|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-563 |
0e+00 |
|
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: 639.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 2 IDKRVFKF-PGVKPAAAIMAVLTFVQAFMIIFQAKYLSVAIVNLWQLK-SVRTIVLPLLLFAGAFLARHLLTLSNNWLLY 79
Cdd:COG4988 4 LDKRLKRLaRGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGaPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 80 PFVEKTTKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLTPWIVLIYIAFIQWKEALF 159
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 160 LLAIYPLIIFFMIILGLAAQAKADRQYAGYQRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMSTLTIAMT 239
Cdd:COG4988 164 LLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 240 STFALDFFTTLSIAIIAVFLGFGLMNNTIQLLPALIILTLAPDYFAPIRNFANDYHATLNGKNTLTAVLDILQRPTPTDR 319
Cdd:COG4988 244 SSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 320 DllPVRQPTWQADDTLALNKVNVSYGESQtPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTA 399
Cdd:COG4988 324 A--GTAPLPAAGPPSIELEDVSFSYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 400 VPHLDKQAWQRSFVYIPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQ 479
Cdd:COG4988 401 LSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 480 RIALARAFLDDsRRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELE 559
Cdd:COG4988 481 RLALARALLRD-APLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
....
gi 1834933330 560 QQGG 563
Cdd:COG4988 560 AKNG 563
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-544 |
1.17e-165 |
|
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: 481.79 E-value: 1.17e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 12 VKPAAAIMAVLTFVQAFMIIFQAKYLSVAIVNLWQLKSVRTIVLP-LLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLR 90
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPaLGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 91 KQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLTPWIVLIYIAFIQWKEALFLLAIYPLIIFF 170
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 171 MIILGLAAQAKADRQYAGYQRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTL 250
Cdd:TIGR02857 161 MILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 251 SIAIIAVFLGFGLMNNTIQLLPALIILTLAPDYFAPIRNFANDYHATLNGK---NTLTAVLDILQRPTPTDRDLlpvrqp 327
Cdd:TIGR02857 241 SVALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVaaaEALFAVLDAAPRPLAGKAPV------ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 328 TWQADDTLALNKVNVSYgESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQA 407
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 408 WQRSFVYIPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAF 487
Cdd:TIGR02857 394 WRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAF 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1834933330 488 LDDsRRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVM 544
Cdd:TIGR02857 474 LRD-APLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-568 |
2.60e-118 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 362.17 E-value: 2.60e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 4 KRVFKF-PGVKPAAAIMAVLTFVQAFMIIFQAKYLSVAIVNLWQLKSVRTIVLPLLLFAGAFLARHLLTLSNNWLLYPFV 82
Cdd:COG1132 10 RRLLRYlRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 83 EKTTKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLTPWIVLIYIAFIQWKEALFLLA 162
Cdd:COG1132 90 QRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 163 IYPLIIFFMIILGLAAQAKADRQYAGYQRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMSTLTIAMTSTF 242
Cdd:COG1132 170 VLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 243 ALDFFTTLSIAIIAVFLGFGLMNNTIQL--LPALIILTLApdYFAPIRNFANDYHATLNGKNTLTAVLDILQRPTPTDRD 320
Cdd:COG1132 250 LMELLGNLGLALVLLVGGLLVLSGSLTVgdLVAFILYLLR--LFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 321 LLPVRQPtwQADDTLALNKVNVSYGESQtPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAV 400
Cdd:COG1132 328 PGAVPLP--PVRGEIEFENVSFSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 401 PHLDKQAWQRSFVYIPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQR 480
Cdd:COG1132 405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 481 IALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQ 560
Cdd:COG1132 485 IAIARALLKDP-PILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA 563
|
....*...
gi 1834933330 561 QGGTYVRL 568
Cdd:COG1132 564 RGGLYARL 571
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
89-571 |
2.82e-108 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 336.43 E-value: 2.82e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 89 LRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYL------MLIIGkvldlsLTPWIVLIYIAFIQWKEALFLLA 162
Cdd:PRK11174 98 IRQQVLDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDFYarylpqMALAV------LVPLLILIAVFPINWAAGLILLG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 163 IYPLIIFFMIILGLAAqAKADRQ-YAGYQRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMSTLTIAMTST 241
Cdd:PRK11174 172 TAPLIPLFMALVGMGA-ADANRRnFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLSS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 242 FALDFFTTLSIAIIAVFLGF--------GLMNNTIQLLPALIILTLAPDYFAPIRNFANDYHATLNGKNTLTAVLDILQR 313
Cdd:PRK11174 251 AVLEFFASISIALVAVYFGFsylgelnfGHYGTGVTLFAGFFVLILAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFLET 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 314 PTPTDRDllpvRQPTWQADDTLALNKVNVS-YGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLsPQDGQ 392
Cdd:PRK11174 331 PLAHPQQ----GEKELASNDPVTIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGS 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 393 INVRDTAVPHLDKQAWQRSFVYIPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARG 472
Cdd:PRK11174 406 LKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAG 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 473 VSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQ 552
Cdd:PRK11174 486 LSVGQAQRLALARALLQPC-QLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQ 564
|
490
....*....|....*....
gi 1834933330 553 GTPAELEQQGGTYVRLRSE 571
Cdd:PRK11174 565 GDYAELSQAGGLFATLLAH 583
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
89-568 |
1.86e-95 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 302.84 E-value: 1.86e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 89 LRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLTPWIVLIYIAFIQWKEALFLLAIYPLII 168
Cdd:COG4987 90 LRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 169 FFMIILGLAAQAKADRQYA-GYQRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRK--KTMSTLTIAmtSTFALD 245
Cdd:COG4987 170 LLLPLLAARLGRRAGRRLAaARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAaqRRLARLSAL--AQALLQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 246 FFTTLSIAIIAVFLGFGLMNNTIQ--LLPALIILTLA-PDYFAPIRNFANDYHATLNGKNTLTAVLDilQRPTPTDrdll 322
Cdd:COG4987 248 LAAGLAVVAVLWLAAPLVAAGALSgpLLALLVLAALAlFEALAPLPAAAQHLGRVRAAARRLNELLD--APPAVTE---- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 323 PVRQPTWQADDTLALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPH 402
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 403 LDKQAWQRSFVYIPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIA 482
Cdd:COG4987 402 LDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLA 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 483 LARAFLDDsRRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQG 562
Cdd:COG4987 482 LARALLRD-APILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
....*.
