 KQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQ---ALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTH 552
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQlikVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSV 253
|
....*
gi 492039060 553 EELLK 557
Cdd:PRK10261 254 EQIFH 258
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
336-566 |
5.31e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.43 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYPDgdDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQ 415
Cdd:PRK10575 15 RNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 RAVLFSGTIASNL-------------RQGnaQAKLHELQRAANMAQASEFIERYNDSfdheveersanFSGGQKQRLSIA 482
Cdd:PRK10575 93 QLPAAEGMTVRELvaigrypwhgalgRFG--AADREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 483 RGLIAKAPILILDDSTSALDAESEKKVQ---QALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKtS 559
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLalvHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR-G 238
|
....*..
gi 492039060 560 LVYQEIF 566
Cdd:PRK10575 239 ETLEQIY 245
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
21-226 |
7.31e-13 |
|
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: 69.44 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 21 AIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLSDGIW--LVVLGIIAIISGiFNVYFAAKIAQGVVSDLREDTYAKI 98
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLllLAVALVLALASA-LRFYLVSWLGERVVADLRKAVFAHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 99 QTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLRQ 178
Cdd:cd18575 80 LRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492039060 179 MNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQ 226
Cdd:cd18575 160 VRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEA 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
350-556 |
7.92e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.38 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVT-EAALRKTVSFVLQRAVLFSGTIASNL 428
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRLSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 429 RQGNAQAKlHELQRAANMAQASEFIERYNDSfdHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKK 508
Cdd:PRK10895 99 LMAVLQIR-DDLSAEQREDRANELMEEFHIE--HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492039060 509 VQQALEHELPDTTTFIIAEKIV--SVINADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK10895 176 IKRIIEHLRDSGLGVLITDHNVreTLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
349-554 |
9.77e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.52 E-value: 9.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 349 TLKDISFKIK---PGQMV-GIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE----AALRKTVSFVLQRAVLF 420
Cdd:PRK11144 9 QLGDLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiclPPEKRRIGYVFQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SG-TIASNLRQGnaqaklhelqraanMAQASefieryNDSFDHEVE--------ER-SANFSGGQKQRLSIARGLIAKAP 490
Cdd:PRK11144 89 PHyKVRGNLRYG--------------MAKSM------VAQFDKIVAllgiepllDRyPGSLSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 491 ILILDDSTSALDAESEKKVQQALEHELPDTTTFII-----AEKIVSVinADTILVLDDGKLVAQGTHEE 554
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLPYLERLAREINIPILyvshsLDEILRL--ADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
350-502 |
9.79e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.04 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALRKTVSFVLQ---------RA 417
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqALRRDIQFIFQdpyasldprQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 418 VLFSgtIASNLR-----QGNAQAKlhelqRAANMAQASEFIERYNDSFDHEveersanFSGGQKQRLSIARGLIAKAPIL 492
Cdd:PRK10261 420 VGDS--IMEPLRvhgllPGKAAAA-----RVAWLLERVGLLPEHAWRYPHE-------FSGGQRQRICIARALALNPKVI 485
|
170
....*....|
gi 492039060 493 ILDDSTSALD 502
Cdd:PRK10261 486 IADEAVSALD 495
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
336-520 |
1.81e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.96 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGK------VKIG----------GQNIK 399
Cdd:TIGR03719 8 NRVSKVVP-PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEarpqpgIKVGylpqepqldpTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 400 DVTEAALRKTVSfVLQR----AVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSF-----DHEVEersaN 470
Cdd:TIGR03719 87 ENVEEGVAEIKD-ALDRfneiSAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALrcppwDADVT----K 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492039060 471 FSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDT 520
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPGT 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
345-553 |
1.90e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIA--RLYDPTKGKVKIGGQNIKDVT-EAALRKTVSFVLQRAVLFS 421
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 GTiaSN---LRQG-NAQAKLHELqraaNMAQASEFIERYND-----SFDHEVEERSAN--FSGGQKQRLSIARGLIAKAP 490
Cdd:CHL00131 98 GV--SNadfLRLAyNSKRKFQGL----PELDPLEFLEIINEklklvGMDPSFLSRNVNegFSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 491 ILILDDSTSALDAESEKKVQQALeHELPDTTTFIIA----EKIVSVINADTILVLDDGKLVAQGTHE 553
Cdd:CHL00131 172 LAILDETDSGLDIDALKIIAEGI-NKLMTSENSIILithyQRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
346-558 |
2.18e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.42 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKS-TLAQLIARLydP-----TKGKVKIGGQnikDVTEAALR-KTVSFVLQ--R 416
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PagvrqTAGRVLLDGK---PVAPCALRgRKIATIMQnpR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 417 AvlfsgtiASN-LRQGNAQAK--LHELQRAANMAQASEFIERYNDSFDHEVEERSA-NFSGGQKQRLSIARGLIAKAPIL 492
Cdd:PRK10418 90 S-------AFNpLHTMHTHARetCLALGKPADDATLTAALEAVGLENAARVLKLYPfEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHelpdtttfIIAEK-----IVS----VIN--ADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLES--------IVQKRalgmlLVThdmgVVArlADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
352-502 |
2.37e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.26 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 352 DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ-----NIKDVTEAALRKTV----SFVLQRAvlfsg 422
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLLrtewGFVHQHP----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 tiASNLRQG-NAQAKLHELQRAANM-------AQASEFIERyndsfdheVE-------ERSANFSGGQKQRLSIARGLIA 487
Cdd:PRK11701 99 --RDGLRMQvSAGGNIGERLMAVGArhygdirATAGDWLER--------VEidaaridDLPTTFSGGMQQRLQIARNLVT 168
|
170
....*....|....*
gi 492039060 488 KAPILILDDSTSALD 502
Cdd:PRK11701 169 HPRLVFMDEPTGGLD 183
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
348-551 |
4.18e-12 |
|
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: 69.66 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAaLRKTVSFVLQRAVLFSGTIASN 427
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDA-VRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 428 LRQGNAQAKlhelQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEK 507
Cdd:TIGR01257 1023 HILFYAQLK----GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492039060 508 KVQQALEHELPDTTTFIIAEKIVSV-INADTILVLDDGKLVAQGT 551
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
348-556 |
5.64e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVT-EAAL----------RKTVSFVLQR 416
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLangivyisedRKRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 417 AVLFSGTIASnLRQGNAQAKlhELQRAANMAQASEFIERYN---DSFDHEVeersANFSGGQKQRLSIARGLIAKAPILI 493
Cdd:PRK10762 346 SVKENMSLTA-LRYFSRAGG--SLKHADEQQAVSDFIRLFNiktPSMEQAI----GLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 494 LDDSTSALDAESEKKVQQaLEHELPDTTTFIIaekIVS-----VIN-ADTILVLDDGKL-----VAQGTHEELL 556
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQ-LINQFKAEGLSII---LVSsempeVLGmSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
350-547 |
5.99e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.36 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLY--DPTKGKVKIGGQNIKDvtEAALrktvsfvlqravlfsgtIASN 427
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--EASL-----------------IDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 428 LRQGNAQAKLhELQRAANMAQASEFIERYndsfdheveersANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEK 507
Cdd:COG2401 107 GRKGDFKDAV-ELLNAVGLSDAVLWLRRF------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492039060 508 KVQQALeHELPDT--TTFIIA---EKIVSVINADTILVLDDGKLV 547
Cdd:COG2401 174 RVARNL-QKLARRagITLVVAthhYDVIDDLQPDLLIFVGYGGVP 217
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
350-560 |
6.15e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.35 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAvlfsgTIASNLR 429
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP-----STSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 430 QgnaqaklhelqraaNMAQASEFIERYNDSFDHEVEERSAN-------------------FSGGQKQRLSIARGLIAKAP 490
Cdd:PRK15112 104 Q--------------RISQILDFPLRLNTDLEPEQREKQIIetlrqvgllpdhasyyphmLAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 491 ILILDDSTSALDAESEKK-VQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELLKTSL 560
Cdd:PRK15112 170 VIIADEALASLDMSMRSQlINLMLELQEKQGISYIYVTQHLGMMKhiSDQVLVMHQGEVVERGSTADVLASPL 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
350-550 |
7.10e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA-ALRKTVSFVLQR-AVLFSGTIASN 427
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 428 LRQGNAQAK----LHELQRAANMAQASEFIERYNDSFDheVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSAL-D 502
Cdd:PRK09700 101 LYIGRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVD--LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtN 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492039060 503 AESEK--KVQQALEHElpDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQG 550
Cdd:PRK09700 179 KEVDYlfLIMNQLRKE--GTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
350-495 |
9.09e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.05 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikDVTEAAL----RKTVSFVLQRAVLFSG-TI 424
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE---DITHLPMhkraRLGIGYLPQEASIFRKlTV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 425 ASNLRqgnAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILD 495
Cdd:COG1137 96 EDNIL---AVLELRKLSKKEREERLEELLEEFG--ITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
350-558 |
9.46e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.26 E-value: 9.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI-KDvtEAALRKTVSFVL-QRAVLF------- 420
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPfKR--RKEFARRIGVVFgQRSQLWwdlpaid 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SGTIasnlrqgnaQAKLHELQRAANMAQASEFIERYndsfdhEVEE------RsaNFSGGQKQRLSIARGLIAKAPILIL 494
Cdd:COG4586 116 SFRL---------LKAIYRIPDAEYKKRLDELVELL------DLGElldtpvR--QLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 495 DDSTSALDAESEKKVQQAL-----EHElpdtTTFIIA-------EKIvsvinADTILVLDDGKLVAQGTHEELLKT 558
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLkeynrERG----TTILLTshdmddiEAL-----CDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
343-513 |
1.06e-11 |
|
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: 64.19 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 343 PDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP--TKGKVKIGGQNIKDvteaALRKTVSFVLQRAVLF 420
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDK----NFQRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SG-TIASNLRqgnAQAKLHELqraanmaqasefieryndsfdheveersanfSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:cd03232 92 PNlTVREALR---FSALLRGL-------------------------------SVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170
....*....|....
gi 492039060 500 ALDAESEKKVQQAL 513
Cdd:cd03232 138 GLDSQAAYNIVRFL 151
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
333-514 |
1.98e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.68 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGgqnikdvteaalrKTV-- 410
Cdd:PRK11819 325 IEAENLSKSF--GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG-------------ETVkl 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQ-RAVLFSG-TIASNLRQGNAQAKLHELQ---RAanmaqaseFIERYNdsF---DHevEERSANFSGGQKQRLSIA 482
Cdd:PRK11819 390 AYVDQsRDALDPNkTVWEEISGGLDIIKVGNREipsRA--------YVGRFN--FkggDQ--QKKVGVLSGGERNRLHLA 457
|
170 180 190
....*....|....*....|....*....|..
gi 492039060 483 RGLIAKAPILILDDSTSALDAESEKKVQQALE 514
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
346-552 |
2.00e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.43 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIA--RLYDPTKGKVKIGGQNIKDVT-EAALRKTVSFVLQRAV---- 418
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVeipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 419 ----LFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDsfdheVEERSAN--FSGGQKQRLSIARGLIAKAPIL 492
Cdd:PRK09580 93 vsnqFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPED-----LLTRSVNvgFSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELPDTTTFIIA---EKIVSVINADTILVLDDGKLVAQGTH 552
Cdd:PRK09580 168 ILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
351-546 |
3.41e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 351 KDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI-KDVTEAALRKTVSFV---LQRAVLFsgtIAS 426
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInALSTAQRLARGLVYLpedRQSSGLY---LDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 NLRQGNAQAKLHELQRAANMAQASEFIERY----NDSFDHEvEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:PRK15439 357 PLAWNVCALTHNRRGFWIKPARENAVLERYrralNIKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 503 AESEKKVQQALEHelpdtttfiIAEKIVSVI-----------NADTILVLDDGKL 546
Cdd:PRK15439 436 VSARNDIYQLIRS---------IAAQNVAVLfissdleeieqMADRVLVMHQGEI 481
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
341-503 |
5.12e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.48 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 341 TYpDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVtEAALRKtVSFVLQRAVLF 420
Cdd:PRK11650 12 SY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL-EPADRD-IAMVFQNYALY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SG-TIASNLRQG--NAQAKLHELQR----AANMAQASEFIERyndsfdheveeRSANFSGGQKQRLSIARGLIAKAPILI 493
Cdd:PRK11650 89 PHmSVRENMAYGlkIRGMPKAEIEErvaeAARILELEPLLDR-----------KPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170
....*....|
gi 492039060 494 LDDSTSALDA 503
Cdd:PRK11650 158 FDEPLSNLDA 167
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
329-502 |
7.22e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 329 LSGSVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVK------IGGQNIKDVT 402
Cdd:PRK09544 1 MTSLVSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKrngklrIGYVPQKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 403 EAALRKTVS-FVLQRAVLFSGTIASNLRQGNAQaklhelqraanmaqasefieryndsfdHEVEERSANFSGGQKQRLSI 481
Cdd:PRK09544 79 DTTLPLTVNrFLRLRPGTKKEDILPALKRVQAG---------------------------HLIDAPMQKLSGGETQRVLL 131
|
170 180
....*....|....*....|.