gi 1834933330 563 GTYVRL 568
Cdd:COG4987 561 GRYRQL 566
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
20-307 |
2.35e-95 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 292.78 E-value: 2.35e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 20 AVLTFVQAFMIIFQAKYLSVAIVNLW-QLKSVRTIVLPLLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMAKLF 98
Cdd:cd18584 2 VLLGLLAALLIIAQAWLLARIIAGVFlEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 99 DLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLTPWIVLIYIAFIQWKEALFLLAIYPLIIFFMIILGLAA 178
Cdd:cd18584 82 ALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 179 QAKADRQYAGYQRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTLSIAIIAVF 258
Cdd:cd18584 162 QAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAVY 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1834933330 259 LGFGLMNNTIQLLPALIILTLAPDYFAPIRNFANDYHATLNGKNTLTAV 307
Cdd:cd18584 242 IGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
48-571 |
5.30e-94 |
|
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: 302.91 E-value: 5.30e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 48 KSVRTIVLPLLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMgLEGIDKIQTY 127
Cdd:COG2274 190 QDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASR-FRDVESIREF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 128 LM-LIIGKVLDLsLTPWIVLIYIAFIQWKEALFLLAIYPLIIFFMIILGLAAQAKADRQYAGYQRLSNHFVDTLRGLPTL 206
Cdd:COG2274 269 LTgSLLTALLDL-LFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 207 KQLGLNKTYADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTLSIAIIAVFLGFGLMNNTI---QLLPALIILTLApdy 283
Cdd:COG2274 348 KALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLtlgQLIAFNILSGRF--- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 284 FAPIRNFAN---DYHATlngKNTLTAVLDILQRPTPTDRDLLPVRQPTWQADdtLALNKVNVSYGESQTPTLKDITFSVH 360
Cdd:COG2274 425 LAPVAQLIGllqRFQDA---KIALERLDDILDLPPEREEGRSKLSLPRLKGD--IELENVSFRYPGDSPPVLDNISLTIK 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 361 GFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPYLFHASLRDNLAFYAPGASEE 440
Cdd:COG2274 500 PGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDE 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 441 AVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVF 520
Cdd:COG2274 580 EIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNP-RILILDEATSALDAETEAIILENLRRLL 658
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 521 DHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTYVRLRSE 571
Cdd:COG2274 659 KGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
335-553 |
1.92e-63 |
|
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: 207.44 E-value: 1.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVY 414
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDsRRV 494
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND-PPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 495 LLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQG 553
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
89-532 |
2.59e-62 |
|
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: 214.15 E-value: 2.59e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 89 LRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLTPWIVLIYIAFIQWKEALFLLAIYPLII 168
Cdd:TIGR02868 88 LRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 169 FFM-IILGLAAQAKADRQYAGYQRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDY-----RKKTMSTLTIAMTSTF 242
Cdd:TIGR02868 168 FVApLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELtraerRAAAATALGAALTLLA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 243 AldfftTLSIAIIAVFLGFGLMNNTI--QLLPALIILTLAP-DYFAPIRNFANdyhatlngknTLTAVLDILQRPTPTDR 319
Cdd:TIGR02868 248 A-----GLAVLGALWAGGPAVADGRLapVTLAVLVLLPLAAfEAFAALPAAAQ----------QLTRVRAAAERIVEVLD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 320 DLLPVRQPTWQADDTLALNKV-----NVSYG-ESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQI 393
Cdd:TIGR02868 313 AAGPVAEGSAPAAGAVGLGKPtlelrDLSAGyPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 394 NVRDTAVPHLDKQAWQRSFVYIPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGV 473
Cdd:TIGR02868 393 TLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARL 472
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 474 SGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRL 532
Cdd:TIGR02868 473 SGGERQRLALARALLADA-PILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
340-563 |
3.46e-61 |
|
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: 202.07 E-value: 3.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 340 VNVSYGEsQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAP 419
Cdd:cd03254 8 VNFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 420 YLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDE 499
Cdd:cd03254 87 FLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP-KILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 500 PTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGG 563
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
335-548 |
3.51e-59 |
|
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: 194.52 E-value: 3.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVY 414
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLFHASLRDNLafyapgaseeavmqaaakagltdwiatlpdglatqigegargVSGGQAQRIALARAFLDDSrRV 494
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDP-PI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 495 LLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGK 548
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
335-569 |
1.15e-58 |
|
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: 195.53 E-value: 1.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVY 414
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEgaRGV--SGGQAQRIALARAFLDDSr 492
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGE--RGVklSGGQRQRIAIARALLKDP- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834933330 493 RVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTYVRLR 569
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
341-568 |
5.86e-57 |
|
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: 190.90 E-value: 5.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQT-PTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAP 419
Cdd:cd03253 5 NVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 420 YLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEgaRGV--SGGQAQRIALARAFLDDSrRVLLF 497
Cdd:cd03253 85 VLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGE--RGLklSGGEKQRVAIARAILKNP-PILLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 498 DEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTYVRL 568
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
338-555 |
1.26e-54 |
|
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: 184.23 E-value: 1.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 338 NKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQ 417
Cdd:cd03244 6 KNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 418 APYLFHASLRDNLAFYApGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLF 497
Cdd:cd03244 86 DPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS-KILVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 498 DEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTP 555
Cdd:cd03244 164 DEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
335-568 |
2.75e-50 |
|
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: 173.44 E-value: 2.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVY 414
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRV 494
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP-RI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 495 LLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTYVRL 568
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
350-568 |
6.19e-50 |
|
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: 172.34 E-value: 6.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 350 PTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPYLFHASLRDN 429
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 430 LAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETE 509
Cdd:cd03249 97 IRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP-KILLLDEATSALDAESE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 510 VELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTYVRL 568
Cdd:cd03249 176 KLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
57-568 |
4.41e-49 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 181.09 E-value: 4.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 57 LLLFAGAFLARHL----LTLSNNWLLYPFVEKTTKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEgIDKIQTYLMlii 132
Cdd:TIGR01846 178 LSVLALAMLAVAIfepaLGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLT--- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 133 GKVLDLSLTPWIVLIYIAFIQW-KEALFLLAIYPLIIFFMIILGLAA--QAKADRQYAGYQRLSNHFVDTLRGLPTLKQL 209
Cdd:TIGR01846 254 GSALTVVLDLLFVVVFLAVMFFySPTLTGVVIGSLVCYALLSVFVGPilRKRVEDKFERSAAATSFLVESVTGIETIKAT 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 210 GLNKTYADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTLSIAIIAVFLGFGLMNNTIQLLPALIILTLAPDYFAPIRN 289
Cdd:TIGR01846 334 ATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 290 FAN---DYHATLNGKNTLTAVLDILQRPTPTDRDLLPVRqptwqaDDTLALNKVNVSYGESQTPTLKDITFSVHGFQKVG 366
Cdd:TIGR01846 414 LAQlwqDFQQTGIALERLGDILNSPTEPRSAGLAALPEL------RGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIG 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 367 IIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPYLFHASLRDNLAFYAPGASEEAVMQAA 446
Cdd:TIGR01846 488 IVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 447 AKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVF 526
Cdd:TIGR01846 568 KLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNP-RILIFDEATSALDYESEALIMRNMREICRGRTVI 646
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1834933330 527 FATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTYVRL 568
Cdd:TIGR01846 647 IIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
326-569 |
6.20e-49 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 178.87 E-value: 6.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 326 QPTWQAD-DTLALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLD 404
Cdd:PRK11160 329 TSTAAADqVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 405 KQAWQRSFVYIPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDwIATLPDGLATQIGEGARGVSGGQAQRIALA 484
Cdd:PRK11160 409 EAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEK-LLEDDKGLNAWLGEGGRQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 485 RAFLDDSRRVLLfDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGT 564
Cdd:PRK11160 488 RALLHDAPLLLL-DEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGR 566
|
....*
gi 1834933330 565 YVRLR 569
Cdd:PRK11160 567 YYQLK 571
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
55-570 |
1.75e-48 |
|
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: 177.60 E-value: 1.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 55 LPLLLFaGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGK 134
Cdd:TIGR02203 56 VPLVVI-GLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 135 VLDLSLTPWIVLIYIAFIQWKEALFLLAIYPLIiffmiilGLAAQAKADRqyagYQRLSNHFVDTLRGLPTLKQLGLN-- 212
Cdd:TIGR02203 135 LVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVL-------SILMRRVSKR----LRRISKEIQNSMGQVTTVAEETLQgy 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 213 ---KTYADNVYQvSEDYRKKTMSTLTIAMTSTFALDFFTTLSIAIIAVFLGFGLMnntIQLLPALIILTLAPDY------ 283
Cdd:TIGR02203 204 rvvKLFGGQAYE-TRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLF---IALFQAQAGSLTAGDFtafita 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 284 ----FAPIR---NFANDYHATLNGKNTLTAVLDilqrpTPTDRDllPVRQPTWQADDTLALNKVNVSYGESQTPTLKDIT 356
Cdd:TIGR02203 280 mialIRPLKsltNVNAPMQRGLAAAESLFTLLD-----SPPEKD--TGTRAIERARGDVEFRNVTFRYPGRDRPALDSIS 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 357 FSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPYLFHASLRDNLAFYAPG 436
Cdd:TIGR02203 353 LVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 437 -ASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSRrVLLFDEPTAHLDIETEVELKRA 515
Cdd:TIGR02203 433 qADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAP-ILILDEATSALDNESERLVQAA 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1834933330 516 MLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTYVRLRS 570
Cdd:TIGR02203 512 LERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHN 566
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
304-568 |
3.52e-48 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 176.81 E-value: 3.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 304 LTAVLDILQRPTPTDrdlLPVRqptwqADDTLALNKVNVSY-GESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTL 382
Cdd:TIGR02204 315 LQAEPDIKAPAHPKT---LPVP-----LRGEIEFEQVNFAYpARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 383 GGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGL 462
Cdd:TIGR02204 387 LRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGY 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 463 ATQIGEGARGVSGGQAQRIALARAFLDDsRRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYIL 542
Cdd:TIGR02204 467 DTYLGERGVTLSGGQRQRIAIARAILKD-APILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIV 545
|
250 260
....*....|....*....|....*.