gi 492039060 482 ARGLIAKAPILILDDSTSALD 502
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVD 152
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
350-556 |
1.22e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.17 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGT------ 423
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMpvfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 424 ---IASNLRQGNAQAKLHELQRAANMAqasefiERYNDSFDHeveersanFSGGQKQRLSIARGLI-------AKAPILI 493
Cdd:COG4138 91 alhQPAGASSEAVEQLLAQLAEALGLE------DKLSRPLTQ--------LSGGEWQRVRLAAVLLqvwptinPEGQLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 494 LDDSTSALDAesekkVQQALehelpdTTTFI--IAEKIVSVI------N-----ADTILVLDDGKLVAQGTHEELL 556
Cdd:COG4138 157 LDEPMNSLDV-----AQQAA------LDRLLreLCQQGITVVmsshdlNhtlrhADRVWLLKQGKLVASGETAEVM 221
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
350-563 |
1.24e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIA-RLYDPT-------KGKVKIGGQNIKDVTE---AALRKTVSFVLQRAV 418
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAprlARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 419 LFSGTiasnlrqgnaqaKLHELQRAANMAQASEFIERYNDSFDHEVEERSAN---------FSGGQKQRLSIARGL---- 485
Cdd:PRK13547 97 AFSAR------------EIVLLGRYPHARRAGALTHRDGEIAWQALALAGATalvgrdvttLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 486 -----IAKAPILILDDSTSALDAesekkvqqALEHELPDTTTFIIAE------KIVSVIN-----ADTILVLDDGKLVAQ 549
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDL--------AHQHRLLDTVRRLARDwnlgvlAIVHDPNlaarhADRIAMLADGAIVAH 236
|
250
....*....|....
gi 492039060 550 GTHEELLKTSLVYQ 563
Cdd:PRK13547 237 GAPADVLTPAHIAR 250
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
21-308 |
1.51e-10 |
|
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: 62.51 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 21 AIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYAKIQ 99
Cdd:cd18546 4 ALLLVVVDTAASLAGPLLVRYgIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 100 TFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLfmqmlrLPILIVGSFIFCIVIIPRFWWAP----VVMVALIFGFGAYV 175
Cdd:cd18546 84 RLSLDFHERETSGRIMTRMTSDIDALSELLQTG------LVQLVVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 176 LRQMNSLFTkFQEMMDRISN---QAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTV 252
Cdd:cd18546 158 WFRRRSSRA-YRRARERIAAvnaDLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 253 IALIVYLIGKNITAHPSDIAVVSPFVNYvLTLLFT-IMIAGMTLMQFSRANISLGRI 308
Cdd:cd18546 237 TAAVLLVGAWRVAAGTLTVGVLVAFLLY-LRRFFApIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
59-226 |
2.31e-10 |
|
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: 62.14 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 59 IWLVVLGI--IAIISGIF---NVYFAAKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLF 133
Cdd:cd18564 53 LLLAAAALvgIALLRGLAsyaGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 134 mqmlrLPIL-----IVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVK 208
Cdd:cd18564 133 -----LPLLtnlltLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQ 207
|
170
....*....|....*...
gi 492039060 209 SFNQGPQEIKKFDQTSDQ 226
Cdd:cd18564 208 AFGREEHEERRFARENRK 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
350-513 |
2.45e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.18 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLY--DPTKGK--------VKIGGQNIKDVTEAalRKTVSFVLQRAVL 419
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShiellgrtVQREGRLARDIRKS--RANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 420 FS----------GTIASN------LRQGNAQAKLHELQRAANMAQAsefieryndsfdHEVEERSANFSGGQKQRLSIAR 483
Cdd:PRK09984 98 VNrlsvlenvliGALGSTpfwrtcFSWFTREQKQRALQALTRVGMV------------HFAHQRVSTLSGGQQQRVAIAR 165
|
170 180 190
....*....|....*....|....*....|
gi 492039060 484 GLIAKAPILILDDSTSALDAESEKKVQQAL 513
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTL 195
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
347-569 |
2.45e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.10 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 347 DPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPTKGKVKIGGQNIKDVTEAAL-RKTVSFVLQRAVLFSGTI- 424
Cdd:PRK03695 9 STRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 -------ASNLRQGNAQAKLHELQRAANMAqasefierynDSFdheveERSAN-FSGGQKQR-------LSIARGLIAKA 489
Cdd:PRK03695 88 qyltlhqPDKTRTEAVASALNEVAEALGLD----------DKL-----GRSVNqLSGGEWQRvrlaavvLQVWPDINPAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 490 PILILDDSTSALDAESEKKVQQALEHelpdtttfiIAEKIVSVI-----------NADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSE---------LCQQGIAVVmsshdlnhtlrHADRVWLLKQGKLLASGRRDEVLTP 223
|
250
....*....|.
gi 492039060 559 SlVYQEIFKTQ 569
Cdd:PRK03695 224 E-NLAQVFGVN 233
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
336-558 |
4.48e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.30 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYPDGDDP--TLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD-PTK---GKVKIGGQNIKDVTEAALRK- 408
Cdd:PRK11022 7 DKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRvmaEKLEFNGQDLQRISEKERRNl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 409 ---TVSFVLQRA---------VLFSGTIASNLRQGNAQAKLHelQRAANM-------AQASEFierynDSFDHEVeersa 469
Cdd:PRK11022 87 vgaEVAMIFQDPmtslnpcytVGFQIMEAIKVHQGGNKKTRR--QRAIDLlnqvgipDPASRL-----DVYPHQL----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 470 nfSGGQKQRLSIARGLIAKAPILILDDSTSALDA-----------ESEKKVQQAL---EHELPdtttfIIAEKivsvinA 535
Cdd:PRK11022 155 --SGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaqiielllELQQKENMALvliTHDLA-----LVAEA------A 221
|
250 260
....*....|....*....|...
gi 492039060 536 DTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK11022 222 HKIIVMYAGQVVETGKAHDIFRA 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
333-565 |
5.31e-10 |
|
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: 61.76 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLY--DPTKGKVKIGGQ-----NIKDvTEaa 405
Cdd:TIGR02633 2 LEMKGIVKTF--GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSplkasNIRD-TE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 lRKTVSFVLQRAVLFSG-TIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARG 484
Cdd:TIGR02633 77 -RAGIVIIHQELTLVPElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 485 LIAKAPILILDDSTSALdAESEKKVQQALEHELP--DTTTFIIAEKIVSVIN-ADTILVLDDGKLVA----QGTHEELLK 557
Cdd:TIGR02633 156 LNKQARLLILDEPSSSL-TEKETEILLDIIRDLKahGVACVYISHKLNEVKAvCDTICVIRDGQHVAtkdmSTMSEDDII 234
|
....*...
gi 492039060 558 TSLVYQEI 565
Cdd:TIGR02633 235 TMMVGREI 242
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
259-507 |
7.52e-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: 62.34 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 259 LIGKNITAhpsdiAVVSPFVNYVLTLLFTimiagmtlMQFSRANISLGRIREVLETEPDVKFVESGSVapLSGS-----V 333
Cdd:TIGR01257 1874 LIGKNLVA-----MAVEGVVYFLLTLLIQ--------HHFFLSRWIAEPAKEPIFDEDDDVAEERQRI--ISGGnktdiL 1938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ----NIKDVTEA----- 404
Cdd:TIGR01257 1939 RLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISDVHQNmgycp 2018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 405 ALRKTVSFVLQRAVLFsgtIASNLRQGNAQaklhELQRAANMAQASEFIERYNDSFdheveerSANFSGGQKQRLSIARG 484
Cdd:TIGR01257 2019 QFDAIDDLLTGREHLY---LYARLRGVPAE----EIEKVANWSIQSLGLSLYADRL-------AGTYSGGNKRKLSTAIA 2084
|
250 260
....*....|....*....|...
gi 492039060 485 LIAKAPILILDDSTSALDAESEK 507
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARR 2107
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
338-505 |
8.97e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 338 VSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKV------KIG----------GQNIKDV 401
Cdd:PRK11819 12 VSKVVP-PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEArpapgiKVGylpqepqldpEKTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 402 TEAALRKTVSfVLQRavlFSGtIASNLrqGNAQAKLHELqrAANMAQASEFIERYN-DSFDHEVE------------ERS 468
Cdd:PRK11819 91 VEEGVAEVKA-ALDR---FNE-IYAAY--AEPDADFDAL--AAEQGELQEIIDAADaWDLDSQLEiamdalrcppwdAKV 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 492039060 469 ANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAES 505
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
333-555 |
1.23e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.39 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTypDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---RKT 409
Cdd:PRK11831 8 VDMRGVSFT--RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVLFSG-----TIASNLRQGNA--QAKLHE----------LQRAANMaqasefieryndsfdheveeRSANFS 472
Cdd:PRK11831 86 MSMLFQSGALFTDmnvfdNVAYPLREHTQlpAPLLHStvmmkleavgLRGAAKL--------------------MPSELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 473 GGQKQRLSIARGlIAKAPILIL-DDSTSALDAESEK---KVQQALEHELpDTTTFIIAEKIVSVIN-ADTILVLDDGKLV 547
Cdd:PRK11831 146 GGMARRAALARA-IALEPDLIMfDEPFVGQDPITMGvlvKLISELNSAL-GVTCVVVSHDVPEVLSiADHAYIVADKKIV 223
|
....*...
gi 492039060 548 AQGTHEEL 555
Cdd:PRK11831 224 AHGSAQAL 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
357-542 |
1.41e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 357 IKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKV----KIG--GQNIKDVTEAalrkTVSFVLQRAvlfSGTIASNLRQ 430
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelKISykPQYIKPDYDG----TVEDLLRSI---TDDLGSSYYK 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 431 gnaqaklhelqraanmaqaSEFIERYN--DSFDHEVEErsanFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKK 508
Cdd:PRK13409 435 -------------------SEIIKPLQleRLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190
....*....|....*....|....*....|....*...
gi 492039060 509 VQQALEH--ELPDTTTFIIAEKIVsVIN--ADTILVLD 542
Cdd:PRK13409 492 VAKAIRRiaEEREATALVVDHDIY-MIDyiSDRLMVFE 528
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
341-504 |
1.48e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 341 TYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAalrktvsfvlqRAVLF 420
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS-----------RFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SGTIASNLRQGNAQAKLHEL-----QRAANMAQASEFIERYNDSFDHEVEERSAnfsgGQKQRLSIARGLIAKAPILILD 495
Cdd:PRK13543 87 LGHLPGLKADLSTLENLHFLcglhgRRAKQMPGSALAIVGLAGYEDTLVRQLSA----GQKKRLALARLWLSPAPLWLLD 162
|
....*....
gi 492039060 496 DSTSALDAE 504
Cdd:PRK13543 163 EPYANLDLE 171
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
345-555 |
1.55e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAqLIARLYDPTKGKvKIGGQNIKDVTEAALRKTVSF----VLQRAVLF 420
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR-RPWRF*TWCANRRALRRTIG*hrpvR*GRRESF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SGTiaSNLRQgnaQAKLHELQRAANMAQASEFIERYndSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:NF000106 102 SGR--ENLYM---IGR*LDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 501 LDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEEL 555
Cdd:NF000106 175 LDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
338-558 |
3.01e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 338 VSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPT------KGKVKIGGQNIKDVTEAALRKT-- 409
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTLRGVrg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 --VSFVLQRAVLFSGTIASNLRQGNAQAKLHE-LQRAANMAQASEFIERYNDsfdHEVEERSANF----SGGQKQRLSIA 482
Cdd:PRK15134 92 nkIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRgMRREAARGEILNCLDRVGI---RQAAKRLTDYphqlSGGERQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 483 RGLIAKAPILILDDSTSALDAESEKKVQQ---ALEHELPDTTTFIIAE-KIVSVInADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQllrELQQELNMGLLFITHNlSIVRKL-ADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
57-303 |
7.65e-09 |
|
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: 57.10 E-value: 7.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 57 DGIWLVVL--GIIAIISGIFN---VYFAAKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDmnqvmnmmmq 131
Cdd:cd18540 39 DGLTGFILlyLGLILIQALSVflfIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSD---------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 132 lfmqMLRLP--------------ILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQA 197
Cdd:cd18540 109 ----TQRLGeiiswglvdlvwgiTYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 198 QETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIvIGYWFSAI-MPAFQMIAYTVIALIVYLIGKNITAHPSDIAVVSP 276
Cdd:cd18540 185 NEGITGAKTTKTLVREEKNLREFKELTEEMRRASV-RAARLSALfLPIVLFLGSIATALVLWYGGILVLAGAITIGTLVA 263
|
250 260
....*....|....*....|....*....