gi 1834933330 543 VMDHGKIVQQGTPAELEQQGGTYVRL 568
Cdd:TIGR02204 546 VMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
62-568 |
1.30e-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: 177.24 E-value: 1.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 62 GAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLt 141
Cdd:TIGR01193 204 IAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWI- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 142 pwIVLIYIAFIQWKEALFLLA-----IYPLII--FFMIILGL---AAQAKAdrqyagyqRLSNHFVDTLRGLPTLKQLGL 211
Cdd:TIGR01193 283 --LVIVGLFLVRQNMLLFLLSllsipVYAVIIilFKRTFNKLnhdAMQANA--------VLNSSIIEDLNGIETIKSLTS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 212 NKTYADNVYQVSEDYRKKTMsTLTIAMTSTFALDFFTTLSIAIIAVFLG-FGLMNNTIQLlPALIILTLAPDYFA-PIRN 289
Cdd:TIGR01193 353 EAERYSKIDSEFGDYLNKSF-KYQKADQGQQAIKAVTKLILNVVILWTGaYLVMRGKLTL-GQLITFNALLSYFLtPLEN 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 290 FAN---DYHATLNGKNTLTAVLDIlqrptptDRDLLPVRQPTW--QADDTLALNKVNVSYGESqTPTLKDITFSVHGFQK 364
Cdd:TIGR01193 431 IINlqpKLQAARVANNRLNEVYLV-------DSEFINKKKRTElnNLNGDIVINDVSYSYGYG-SNILSDISLTIKMNSK 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 365 VGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPYLFHASLRDNLAFYA-PGASEEAVM 443
Cdd:TIGR01193 503 TTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIW 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 444 QAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDHH 523
Cdd:TIGR01193 583 AACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDS-KVLILDESTSNLDTITEKKIVNNLLNLQDKT 661
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1834933330 524 LVFFAtHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTYVRL 568
Cdd:TIGR01193 662 IIFVA-HRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
335-557 |
3.66e-46 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 170.70 E-value: 3.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVY 414
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLFHASLRDNLA-FyaPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSRR 493
Cdd:COG4618 411 LPQDVELFDGTIAENIArF--GDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 494 VLLfDEPTAHLDIETEVELKRAMLpvfdhHL------VFFATHRLHWMNEMDYILVMDHGKIVQQGTPAE 557
Cdd:COG4618 489 VVL-DEPNSNLDDEGEAALAAAIR-----ALkargatVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
341-568 |
8.59e-45 |
|
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: 167.69 E-value: 8.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYG-ESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAP 419
Cdd:COG5265 362 NVSFGyDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 420 YLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEgaRGV--SGGQAQRIALARAFLDDSrRVLLF 497
Cdd:COG5265 442 VLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGE--RGLklSGGEKQRVAIARTLLKNP-PILIF 518
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 498 DEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTYVRL 568
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
340-568 |
1.16e-44 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 167.06 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 340 VNVSYGESqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAP 419
Cdd:PRK13657 340 VSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 420 YLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDE 499
Cdd:PRK13657 419 GLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP-PILILDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 500 PTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTYVRL 568
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
339-549 |
2.69e-40 |
|
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: 146.08 E-value: 2.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 339 KVNVSY-GESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQ 417
Cdd:cd03248 16 NVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 418 APYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLF 497
Cdd:cd03248 96 EPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP-QVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1834933330 498 DEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKI 549
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
20-300 |
7.99e-40 |
|
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: 146.66 E-value: 7.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 20 AVLTFVQAFMIIFQAKYLSVAIVNLWQLKSVRTIVLPLLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMAKLFD 99
Cdd:cd18561 2 VLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 100 LGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLTPWIVLIYIAFIQWKEALFLLAIYPLIIFFMIILGLAAQ 179
Cdd:cd18561 82 LGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 180 AKADRQYAGYQRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTLSIAIIAVFL 259
Cdd:cd18561 162 DTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1834933330 260 GFGLMNNTIQLLPALIILTLAPDYFAPIRNFANDYHATLNG 300
Cdd:cd18561 242 ALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQG 282
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
334-561 |
3.36e-39 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 150.96 E-value: 3.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFV 413
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YIPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSRR 493
Cdd:TIGR01842 396 YLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKL 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 494 VLLfDEPTAHLDIETEVELKRAMLpvfdhHL------VFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQ 561
Cdd:TIGR01842 476 VVL-DEPNSNLDEEGEQALANAIK-----ALkargitVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
340-568 |
1.27e-38 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 149.78 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 340 VNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQI-----NVRDTAVPHLDKQawqrsFVY 414
Cdd:PRK11176 347 VTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIlldghDLRDYTLASLRNQ-----VAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLFHASLRDNLAfYAPGA--SEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSr 492
Cdd:PRK11176 422 VSQNVHLFNDTIANNIA-YARTEqySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS- 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834933330 493 RVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTYVRL 568
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
329-555 |
7.33e-38 |
|
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: 138.70 E-value: 7.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 329 WQADDTLALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAW 408
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 409 QRSFVYIPQAPYLFHASLRDNLAFYAPgASEEAVMQaaakagltdwiatlpdglATQIGEGARGVSGGQAQRIALARAFL 488
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDE-YSDEEIYG------------------ALRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834933330 489 dDSRRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTP 555
Cdd:cd03369 142 -KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
334-565 |
1.26e-37 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 146.78 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFV 413
Cdd:PRK10789 313 ELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YIPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEgaRGV--SGGQAQRIALARAFLDDS 491
Cdd:PRK10789 393 VVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGE--RGVmlSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 492 rRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTY 565
Cdd:PRK10789 471 -EILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
335-561 |
1.64e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 138.66 E-value: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHlDKQAWQRSFVY 414
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLF-HASLRDNLAFYA------PGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAF 487
Cdd:COG1131 78 VPQEPALYpDLTVRENLRFFArlyglpRKEARERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 488 LDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDH-HLVFFATHRlhwMNEM----DYILVMDHGKIVQQGTPAELEQQ 561
Cdd:COG1131 147 LHDP-ELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHY---LEEAerlcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
335-548 |
3.55e-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: 136.83 E-value: 3.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQT---PTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVrdtavphldkqawQRS 411
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAPYLFHASLRDNLAFYAPGASE--EAVMQAAAkagLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLD 489
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEEryEKVIKACA---LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 490 DSrRVLLFDEPTAHLDIETEVELkramlpvFDH----HL-----VFFATHRLHWMNEMDYILVMDHGK 548
Cdd:cd03250 145 DA-DIYLLDDPLSAVDAHVGRHI-------FENcilgLLlnnktRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
335-553 |
8.15e-37 |
|
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: 135.13 E-value: 8.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAwQRSFVY 414