gi 492039060 277 FVNYVLTLLFTIMIAGMTL--MQFSRANI 303
Cdd:cd18540 264 FISYATQFFEPIQQLARVLaeLQSAQASA 292
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
305-513 |
8.34e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.33 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 305 LGRIREVLeTEPDVKF-VESGSVAPLSGSVEFDHVSFTYPDGddPTL-KDISFKIKPGQMVGIVGATGAGKSTLAQLIAR 382
Cdd:PLN03073 481 LGHVDAVV-NDPDYKFeFPTPDDRPGPPIISFSDASFGYPGG--PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 383 LYDPTKG------KVKIGGQNIKDVTeaALRKTVSFVLQRAVLFSGTIASNLRqgnaqAKLHELQRAANMAQASEFiery 456
Cdd:PLN03073 558 ELQPSSGtvfrsaKVRMAVFSQHHVD--GLDLSSNPLLYMMRCFPGVPEQKLR-----AHLGSFGVTGNLALQPMY---- 626
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 457 ndsfdheveersaNFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQAL 513
Cdd:PLN03073 627 -------------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL 670
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
356-542 |
1.11e-08 |
|
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: 57.87 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 356 KIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVkiggqnikdvtEAALRktVSFVLQR-AVLFSGTIASNLRQGNAQ 434
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLK--ISYKPQYiSPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 435 AklhelqRAANMAQaSEFIERYN--DSFDHEVEErsanFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQA 512
Cdd:COG1245 429 D------FGSSYYK-TEIIKPLGleKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 497
|
170 180 190
....*....|....*....|....*....|....
gi 492039060 513 LEH--ELPDTTTFIIAEKIVsVIN--ADTILVLD 542
Cdd:COG1245 498 IRRfaENRGKTAMVVDHDIY-LIDyiSDRLMVFE 530
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
352-502 |
2.12e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.06 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 352 DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIkDVTEAALRKTVSFVLQRAVLFSG-TIASNLrq 430
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAGDIATRRRVGYMSQAFSLYGElTVRQNL-- 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 431 gNAQAKLHELQRAANMAQASEFIERyndsFD--HEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:NF033858 361 -ELHARLFHLPAAEIAARVAEMLER----FDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
336-553 |
2.71e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.27 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNikdvTEAALRKT-VSFVL 414
Cdd:PRK15056 10 NDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP----TRQALQKNlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 415 QR-------AVLFSGTIASNlRQGNA----QAKLHELQRaanmaqASEFIERYnDSFDHEvEERSANFSGGQKQRLSIAR 483
Cdd:PRK15056 85 QSeevdwsfPVLVEDVVMMG-RYGHMgwlrRAKKRDRQI------VTAALARV-DMVEFR-HRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 484 GLIAKAPILILDDSTSALDAESEKKVqQALEHELPD--TTTFIIAEKIVSVINADTILVLDDGKLVAQGTHE 553
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARI-ISLLRELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
340-550 |
3.05e-08 |
|
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: 54.72 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 340 FTYP----DGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIggqnikdvteaaLRKTVSFVLQ 415
Cdd:cd03237 1 YTYPtmkkTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI------------ELDTVSYKPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 ravlfsgTIASNlRQGNAQAKLHE-LQRAANMAQ-ASEFIE--RYNDSFDHEVEErsanFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03237 69 -------YIKAD-YEGTVRDLLSSiTKDFYTHPYfKTEIAKplQIEQILDREVPE----LSGGELQRVAIAACLSKDADI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHelpdtttFII-AEKIVSVINADTILV--LDDGKLVAQG 550
Cdd:cd03237 137 YLLDEPSAYLDVEQRLMASKVIRR-------FAEnNEKTAFVVEHDIIMIdyLADRLIVFEG 191
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
21-259 |
3.56e-08 |
|
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: 55.21 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 21 AIIAILVSAFSGLYQP----KLLENIQKALMANQKQAVLSDGIWLVVLGIIAIiSGIFN---VYFAAKIAQGVVSDLRED 93
Cdd:cd18573 1 ALALLLVSSAVTMSVPfaigKLIDVASKESGDIEIFGLSLKTFALALLGVFVV-GAAANfgrVYLLRIAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 94 TYAKI--QTFSFGNIKKfsAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFI--FCI---------VIIPrfwwa 160
Cdd:cd18573 80 LFKSIlrQDAAFFDKNK--TGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGmmLYIspkltlvmlLVVP----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 161 PVVMVALIFGfgayvlRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSA 240
Cdd:cd18573 153 PIAVGAVFYG------RYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGL 226
|
250
....*....|....*....
gi 492039060 241 IMPAFQMIAYTVIALIVYL 259
Cdd:cd18573 227 FFGSTGFSGNLSLLSVLYY 245
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
336-513 |
1.01e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIgGQNIKdvteaalrktVSFVLQ 415
Cdd:PRK10636 316 EKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK----------LGYFAQ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 RAVLFsgtiasnLRQGnaQAKLHELQRAAnmAQASEFIER-YNDSFDHE---VEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:PRK10636 383 HQLEF-------LRAD--ESPLQHLARLA--PQELEQKLRdYLGGFGFQgdkVTEETRRFSGGEKARLVLALIVWQRPNL 451
|
170 180
....*....|....*....|..