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL-SSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLFHASLRDNLafyapgaseeavmqaaakagltdwiatlpdglatqigeGARgVSGGQAQRIALARAFLDDSRRV 494
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRR-FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 495 LLfDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQG 553
Cdd:cd03247 121 LL-DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
352-502 |
8.95e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 131.23 E-value: 8.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPYLF-HASLRDNL 430
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 431 AFyapGASEEAVMQAAAKAGLTDWIATL--PDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEPTA 502
Cdd:pfam00005 81 RL---GLLLKGLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKP-KLLLLDEPTA 150
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
334-565 |
1.48e-35 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 141.01 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYGESQtPTLKDITFSV--HGFqkVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRS 411
Cdd:PRK10790 340 RIDIDNVSFAYRDDN-LVLQNINLSVpsRGF--VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAPYLFHASLRDNLAFyAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAfLDDS 491
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTL-GRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARV-LVQT 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 492 RRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTY 565
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
335-558 |
1.86e-35 |
|
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: 132.84 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGEsQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVY 414
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAP--YLFHASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARA 486
Cdd:COG1122 80 VFQNPddQLFAPTVEEDVAFgpenlgLPREEIRERVEEALELVGLEHLADRPPHEL-----------SGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834933330 487 FLDDSrRVLLFDEPTAHLDIETEVELKRAM--LPVFDHHLVfFATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:COG1122 149 LAMEP-EVLVLDEPTAGLDPRGRRELLELLkrLNKEGKTVI-IVTHDLDLVAELaDRVIVLDDGRIVADGTPREV 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
337-548 |
5.92e-35 |
|
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: 131.05 E-value: 5.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIP 416
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QAP--YLFHASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAFL 488
Cdd:cd03225 82 QNPddQFFGPTVEEEVAFglenlgLPEEEIEERVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834933330 489 DDSrRVLLFDEPTAHLDIETEVELKRAMlpvfdHHL------VFFATHRLHWMNE-MDYILVMDHGK 548
Cdd:cd03225 151 MDP-DILLLDEPTAGLDPAGRRELLELL-----KKLkaegktIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
350-568 |
6.03e-35 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 140.24 E-value: 6.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 350 PTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPYLFHASLRDN 429
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 430 LAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETE 509
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKP-RVLILDEATSALDAECE 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 510 VELKRamLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTYVRL 568
Cdd:TIGR00958 654 QLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
341-549 |
2.17e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.17 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPY 420
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 421 LFHASLRDNLAFYA----PGASEEAVMQAAAKAGLTdwiatlPDGLATQIGEgargVSGGQAQRIALARAFLDDsRRVLL 496
Cdd:COG4619 85 LWGGTVRDNLPFPFqlreRKFDRERALELLERLGLP------PDILDKPVER----LSGGERQRLALIRALLLQ-PDVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 497 FDEPTAHLDIETevelKRAMLPVFDHHL------VFFATHRLHWMNEM-DYILVMDHGKI 549
Cdd:COG4619 154 LDEPTSALDPEN----TRRVEELLREYLaeegraVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
335-558 |
1.77e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 127.80 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVpHLDKQAWQR---- 410
Cdd:COG1126 2 IEIENLHKSFGD--LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKlrrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 411 -SFVYipQAPYLF-HASLRDNLAfYAP----GAS-EEAVMQAAA---KAGLTDWIATLPDGLatqigegargvSGGQAQR 480
Cdd:COG1126 79 vGMVF--QQFNLFpHLTVLENVT-LAPikvkKMSkAEAEERAMElleRVGLADKADAYPAQL-----------SGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 481 IALARAfLDDSRRVLLFDEPTAHLDIET--EV-----ELKRA---MLPVfdhhlvffaTHrlhwmnEM-------DYILV 543
Cdd:COG1126 145 VAIARA-LAMEPKVMLFDEPTSALDPELvgEVldvmrDLAKEgmtMVVV---------TH------EMgfarevaDRVVF 208
|
250
....*....|....*
gi 1834933330 544 MDHGKIVQQGTPAEL 558
Cdd:COG1126 209 MDGGRIVEEGPPEEF 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
337-578 |
2.22e-33 |
|
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: 127.67 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGESqtPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAwQRSFVYIP 416
Cdd:COG4555 4 VENLSKKYGKV--PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-RRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QAPYLF-HASLRDNLAFYAP------GASEEAVMQAAAKAGLTDWIATLpdglatqigegARGVSGGQAQRIALARAFLD 489
Cdd:COG4555 81 DERGLYdRLTVRENIRYFAElyglfdEELKKRIEELIELLGLEEFLDRR-----------VGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 490 DSRrVLLFDEPTAHLDIETEVELKRAMLPVFDH-HLVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAELEQQGGtyvr 567
Cdd:COG4555 150 DPK-VLLLDEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG---- 224
|
250
....*....|.
gi 1834933330 568 lRSEMEGATVK 578
Cdd:COG4555 225 -EENLEDAFVA 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
335-558 |
4.82e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.45 E-value: 4.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLdkQAWQRSFVY 414
Cdd:COG3842 6 LELENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL--PPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLF-HASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAf 487
Cdd:COG3842 82 VFQDYALFpHLTVAENVAFglrmrgVPKAEIRARVAELLELVGLEGLADRYPHQL-----------SGGQQQRVALARA- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 488 LDDSRRVLLFDEPTAHLD----IETEVELKR-------AMLpvfdhhlvfFATHRLH---WMneMDYILVMDHGKIVQQG 553
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDaklrEEMREELRRlqrelgiTFI---------YVTHDQEealAL--ADRIAVMNDGRIEQVG 218
|
....*
gi 1834933330 554 TPAEL 558
Cdd:COG3842 219 TPEEI 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
335-558 |
6.29e-33 |
|
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: 126.70 E-value: 6.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGesQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVY 414
Cdd:COG1120 2 LEAENLSVGYG--GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYL-FHASLRDNLA---------FYAPGAS-EEAVMQAAAKAGLTDW----IATLpdglatqigegargvSGGQAQ 479
Cdd:COG1120 80 VPQEPPApFGLTVRELVAlgryphlglFGRPSAEdREAVEEALERTGLEHLadrpVDEL---------------SGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 480 RIALARAFLDDSrRVLLFDEPTAHLDIETEVE----LKRamLPVFDHHLVFFATHRL-HWMNEMDYILVMDHGKIVQQGT 554
Cdd:COG1120 145 RVLIARALAQEP-PLLLLDEPTSHLDLAHQLEvlelLRR--LARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGP 221
|
....
gi 1834933330 555 PAEL 558
Cdd:COG1120 222 PEEV 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
335-552 |
7.15e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.54 E-value: 7.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSY--GESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAW---- 408
Cdd:COG1136 5 LELRNLTKSYgtGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 409 QRSFVYIPQAPYLF-HASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRI 481
Cdd:COG1136 85 RRHIGFVFQFFNLLpELTALENVALplllagVSRKERRERARELLERVGLGDRLDHRPSQL-----------SGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 482 ALARAFLDDSrRVLLFDEPTAHLDIET--EV-----ELKRAMlpvfdHHLVFFATHRLHWMNEMDYILVMDHGKIVQQ 552
Cdd:COG1136 154 AIARALVNRP-KLILADEPTGNLDSKTgeEVlellrELNREL-----GTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
328-565 |
8.12e-33 |
|
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: 134.69 E-value: 8.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 328 TWQADDTLALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLinTLGGF--LSPQDGQINVRDTAVPHLDK 405
Cdd:TIGR00957 1278 GWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSL--TLGLFriNESAEGEIIIDGLNIAKIGL 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 406 QAWQRSFVYIPQAPYLFHASLRDNLAFYAPgASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALAR 485
Cdd:TIGR00957 1356 HDLRFKITIIPQDPVLFSGSLRMNLDPFSQ-YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 486 AFLDDSRrVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMneMDY--ILVMDHGKIVQQGTPAELEQQGG 563
Cdd:TIGR00957 1435 ALLRKTK-ILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTI--MDYtrVIVLDKGEVAEFGAPSNLLQQRG 1511
|
..
gi 1834933330 564 TY 565
Cdd:TIGR00957 1512 IF 1513
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
54-551 |
8.33e-33 |
|
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: 134.65 E-value: 8.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 54 VLPLLLFAGAFLARHLLTLSnnwllypfvekttKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIG 133
Cdd:TIGR01271 938 VLALGFFRGLPLVHTLLTVS-------------KRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLF 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 134 KVLDLSLtpwIVLIYIAFIQWKEALFLLAIYPLIIFFMII----LGLAAQAKaDRQYAGYQRLSNHFVDTLRGLPTLKQL 209
Cdd:TIGR01271 1005 DFIQLTL---IVLGAIFVVSVLQPYIFIAAIPVAVIFIMLrayfLRTSQQLK-QLESEARSPIFSHLITSLKGLWTIRAF 1080
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 210 GLNKTY------ADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTLSIAIIAVFLGFGLMNntiqllpalIILTLAPDY 283
Cdd:TIGR01271 1081 GRQSYFetlfhkALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVG---------IILTLAMNI 1151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 284 FAPIR---NFANDYHATLNGKNTLTAVLDILQR-PTPTDR-------DLLPVRQP----TWQADDTLALNKVNVSYGESQ 348
Cdd:TIGR01271 1152 LSTLQwavNSSIDVDGLMRSVSRVFKFIDLPQEePRPSGGggkyqlsTVLVIENPhaqkCWPSGGQMDVQGLTAKYTEAG 1231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 349 TPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSpQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPYLFHASLRD 428
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRK 1310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 429 NLAFYAPGASEEaVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIET 508
Cdd:TIGR01271 1311 NLDPYEQWSDEE-IWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA-KILLLDEPSAHLDPVT 1388
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1834933330 509 EVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQ 551
Cdd:TIGR01271 1389 LQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
143-568 |
3.17e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 132.79 E-value: 3.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 143 WIVLIYIAFIQWKEALFLLAIYPLIIFFMiilglaaqakadRQYAGYQRLSNHF--VDTLRGLPTLKQLG--LNKTYADN 218
Cdd:PLN03232 1036 WQLLSTFALIGTVSTISLWAIMPLLILFY------------AAYLYYQSTSREVrrLDSVTRSPIYAQFGeaLNGLSSIR 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 219 VYQVSEDYRK---KTMST---LTIAMTS-----TFALDFFTTLSIAIIAVF--LGFGLMNNTI---QLLPALIILTL-AP 281
Cdd:PLN03232 1104 AYKAYDRMAKingKSMDNnirFTLANTSsnrwlTIRLETLGGVMIWLTATFavLRNGNAENQAgfaSTMGLLLSYTLnIT 1183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 282 DYFAPIRNFANDYHATLNGKNTLTAVLDILQRPTPTDRDLLPVrqPTWQADDTLALNKVNVSYGESQTPTLKDITFSVHG 361
Cdd:PLN03232 1184 TLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPV--SGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSP 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 362 FQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPYLFHASLRDNLAFYAPgASEEA 441
Cdd:PLN03232 1262 SEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSE-HNDAD 1340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 442 VMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFD 521
Cdd:PLN03232 1341 LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRS-KILVLDEATASVDVRTDSLIQRTIREEFK 1419
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1834933330 522 HHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAE-LEQQGGTYVRL 568
Cdd:PLN03232 1420 SCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQElLSRDTSAFFRM 1467
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
335-558 |
9.67e-32 |
|
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: 122.99 E-value: 9.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGES--QTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSF 412
Cdd:COG1124 2 LEVRNLSVSYGQGgrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 413 VYIPQAPYL-FH------ASLRDNLAFYAPGASEEAVMQAAAKAGltdwiatLPDGLATQIgegARGVSGGQAQRIALAR 485
Cdd:COG1124 82 QMVFQDPYAsLHprhtvdRILAEPLRIHGLPDREERIAELLEQVG-------LPPSFLDRY---PHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 486 AFLDDSrRVLLFDEPTAHLDIETEVE-------LKRamlpvfDHHLVF-FATHRLHWMNEM-DYILVMDHGKIVQQGTPA 556
Cdd:COG1124 152 ALILEP-ELLLLDEPTSALDVSVQAEilnllkdLRE------ERGLTYlFVSHDLAVVAHLcDRVAVMQNGRIVEELTVA 224
|
..
gi 1834933330 557 EL 558
Cdd:COG1124 225 DL 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
335-553 |
1.20e-31 |
|
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: 121.86 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDkqAWQRSFVY 414
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP--PERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLF-HASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAF 487
Cdd:cd03259 77 VFQDYALFpHLTVAENIAFglklrgVPKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 488 LDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDHH--LVFFATHRLHWMNEM-DYILVMDHGKIVQQG 553
Cdd:cd03259 146 AREP-SLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
334-558 |
1.97e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.19 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYGEsqTPTLKDITFSVH--GFqkVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDkqAWQRS 411
Cdd:COG3839 3 SLELENVSKSYGG--VEALKDIDLDIEdgEF--LVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP--PKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAPYLF-HASLRDNLAFY-----APGAS-EEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALA 484
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlklrkVPKAEiDRRVREAAELLGLEDLLDRKPKQL-----------SGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 485 RAFLDDSrRVLLFDEPTAHLD----IETEVELKR-------AMLpvfdhhlvfFATHRLHwmnE-M---DYILVMDHGKI 549
Cdd:COG3839 146 RALVREP-KVFLLDEPLSNLDaklrVEMRAEIKRlhrrlgtTTI---------YVTHDQV---EaMtlaDRIAVMNDGRI 212
|
....*....
gi 1834933330 550 VQQGTPAEL 558
Cdd:COG3839 213 QQVGTPEEL 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
335-558 |
6.50e-31 |
|
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: 120.36 E-value: 6.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFL-----SPQDGQINVRDTAVPHLDKQ--A 407
Cdd:cd03260 1 IELRDLNVYYGDKHA--LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 408 WQRSFVYIPQAPYLFHASLRDNLAfYAP---GASEEAVMQAAAKAGLTdwIATLPDGLATQIgeGARGVSGGQAQRIALA 484
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA-YGLrlhGIKLKEELDERVEEALR--KAALWDEVKDRL--HALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834933330 485 RAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:cd03260 154 RALANEP-EVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
340-551 |
1.02e-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: 121.11 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 340 VNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSpQDGQINVRDTAVPHLDKQAWQRSFVYIPQAP 419
Cdd:cd03289 8 LTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 420 YLFHASLRDNLAFYAPGASEEaVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDE 499
Cdd:cd03289 87 FIFSGTFRKNLDPYGKWSDEE-IWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA-KILLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1834933330 500 PTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQ 551
Cdd:cd03289 165 PSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
335-553 |
1.78e-30 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 119.15 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSY--GESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDK--QAWQR 410
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 411 SFV-YIPQAPY-----------LFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIAT-LPDGLatqigegargvSGGQ 477
Cdd:cd03257 82 KEIqMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrYPHEL-----------SGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 478 AQRIALARAFLDDSrRVLLFDEPTAHLDIETEV-----------ELKRAMLpvfdhhlvfFATHRLHWMNEM-DYILVMD 545
Cdd:cd03257 151 RQRVAIARALALNP-KLLIADEPTSALDVSVQAqildllkklqeELGLTLL---------FITHDLGVVAKIaDRVAVMY 220
|
....*...