gi 492039060 492 LILDDSTSALDAESEKKVQQAL 513
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQALTEAL 473
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
333-556 |
1.08e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIA---RLYDptkGKVKI-GGqnikDVTEAALRK 408
Cdd:NF033858 2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgarKIQQ---GRVEVlGG----DMADARHRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 409 TVS----FVLQravlfsG---------TIASNLR-------QGNAQ--AKLHELQRAANMAqasEFIERyndsfdhevee 466
Cdd:NF033858 73 AVCpriaYMPQ------GlgknlyptlSVFENLDffgrlfgQDAAErrRRIDELLRATGLA---PFADR----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 467 RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESekKVQ-----QALEHELPDtttfiiaekiVSVINA------ 535
Cdd:NF033858 133 PAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS--RRQfweliDRIRAERPG----------MSVLVAtaymee 200
|
250 260
....*....|....*....|....*
gi 492039060 536 ----DTILVLDDGKLVAQGTHEELL 556
Cdd:NF033858 201 aerfDWLVAMDAGRVLATGTPAELL 225
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
359-514 |
1.26e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.22 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 359 PGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVK-IGGQNIKDVTEAALRKTVsfvlqravlfsgtiasnlrqgnaqakl 437
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 438 helqraanmaqasefieryndsfdheVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALE 514
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
20-308 |
1.67e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 52.87 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 20 CAIIAILVSAFSGLYQPKLLENIQKALMANqKQAVLSDGIWLVV-LGIIAIISGIFN---VYFAAKIAQGVVSDLREDTY 95
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSY-PDEPLSEGYLLALaLFLVSLLQSLLLhqyFFLSFRLGMRVRSALSSLIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 96 AKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLrLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYV 175
Cdd:cd18579 80 RKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWS-APLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 176 LRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFN-QGP----------QEIKkfdqtsdQLNDYNIVIGyWFSAIMPA 244
Cdd:cd18579 159 AKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAwEKPflkrieelrkKELK-------ALRKFGYLRA-LNSFLFFS 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 245 FQMIAyTVIALIVY-LIGKNITAhpsdiAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18579 231 TPVLV-SLATFATYvLLGNPLTA-----AKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
350-547 |
2.23e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPT---KGKVKIGGQ-----NIKDvTEAalrKTVSFVLQRAVLFS 421
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkDIRD-SEA---LGIVIIHQELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 G-TIASNLRQGNAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:NF040905 92 YlSIAENIFLGNERAKRGVIDWNETNRRARELLAKVG--LDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492039060 501 L-DAESEKKVQQALEHELPDTTTFIIAEK---IVSVinADTILVLDDGKLV 547
Cdd:NF040905 170 LnEEDSAALLDLLLELKAQGITSIIISHKlneIRRV--ADSITVLRDGRTI 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
345-547 |
4.09e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIAR--LYDptKGKVKIGgqniKDVteaalrkTVSFVLQ---RAVl 419
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevLLD--DGRIIYE----QDL-------IVARLQQdppRNV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 420 fSGTIASNLRQG-NAQAKL----HELQRA----------ANMAQASEFIERYN----DSFDHEV--------EERSANFS 472
Cdd:PRK11147 80 -EGTVYDFVAEGiEEQAEYlkryHDISHLvetdpseknlNELAKLQEQLDHHNlwqlENRINEVlaqlgldpDAALSSLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 473 GGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEhELPDTTTFIIAEKivSVIN--ADTILVLDDGKLV 547
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK-TFQGSIIFISHDR--SFIRnmATRIVDLDRGKLV 232
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
350-395 |
5.84e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.20 E-value: 5.84e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGG 395
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
52-308 |
6.25e-07 |
|
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: 51.41 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 52 QAVLSDGIWLVVLGIIAIISGIFNVYFAAkIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQ 131
Cdd:cd18565 52 QLWLLGGLTVAAFLLESLFQYLSGVLWRR-FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 132 LFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFN 211
Cdd:cd18565 131 GANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 212 QGPQEIKKFDQTSDQLNDYN---IVIGYWFSAIMPAFQMIAYTVIALI---VYLIGKNITAHPSDIAVVSPFVNYVLTLL 285
Cdd:cd18565 211 AEDFERERVADASEEYRDANwraIRLRAAFFPVIRLVAGAGFVATFVVggyWVLDGPPLFTGTLTVGTLVTFLFYTQRLL 290
|
250 260
....*....|....*....|...
gi 492039060 286 FTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18565 291 WPLTRLGDLIDQYQRAMASAKRV 313
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
350-548 |
7.77e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ--NIKDVTEaALRKTVSF-------VLQRAVLf 420
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSKE-ALENGISMvhqelnlVLQRSVM- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 sgtiaSNLRQGNAQAKlhelqraanmaqaSEFIER---YNDS--------FDHEVEERSANFSGGQKQRLSIARGLIAKA 489
Cdd:PRK10982 92 -----DNMWLGRYPTK-------------GMFVDQdkmYRDTkaifdeldIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 490 PILILDDSTSALdaeSEKKVQQALE--HELPDTTTFII-----AEKIVSVinADTILVLDDGKLVA 548
Cdd:PRK10982 154 KIVIMDEPTSSL---TEKEVNHLFTiiRKLKERGCGIVyishkMEEIFQL--CDEITILRDGQWIA 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
331-555 |
7.84e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 331 GSVEFDHVSFTYPDGDDPTLK---DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPTK--GKVKIGGQNIK-----D 400
Cdd:PRK13549 256 GEVILEVRNLTAWDPVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIFIDGKPVKirnpqQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 401 VTEAAL------RKTVSFVLQRAVLFSGTIASnLRQgnaQAKLHELQRAANMAQASEFIERYNDSFDHeVEERSANFSGG 474
Cdd:PRK13549 335 AIAQGIamvpedRKRDGIVPVMGVGKNITLAA-LDR---FTGGSRIDDAAELKTILESIQRLKVKTAS-PELAIARLSGG 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 475 QKQRLSIARGLIAKAPILILDDSTSALD--AESE------KKVQQAL-----EHELPDtttfiiaekIVSVinADTILVL 541
Cdd:PRK13549 410 NQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYEiyklinQLVQQGVaiiviSSELPE---------VLGL--SDRVLVM 478
|
250
....*....|....
gi 492039060 542 DDGKLVAQGTHEEL 555
Cdd:PRK13549 479 HEGKLKGDLINHNL 492
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
350-550 |
1.27e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIA-RLYDPTKGK---VKIGGQNIKDVtEAALRKTVSFVLQRAVLF-SGTI 424
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsNTDGFHIGVegvITYDGITPEEI-KKHYRGDVVYNAETDVHFpHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 ASNLrqgNAQAKLHELQRAANMAQASEFIERYND------SFDHEVEERSAN-----FSGGQKQRLSIARGLIAKAPILI 493
Cdd:TIGR00956 156 GETL---DFAARCKTPQNRPDGVSREEYAKHIADvymatyGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 494 LDDSTSALDAESEKKVQQALE---HELPDTTTFII---AEKIVSVInaDTILVLDDGKLVAQG 550
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALKtsaNILDTTPLVAIyqcSQDAYELF--DKVIVLYEGYQIYFG 293
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
353-554 |
1.39e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 353 ISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI-----KDVTEAAL------RKTVSFVLQRAVlfS 421
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirspRDAIRAGImlcpedRKAEGIIPVHSV--A 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 GTIASNLRQGNAQAK--LHELQRAANmaqASEFIERYNdsfdheVEERSA-----NFSGGQKQRLSIARGLIAKAPILIL 494
Cdd:PRK11288 350 DNINISARRHHLRAGclINNRWEAEN---ADRFIRSLN------IKTPSReqlimNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 495 DDSTSALDAESEKKVQQALeHELPDT--TTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEE 554
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVI-YELAAQgvAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
21-261 |
1.49e-06 |
|
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: 50.23 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 21 AIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLSDGIwlVVLGIIAIISGIFN---VYFAAKIAQGVVSDLREDTYAK 97
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAV--LLLLLLSVLSGLFSglrGGCFSYAGTRLVRRLRRDLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 98 I--QTFSFgnIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPR-----FwwAPVVMVALIFG 170
Cdd:cd18572 79 LlrQDIAF--FDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRltllaF--ITVPVIALITK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 171 -FGAYVlRQMNslfTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIA 249
Cdd:cd18572 155 vYGRYY-RKLS---KEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQ 230
|
250
....*....|..