gi 1834933330 546 HGKIVQQG 553
Cdd:cd03257 221 AGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
307-558 |
4.36e-30 |
|
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: 123.86 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 307 VLDILQRP-----TPTDRDLLPVRQPTWQADDT-LALNKVNVSYGESQTPT---LKDITFSVHGFQKVGIIGASGSGKST 377
Cdd:COG1123 227 PEEILAAPqalaaVPRLGAARGRAAPAAAAAEPlLEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKST 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 378 LINTLGGFLSPQDGQINVRDTAVPHLDKQA--WQRSFV-YIPQAPYlfhASL------RDNLAF-------YAPGASEEA 441
Cdd:COG1123 307 LARLLLGLLRPTSGSILFDGKDLTKLSRRSlrELRRRVqMVFQDPY---SSLnprmtvGDIIAEplrlhglLSRAERRER 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 442 VMQAAAKAGLTDWIAT-LPDGLatqigegargvSGGQAQRIALARAFLDDSrRVLLFDEPTAHLD--IETEV-----ELK 513
Cdd:COG1123 384 VAELLERVGLPPDLADrYPHEL-----------SGGQRQRVAIARALALEP-KLLILDEPTSALDvsVQAQIlnllrDLQ 451
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1834933330 514 RamlpvfDHHL-VFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:COG1123 452 R------ELGLtYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEV 492
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
335-549 |
6.89e-30 |
|
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: 115.39 E-value: 6.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVY 414
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLFHASLRDNLafyapgaseeavmqaaakagltdwiatlpdglatqigegargVSGGQAQRIALARAFLDDsRRV 494
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGN-PRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1834933330 495 LLFDEPTAHLDIETEVELKRA--MLPVFDHHLVFFAtHRLHWMNEMDYILVMDHGKI 549
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAiaALKAAGATRIVIA-HRPETLASADRILVLEDGRV 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
335-549 |
1.57e-29 |
|
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: 116.05 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSY--GESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAW---- 408
Cdd:cd03255 1 IELKNLSKTYggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 409 QRSFVYIPQAPYLF-HASLRDNLA---FYAPGASEEAVMQAAA---KAGLTDWIATLPDGLatqigegargvSGGQAQRI 481
Cdd:cd03255 81 RRHIGFVFQSFNLLpDLTALENVElplLLAGVPKKERRERAEElleRVGLGDRLNHYPSEL-----------SGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834933330 482 ALARAFLDDSrRVLLFDEPTAHLDIET--EV-----ELKRAMlpvfdHHLVFFATHRLHWMNEMDYILVMDHGKI 549
Cdd:cd03255 150 AIARALANDP-KIILADEPTGNLDSETgkEVmellrELNKEA-----GTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-558 |
1.66e-29 |
|
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: 122.32 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQ---DGQINVRDTAVPHLDKQAWQRS 411
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAPY--LFHASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIAL 483
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAEalenlgLSRAEARARVLELLEAVGLERRLDRYPHQL-----------SGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 484 ARAFLDDSrRVLLFDEPTAHLDIETEVELKRAM--LPVFDHHLVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:COG1123 154 AMALALDP-DLLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEI 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
335-558 |
3.12e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 115.62 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGEsqtpTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDtaVPHLDKQAWQRSFVY 414
Cdd:COG3840 2 LRLDDLTYRYGD----FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG--QDLTALPPAERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLF-HASLRDNLAF-YAPG-----ASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAF 487
Cdd:COG3840 76 LFQENNLFpHLTVAQNIGLgLRPGlkltaEQRAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 488 LDDsRRVLLFDEPTAHLDIetevELKRAMLpvfdhHLV-----------FFATHRLhwmNEM----DYILVMDHGKIVQQ 552
Cdd:COG3840 145 VRK-RPILLLDEPFSALDP----ALRQEML-----DLVdelcrergltvLMVTHDP---EDAariaDRVLLVADGRIAAD 211
|
....*.
gi 1834933330 553 GTPAEL 558
Cdd:COG3840 212 GPTAAL 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
335-533 |
3.40e-29 |
|
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: 115.26 E-value: 3.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTPT--LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVphldkQAWQRSF 412
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 413 VYIPQAPYLF-HASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALAR 485
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNVALglelqgVPKAEARERAEELLELVGLSGFENAYPHQL-----------SGGMRQRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1834933330 486 AFLDDsRRVLLFDEPTAHLDIETEVELKRAMLPVFDHHL--VFFATHRLH 533
Cdd:cd03293 145 ALAVD-PDVLLLDEPFSALDALTREQLQEELLDIWRETGktVLLVTHDID 193
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-557 |
4.35e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.57 E-value: 4.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVphldKQAWQRsfV- 413
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP----RRARRR--Ig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YIPQAPYL---FHASLRDNLA---------FYAPGASE-EAVMQAAAKAGLTDwiatlpdgLA-TQIGEgargVSGGQAQ 479
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVLmgrygrrglFRRPSRADrEAVDEALERVGLED--------LAdRPIGE----LSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 480 RIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMlpvfdHHL------VFFATHRLHW-MNEMDYILVMDHGkIVQQ 552
Cdd:COG1121 147 RVLLARALAQDP-DLLLLDEPFAGVDAATEEALYELL-----RELrregktILVVTHDLGAvREYFDRVLLLNRG-LVAH 219
|
....*
gi 1834933330 553 GTPAE 557
Cdd:COG1121 220 GPPEE 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
335-530 |
5.40e-29 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 114.11 E-value: 5.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVpHLDKQAWQRSFVY 414
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLFHA-SLRDNLAFYA----PGASEEAVMQAAAKAGLTDwIATLPdglatqigegARGVSGGQAQRIALARAFLD 489
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAG-LADLP----------VRQLSAGQKRRVALARLLLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1834933330 490 DsRRVLLFDEPTAHLDIETEVELKRAMlpvfDHHL-----VFFATH 530
Cdd:COG4133 149 P-APLWLLDEPFTALDAAGVALLAELI----AAHLarggaVLLTTH 189
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
335-549 |
1.60e-28 |
|
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: 111.72 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGesQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVrDTAVPHLDKQAWQRSFVY 414
Cdd:cd03230 1 IEVRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-LGKDIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLF-HASLRDNLAFyapgaseeavmqaaakagltdwiatlpdglatqigegargvSGGQAQRIALARAFLDDSrR 493
Cdd:cd03230 78 LPEEPSLYeNLTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDP-E 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 494 VLLFDEPTAHLDIETEVELKRAMLP-VFDHHLVFFATHRLHWMNEM-DYILVMDHGKI 549
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
330-530 |
7.08e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 112.49 E-value: 7.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 330 QADDTLALNKVNVSYGESQTPT--LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQa 407
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 408 wqRSFVyiPQAPYLF-HASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQR 480
Cdd:COG1116 82 --RGVV--FQEPALLpWLTVLDNVALglelrgVPKAERRERARELLELVGLAGFEDAYPHQL-----------SGGMRQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1834933330 481 IALARAFLDDsRRVLLFDEPTAHLDIETEVELKRAMLPVFDHH--LVFFATH 530
Cdd:COG1116 147 VAIARALAND-PEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTH 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
341-553 |
1.62e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.06 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPqapy 420
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 421 lfhaslrdnlafyapgaseeavmQAAAKAGLTDwiatlpdgLATQ-IGEgargVSGGQAQRIALARAFLDDSrRVLLFDE 499
Cdd:cd03214 80 -----------------------QALELLGLAH--------LADRpFNE----LSGGERQRVLLARALAQEP-PILLLDE 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 500 PTAHLDIETEVELkraMLPVFDHH-----LVFFATHRL-HWMNEMDYILVMDHGKIVQQG 553
Cdd:cd03214 124 PTSHLDIAHQIEL---LELLRRLArergkTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
340-558 |
2.01e-27 |
|
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: 110.89 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 340 VNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYipQAP 419
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF--QHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 420 YLF-HASLRDNLAF---YAPGASE--EAVMQAAAKAGLT----DWIAtlpDGLATQIgegargvSGGQAQRIALARAfLD 489
Cdd:cd03296 84 ALFrHMTVFDNVAFglrVKPRSERppEAEIRAKVHELLKlvqlDWLA---DRYPAQL-------SGGQRQRVALARA-LA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834933330 490 DSRRVLLFDEPTAHLDIETEVELKRAMLPVFD--HHLVFFATH-RLHWMNEMDYILVMDHGKIVQQGTPAEL 558
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
337-548 |
2.38e-27 |
|
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: 107.72 E-value: 2.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGESqtPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIP 416
Cdd:cd00267 2 IENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QApylfhaslrdnlafyapgaseeavmqaaakagltdwiatlpdglatqigegargvSGGQAQRIALARAFLDDsRRVLL 496
Cdd:cd00267 80 QL-------------------------------------------------------SGGQRQRVALARALLLN-PDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 497 FDEPTAHLDIETEVELKRAMLPVFDHHL-VFFATHRLHWMNE-MDYILVMDHGK 548
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRtVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
337-567 |
2.54e-27 |
|
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: 110.28 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHL---DKQAWQRSFV 413
Cdd:cd03261 3 LRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YIPQAPYLFHA-SLRDNLAF-------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALAR 485
Cdd:cd03261 81 MLFQSGALFDSlTVFENVAFplrehtrLSEEEIREIVLEKLEAVGLRGAEDLYPAEL-----------SGGMKKRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 486 AFLDDSrRVLLFDEPTAHLD-IETEV------ELKRAMlpvfdHHLVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAE 557
Cdd:cd03261 150 ALALDP-ELLLYDEPTAGLDpIASGViddlirSLKKEL-----GLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEE 223
|
250
....*....|
gi 1834933330 558 LEQQGGTYVR 567
Cdd:cd03261 224 LRASDDPLVR 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
334-558 |
2.94e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 117.57 E-value: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINV--RDTAVPHLdkQAWQRS 411
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVngREIGAYGL--RELRRQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAPYLFHASLRDNLAFYAPGASEEaVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDS 491
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNVDPFLEASSAE-VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKG 1464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834933330 492 RRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAEL 558
Cdd:PTZ00243 1465 SGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
334-558 |
5.33e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 112.16 E-value: 5.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYGesQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQI--NVRDTAVpHLDKQawQRS 411
Cdd:COG1118 2 SIEVRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIvlNGRDLFT-NLPPR--ERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAPYLF-HASLRDNLAFyapGASEEAVMQAAAKAGLTDWIATLP-DGLA----TQIgegargvSGGQAQRIALAR 485
Cdd:COG1118 77 VGFVFQHYALFpHMTVAENIAF---GLRVRPPSKAEIRARVEELLELVQlEGLAdrypSQL-------SGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 486 AfLDDSRRVLLFDEPTAHLDIETEVELKRAMLPVFD--HHLVFFATH------RLhwmneMDYILVMDHGKIVQQGTPAE 557
Cdd:COG1118 147 A-LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDE 220
|
.
gi 1834933330 558 L 558
Cdd:COG1118 221 V 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
354-558 |
8.97e-27 |
|
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: 111.73 E-value: 8.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 354 DITFSVHGfQKV-GIIGASGSGKSTLINTLGGFLSPQDGQINV---------RDTAVPhldkqAWQRSFVYIPQAPYLF- 422
Cdd:COG4148 17 DVDFTLPG-RGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsaRGIFLP-----PHRRRIGYVFQEARLFp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 423 HASLRDNLAFyapGASeeAVMQAAAKAGLTDWIATLpdGLATQIGEGARGVSGGQAQRIALARAFLddSR-RVLLFDEPT 501
Cdd:COG4148 91 HLSVRGNLLY---GRK--RAPRAERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALL--SSpRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834933330 502 AHLDieteVELKRAMLPVFD---HHL---VFFATHRlhwMNEM----DYILVMDHGKIVQQGTPAEL 558
Cdd:COG4148 162 AALD----LARKAEILPYLErlrDELdipILYVSHS---LDEVarlaDHVVLLEQGRVVASGPLAEV 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
327-564 |
1.48e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 115.22 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 327 PTWQADDTLALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQ 406
Cdd:PLN03130 1230 PGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLM 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 407 AWQRSFVYIPQAPYLFHASLRDNLAFYAPgASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARA 486
Cdd:PLN03130 1310 DLRKVLGIIPQAPVLFSGTVRFNLDPFNE-HNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARA 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 487 FLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGT 564
Cdd:PLN03130 1389 LLRRS-KILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
337-558 |
1.88e-26 |
|
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: 108.67 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINV--RDTAVPhldKQAWQ-RSFV 413
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVdgLDTLDE---ENLWEiRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 -YIPQAP--YLFHASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALA 484
Cdd:TIGR04520 80 gMVFQNPdnQFVGATVEDDVAFglenlgVPREEMRKRVDEALKLVGMEDFRDREPHLL-----------SGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 485 RAfLDDSRRVLLFDEPTAHLD-------IETEVELKRamlpvfDHHL-VFFATHRlhwMNEM---DYILVMDHGKIVQQG 553
Cdd:TIGR04520 149 GV-LAMRPDIIILDEATSMLDpkgrkevLETIRKLNK------EEGItVISITHD---MEEAvlaDRVIVMNKGKIVAEG 218
|
....*
gi 1834933330 554 TPAEL 558
Cdd:TIGR04520 219 TPREI 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
340-567 |
2.60e-26 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 107.37 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 340 VNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQR-----SFVY 414
Cdd:COG1127 11 LTKSFGD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYElrrriGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 ipQAPYLFHA-SLRDNLAF-------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARA 486
Cdd:COG1127 89 --QGGALFDSlTVFENVAFplrehtdLSEAEIRELVLEKLELVGLPGAADKMPSEL-----------SGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 487 FLDDSrRVLLFDEPTAHLDIETE-------VELKRAMlpvfdhHL-VFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAE 557
Cdd:COG1127 156 LALDP-EILLYDEPTAGLDPITSavideliRELRDEL------GLtSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEE 228
|
250
....*....|
gi 1834933330 558 LEQQGGTYVR 567
Cdd:COG1127 229 LLASDDPWVR 238
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
335-557 |
2.43e-25 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 104.73 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQtptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQawQRSFVY 414
Cdd:cd03299 1 LKVENLSKDWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLF-HASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAF 487
Cdd:cd03299 76 VPQNYALFpHMTVYKNIAYglkkrkVDKKEIERKVLEIAEMLGIDHLLNRKPETL-----------SGGEQQRVAIARAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 488 LDDSrRVLLFDEPTAHLDIETEVELkRAMLPVFDHHLVFFATHRLHWMNEM----DYILVMDHGKIVQQGTPAE 557
Cdd:cd03299 145 VVNP-KILLLDEPFSALDVRTKEKL-REELKKIRKEFGVTVLHVTHDFEEAwalaDKVAIMLNGKLIQVGKPEE 216
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
337-557 |
5.71e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.21 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGESQtPTLKDITFSVH--GFqkVGIIGASGSGKSTLINTLGGFLSPQDGQINV--------RDTAVPHLdkq 406
Cdd:COG2884 4 FENVSKRYPGGR-EALSDVSLEIEkgEF--VFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlsrlKRREIPYL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 407 awQRSFVYIPQ-APYLFHASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQ 479
Cdd:COG2884 78 --RRRIGVVFQdFRLLPDRTVYENVALplrvtgKSRKEIRRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 480 RIALARAFLDDSrRVLLFDEPTAHLDIETEVELkramLPVFD--HHL---VFFATHRLHWMNEMDY-ILVMDHGKIVQQG 553
Cdd:COG2884 145 RVAIARALVNRP-ELLLADEPTGNLDPETSWEI----MELLEeiNRRgttVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
....
gi 1834933330 554 TPAE 557
Cdd:COG2884 220 ARGV 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
242-575 |
8.20e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 110.07 E-value: 8.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 242 FALDFFTTLSIAIIAVFLGFG---LMNNTIQLLPALIILTLAPDYFAPIRNFANDYHATLNGKNTLTAVLDILQrptpTD 318
Cdd:PLN03232 523 SAFNSFILNSIPVVVTLVSFGvfvLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLL----SE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 319 RDLLPVRQPTWQADDTLALNKVNVSY-GESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSP-QDGQINVR 396
Cdd:PLN03232 599 ERILAQNPPLQPGAPAISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIR 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 397 DTAVphldkqawqrsfvYIPQAPYLFHASLRDNLAFYAPGASEEaVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGG 476
Cdd:PLN03232 679 GSVA-------------YVPQVSWIFNATVRENILFGSDFESER-YWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGG 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 477 QAQRIALARAFLDDSrRVLLFDEPTAHLDIETEVElkramlpVFD----HHLV----FFATHRLHWMNEMDYILVMDHGK 548
Cdd:PLN03232 745 QKQRVSMARAVYSNS-DIYIFDDPLSALDAHVAHQ-------VFDscmkDELKgktrVLVTNQLHFLPLMDRIILVSEGM 816
|
330 340
....*....|....*....|....*..