gi 492039060 250 YTVIALIVYLIG 261
Cdd:cd18572 231 NGTQVLVLFYGG 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
348-562 |
1.97e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD-------------VTEAalRKTVSFVL 414
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneainhgfalVTEE--RRSTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 415 QRAVLFSGTIaSNLRQGNAQAKLHELQRaanMAQASEFIErynDSFDHEVEERSAN---FSGGQKQRLSIARGLIAKAPI 491
Cdd:PRK10982 340 YLDIGFNSLI-SNIRNYKNKVGLLDNSR---MKSDTQWVI---DSMRVKTPGHRTQigsLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 492 LILDDSTSALDAESEKKVQQ-ALEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLV-----AQGTHEELLKTSLVY 562
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQlIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVAgivdtKTTTQNEILRLASLH 490
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
350-550 |
2.45e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.26 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIA-RLYDPT-KGKVKIGGQNIkdvTEAALRKTvSFVLQRAVLF------- 420
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKP---TKQILKRT-GFVTQDDILYphltvre 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYN----DSFDHEVeersanfSGGQKQRLSIARGLIAKAPILILDD 496
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENtiigNSFIRGI-------SGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 497 STSALDAESEKKVQQALEHelpdtttfiIAEKIVSVINA------------DTILVLDDGKLVAQG 550
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGS---------LAQKGKTIVTSmhqpssrvyqmfDSVLVLSEGRCLFFG 289
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
350-502 |
3.47e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLA-QLIARLYDP-TKGKVKIGGQ-----NIKDVTEAAL------RKTVSFVLQR 416
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKevdvsTVSDAIDAGLayvtedRKGYGLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 417 AVLFSGTIASnlrqgnaqakLHELQRAANMAQASEFI--ERYNDSFD---HEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:NF040905 356 DIKRNITLAN----------LGKVSRRGVIDENEEIKvaEEYRKKMNiktPSVFQKVGNLSGGNQQKVVLSKWLFTDPDV 425
|
170
....*....|.
gi 492039060 492 LILDDSTSALD 502
Cdd:NF040905 426 LILDEPTRGID 436
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
330-504 |
3.51e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 330 SGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikdvTEAALrkt 409
Cdd:PRK11147 315 SGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-----LEVAY--- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 vsFVLQRAVL-FSGTIASNLRQG------NAQAK--LHELQ-------RAANMAQAsefieryndsfdheveersanFSG 473
Cdd:PRK11147 387 --FDQHRAELdPEKTVMDNLAEGkqevmvNGRPRhvLGYLQdflfhpkRAMTPVKA---------------------LSG 443
|
170 180 190
....*....|....*....|....*....|.
gi 492039060 474 GQKQRLSIARGLIAKAPILILDDSTSALDAE 504
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
40-297 |
3.60e-06 |
|
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: 49.20 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 40 ENIQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLI 119
Cdd:cd18558 44 LNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 120 NDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIViipRFWWAPVVMVAL--IFGFGAYVLRQMNSLFT-KFQEMMDRISNQ 196
Cdd:cd18558 124 DDVSKINEGIGDKIGVIFQNIATFGTGFIIGFI---RGWKLTLVILAIspVLGLSAVVWAKILSGFTdKEKKAYAKAGAV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 197 AQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIALIVYLIGKNITAHPSDIAvvsp 276
Cdd:cd18558 201 AEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIG---- 276
|
250 260
....*....|....*....|.
gi 492039060 277 fvnYVLTLLFTIMIAGMTLMQ 297
Cdd:cd18558 277 ---EVLTVFFSVLIGAFSAGQ 294
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
346-563 |
6.40e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQR--AVLFS-- 421
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRnnTDMLSpg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 ----GTIASNLrqgnAQAKLHELQRAANMAQasEFieryndSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDS 497
Cdd:PRK10938 95 eddtGRTTAEI----IQDEVKDPARCEQLAQ--QF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 498 TSALDAESEKKVQQALEHelpdtttfIIAEKI--VSVIN--------ADTILVLDDGKLVAQGTHEELLKTSLVYQ 563
Cdd:PRK10938 163 FDGLDVASRQQLAELLAS--------LHQSGItlVLVLNrfdeipdfVQFAGVLADCTLAETGEREEILQQALVAQ 230
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
333-557 |
6.62e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGddPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVK------IG--GQNI-----K 399
Cdd:PRK15064 320 LEVENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsenanIGyyAQDHaydfeN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 400 DVT--------------EAALRKTvsfvLQRaVLFSGtiasnlrqgnaqaklhelqraanmaqasefieryndsfdHEVE 465
Cdd:PRK15064 398 DLTlfdwmsqwrqegddEQAVRGT----LGR-LLFSQ---------------------------------------DDIK 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 466 ERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEhELPDTTTFIIAEK-IVSVInADTILVLDDG 544
Cdd:PRK15064 434 KSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE-KYEGTLIFVSHDReFVSSL-ATRIIEITPD 511
|
250
....*....|....
gi 492039060 545 KLVA-QGTHEELLK 557
Cdd:PRK15064 512 GVVDfSGTYEEYLR 525
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
21-297 |
7.55e-06 |
|
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: 48.01 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 21 AIIAILVSAFSGLYQPKLLENI-----------QKALMANQKQAVLsdgIWLVVLGIIAIISGIFNVYFAAkIAQGVVSD 89
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVidavtnhsgsgGEEALRALNQAVL---ILLGVVLIGSIATFLRSWLFTL-AGERVVAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 90 LREDTYAKI--QTFSFGNIKKfsAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIF-----------CIVIIPr 156
Cdd:cd18780 77 LRKRLFSAIiaQEIAFFDVTR--TGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFmfttswkltlvMLSVVP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 157 fwwaPVVMVALIFGfgayvlRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFdqTSDQLNDYNIVIGY 236
Cdd:cd18780 154 ----PLSIGAVIYG------KYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRY--SEKINESYLLGKKL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 237 -----WFSAIMPAFQMIAytvIALIVYLIGKNITAHPSDIAVVSPFVNYVLTLLFTI-MIAGM--TLMQ 297
Cdd:cd18780 222 arasgGFNGFMGAAAQLA---IVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFaFLSSLygDFMQ 287
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
365-514 |
1.75e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.77 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 365 IVGATGAGKSTLAQLIAR-LYDPTKGKVKIGGQNIKDVTEAAlrkTVSFVLQ------RAVLFSGTIASNLRQ------- 430
Cdd:COG0419 28 IVGPNGAGKSTILEAIRYaLYGKARSRSKLRSDLINVGSEEA---SVELEFEhggkryRIERRQGEFAEFLEAkpserke 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 431 -----------GNAQAKLHELQRAAN--MAQASEFIERYNDSFDHEVEERSAN-FSGGQKQRLSIARGLiakapILILDd 496
Cdd:COG0419 105 alkrllgleiyEELKERLKELEEALEsaLEELAELQKLKQEILAQLSGLDPIEtLSGGERLRLALADLL-----SLILD- 178
|
170
....*....|....*...
gi 492039060 497 sTSALDAESEKKVQQALE 514
Cdd:COG0419 179 -FGSLDEERLERLLDALE 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
345-514 |
2.82e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIA-----------RLYdptkGKVKIGGQNIKDVteaalRKTVSFV 413
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndlTLF----GRRRGSGETIWDI-----KKHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQ------------RAVLFSGTIAS-NLRQG--NAQAKLhelqraanmaqASEFIERYNdsfdheVEERSAN-----FSG 473
Cdd:PRK10938 342 SSslhldyrvstsvRNVILSGFFDSiGIYQAvsDRQQKL-----------AQQWLDILG------IDKRTADapfhsLSW 404
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492039060 474 GQkQRLS-IARGLIAKAPILILDDSTSALDAESEKKVQQALE 514
Cdd:PRK10938 405 GQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVD 445
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
350-539 |
3.86e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.54 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI-----KDVTEAAlrktVSFVLQRAVLFSG-T 423
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpKSSQEAG----IGIIHQELNLIPQlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 424 IASNLRQGNA-QAKLHELQRAANMAQASEFIERYNDSfdHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSAL- 501
Cdd:PRK10762 96 IAENIFLGREfVNRFGRIDWKKMYAEADKLLARLNLR--FSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALt 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 502 DAESEK--KVQQALE----------HELP-------DTTTF----IIAEKIVSVINADTIL 539
Cdd:PRK10762 174 DTETESlfRVIRELKsqgrgivyisHRLKeifeicdDVTVFrdgqFIAEREVADLTEDSLI 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
346-561 |
5.00e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLyDPTK-GKVKIGGQNIKDVTE-AALRKTVSFVLQ--RAVLFS 421
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-DKRAgGEIRLNGKDISPRSPlDAVKKGMAYITEsrRDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 G--TIASNL---------RQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEErsanFSGGQKQRLSIARGLIAKAP 490
Cdd:PRK09700 354 PnfSIAQNMaisrslkdgGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 491 ILILDDSTSALDAESEKKVQQaLEHELPDTTTFIIA-----EKIVSVinADTILVLDDGKLVA------QGTHEELLKTS 559
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYK-VMRQLADDGKVILMvsselPEIITV--CDRIAVFCEGRLTQiltnrdDMSEEEIMAWA 506
|
..
gi 492039060 560 LV 561
Cdd:PRK09700 507 LP 508
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
350-577 |
8.71e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVlqRAVLFsgtiaSNLR 429
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGI--ENIEF-----KMLC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 430 QGNAQAKLHELqraanMAQASEFIEryndsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAE-SEKK 508
Cdd:PRK13546 113 MGFKRKEIKAM-----TPKIIEFSE-----LGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTfAQKC 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 509 VQQALEHELPDTTTFIIAEKIVSVINADT-ILVLDDGKLVAQGTHEELLKTslvYQEIFKTQKGKKGGNE 577
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGQVRQFCTkIAWIEGGKLKDYGELDDVLPK---YEAFLNDFKKKSKAEQ 249
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
141-310 |
1.92e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 43.65 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 141 ILIVGSFIFCIVIIPRFWWA-PVVMVALIFGFGAYV-----LRQMNS-----LFTKFqemmdrisnqaQETLQGVRVVKS 209
Cdd:cd18580 125 FSVLGSLIVIAIVSPYFLIVlPPLLVVYYLLQRYYLrtsrqLRRLESesrspLYSHF-----------SETLSGLSTIRA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 210 FNQGpqeiKKFDQTSDQLNDYNIVIGYWFSAIMPAFQM--------IAYTVIALIVYLIGkniTAHPSDIAVVspfVNYV 281
Cdd:cd18580 194 FGWQ----ERFIEENLRLLDASQRAFYLLLAVQRWLGLrldllgalLALVVALLAVLLRS---SISAGLVGLA---LTYA 263
|
170 180 190
....*....|....*....|....*....|..
gi 492039060 282 LTLLFTIMiagMTLMQFSRANISLG---RIRE 310
Cdd:cd18580 264 LSLTGSLQ---WLVRQWTELETSMVsveRILE 292
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
472-555 |
3.82e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 472 SGGQKQRLSIARGLIAKA---PILILDDSTSALDAESEKKVQQALeHELPDT-TTFIIAEKIVSVI-NADTILVL----- 541
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVL-QRLVDKgNTVVVIEHNLDVIkTADYIIDLgpegg 909
|
90
....*....|....*
gi 492039060 542 -DDGKLVAQGTHEEL 555
Cdd:TIGR00630 910 dGGGTVVASGTPEEV 924
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
147-263 |
5.33e-03 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 38.96 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 147 FIFCIVIiprFW------WAPVVMVALIFGFGAYVLRQMNSLFtkfQEMMdRISNQAQ----ETLQGVRVVKSFNQGPQE 216
Cdd:cd18587 129 LLFLAVI---ALiggplaLVPLVAIPLVLLYGLLLQKPLRRLV---EESM-RESAQKNallvESLSGLETIKALGAEGRM 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 492039060 217 IKKFDQTSDQLNDYNIVIGYWFSAIM---PAFQMIAYTVIALI-VYLIGKN 263
Cdd:cd18587 202 QRRWEEAVAALARSSLKSRLLSSSATnfaQFVQQLVTVAIVIVgVYLISDG 252
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
42-227 |
6.52e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 38.80 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 42 IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNV---------YFAAKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAG 112
Cdd:cd18561 14 AQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLraallwlreRVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 113 SLTTRLINDMNQVMNMMMQLfmqmlrLP---ILIVGSFIFCIVIIPRFWWAPV---VMVALIFGFGAYVLRQMNSLFTKF 186
Cdd:cd18561 94 ELQTTVVDGVEALEAYYGRY------LPqllVALLGPLLILIYLFFLDPLVALillVFALLIPLSPALWDRLAKDTGRRH 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492039060 187 QEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQL 227
Cdd:cd18561 168 WAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDL 208
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
336-383 |
7.10e-03 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 38.38 E-value: 7.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 336 DHVSFTYPDGD-----DPTLKDISFKIKPGQ---MVGIVGATGAGKSTLAQLIARL 383
Cdd:PRK09270 1 LKVQAQYRDEEieavhKPLLRRLAALQAEPQrrtIVGIAGPPGAGKSTLAEFLEAL 56
|
|
|