gi 1834933330 549 IVQQGTPAELEQQGGTYVRLrseMEGA 575
Cdd:PLN03232 817 IKEEGTFAELSKSGSLFKKL---MENA 840
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
337-558 |
1.05e-24 |
|
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: 102.20 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVnvsYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVpHLDKQAWQRSFVYIP 416
Cdd:cd03263 6 LTKT---YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QAPYLFHA-SLRDNLAFYA-----PGASEEAVMQAAAKA-GLTDWIATLpdglatqigegARGVSGGQAQRIALARAFLD 489
Cdd:cd03263 82 QFDALFDElTVREHLRFYArlkglPKSEIKEEVELLLRVlGLTDKANKR-----------ARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 490 DSrRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRlhwMNEM----DYILVMDHGKIVQQGTPAEL 558
Cdd:cd03263 151 GP-SVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHS---MDEAealcDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
342-561 |
1.10e-24 |
|
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: 103.45 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 342 VSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPYL 421
Cdd:cd03288 27 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPIL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 422 FHASLRDNLAfyaP--GASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSRrVLLFDE 499
Cdd:cd03288 107 FSGSIRFNLD---PecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS-ILIMDE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834933330 500 PTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQ 561
Cdd:cd03288 183 ATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
341-548 |
1.56e-24 |
|
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: 100.72 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQ--AWQRSFVYIPQA 418
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 419 PYLF-HASLRDNLAFyapgaseeavmqaaakagltdwiatlpdglatqigegarGVSGGQAQRIALARAFLDDSrRVLLF 497
Cdd:cd03229 85 FALFpHLTVLENIAL---------------------------------------GLSGGQQQRVALARALAMDP-DVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 498 DEPTAHLDIETEVELKRAMLPVFDHH--LVFFATHRLHWMNEM-DYILVMDHGK 548
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
352-571 |
1.84e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 108.71 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQInvrdtavphldkqaW-QRSFVYIPQAPYLFHASLRDNL 430
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WaERSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 431 AFYAPgaSEEAVMQAAAK-AGLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDsRRVLLFDEPTAHLDIETE 509
Cdd:PTZ00243 742 LFFDE--EDAARLADAVRvSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYAN-RDVYLLDDPLSALDAHVG 818
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834933330 510 velKRAMLPVFDHHLV----FFATHRLHWMNEMDYILVMDHGKIVQQGTPAELeQQGGTYVRLRSE 571
Cdd:PTZ00243 819 ---ERVVEECFLGALAgktrVLATHQVHVVPRADYVVALGDGRVEFSGSSADF-MRTSLYATLAAE 880
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
346-575 |
2.20e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 108.67 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 346 ESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSP-QDGQINVRDTAVphldkqawqrsfvYIPQAPYLFHA 424
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTVA-------------YVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 425 SLRDNLAFYAPGASEEaVMQAAAKAGLTDWIATLPDGLATQIGEgaRGV--SGGQAQRIALARAFLDDSrRVLLFDEPTA 502
Cdd:PLN03130 694 TVRDNILFGSPFDPER-YERAIDVTALQHDLDLLPGGDLTEIGE--RGVniSGGQKQRVSMARAVYSNS-DVYIFDDPLS 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 503 HLD-----------IETEVELKRAMLpvfdhhlvffATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTYVRLrse 571
Cdd:PLN03130 770 ALDahvgrqvfdkcIKDELRGKTRVL----------VTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL--- 836
|
....
gi 1834933330 572 MEGA 575
Cdd:PLN03130 837 MENA 840
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
335-558 |
3.94e-24 |
|
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: 101.16 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGesQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDkqAWQRSFVY 414
Cdd:cd03300 1 IELENVSKFYG--GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP--PHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLF-HASLRDNLAF-----YAPGAS-EEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAF 487
Cdd:cd03300 77 VFQNYALFpHLTVFENIAFglrlkKLPKAEiKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 488 LDDSrRVLLFDEPTAHLDI----ETEVELKRAmlpvfdHHLV----FFATH-RLHWMNEMDYILVMDHGKIVQQGTPAEL 558
Cdd:cd03300 146 VNEP-KVLLLDEPLGALDLklrkDMQLELKRL------QKELgitfVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
337-558 |
4.18e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.99 E-value: 4.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIP 416
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QAP--YLFHASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAFL 488
Cdd:PRK13632 90 QNPdnQFIGATVEDDIAFglenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834933330 489 DDSrRVLLFDEPTAHLDIETEVELKRAMLPVFD--HHLVFFATHRlhwMNEM---DYILVMDHGKIVQQGTPAEL 558
Cdd:PRK13632 159 LNP-EIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHD---MDEAilaDKVIVFSEGKLIAQGKPKEI 229
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
24-300 |
5.42e-24 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. 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). 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: 350054 [Multi-domain] Cd Length: 290 Bit Score: 102.23 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 24 FVQAFMIIFQAKYLSVAIVNLWQLKSvrtIVLPLLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMAKLFDLGPS 103
Cdd:cd18781 10 LANIAFVFSIANLLQKLLEGKLTTAS---LLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLRLGPS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 104 VVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLTPWIVLIYIAFIQWKEALFLLAIYPLIIFFMIILGLAAQAKAD 183
Cdd:cd18781 87 YQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKIAKKLLS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 184 RQYAGYQRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMSTLTIAMTSTFALDFF----TTLSIaIIAVfl 259
Cdd:cd18781 167 KYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVayggAALGI-ILAL-- 243
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1834933330 260 gFGLMNNTIQLLPALIILTLAPDYFAPIRNFANDYHATLNG 300
Cdd:cd18781 244 -LQFANGSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNG 283
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
335-558 |
6.25e-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: 100.20 E-value: 6.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLdkQAWQRSF-- 412
Cdd:cd03224 1 LEVENLNAGYGKSQI--LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL--PPHERARag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 413 -VYIPQAPYLFHA-SLRDNLAFYApgaseEAVMQAAAKAGLtDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDD 490
Cdd:cd03224 77 iGYVPEGRRIFPElTVEENLLLGA-----YARRRAKRKARL-ERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 491 sRRVLLFDEPTAHL------DIETEV-ELKR---AMLPVfDHHlVFFATHRlhwmneMDYILVMDHGKIVQQGTPAEL 558
Cdd:cd03224 151 -PKLLLLDEPSEGLapkiveEIFEAIrELRDegvTILLV-EQN-ARFALEI------ADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
335-553 |
8.97e-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: 99.49 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGEsqTPTLKDITFSvhGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVY 414
Cdd:cd03298 1 VRLDKIRFSYGE--QPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 ipQAPYLF-HASLRDNLAF-YAPG-----ASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAF 487
Cdd:cd03298 77 --QENNLFaHLTVEQNVGLgLSPGlkltaEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 488 LDDsRRVLLFDEPTAHLDieteVELKRAMLP-VFDHH-----LVFFATHRLHWMNEM-DYILVMDHGKIVQQG 553
Cdd:cd03298 144 VRD-KPVLLLDEPFAALD----PALRAEMLDlVLDLHaetkmTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
337-549 |
3.37e-23 |
|
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: 97.99 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHlDKQAWQR-----S 411
Cdd:cd03262 3 IKNLHKSFGDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINElrqkvG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYipQAPYLF-HASLRDNLAFyAP----GASEEAV----MQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIA 482
Cdd:cd03262 80 MVF--QQFNLFpHLTVLENITL-APikvkGMSKAEAeeraLELLEKVGLADKADAYPAQL-----------SGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 483 LARAFLDDSrRVLLFDEPTAHLDIET--EV-----ELKR---AMLPVfdhhlvffaTHrlhwmnEM-------DYILVMD 545
Cdd:cd03262 146 IARALAMNP-KVMLFDEPTSALDPELvgEVldvmkDLAEegmTMVVV---------TH------EMgfarevaDRVIFMD 209
|
....
gi 1834933330 546 HGKI 549
Cdd:cd03262 210 DGRI 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
341-549 |
3.77e-23 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 97.60 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDtavphLDKQAWQRSFVYIPQ--- 417
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYVPQrrs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 418 APYLFHASLRD----------NLAFYAPGASEEAVMQAAAKAGLTDwiatlpdgLAT-QIGEgargVSGGQAQRIALARA 486
Cdd:cd03235 79 IDRDFPISVRDvvlmglyghkGLFRRLSKADKAKVDEALERVGLSE--------LADrQIGE----LSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834933330 487 FLDDsRRVLLFDEPTAHLDIETEVELKRAMLPVFDH-HLVFFATHRLHW-MNEMDYILVMDHGKI 549
Cdd:cd03235 147 LVQD-PDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLvLEYFDRVLLLNRTVV 210
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
343-565 |
1.28e-22 |
|
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: 103.10 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 343 SYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDtavphldkqawqrSFVYIPQAPYLF 422
Cdd:TIGR00957 645 TWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 423 HASLRDNLAFYAPGASE--EAVMQAAAKagLTDwIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEP 500
Cdd:TIGR00957 712 NDSLRENILFGKALNEKyyQQVLEACAL--LPD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA-DIYLFDDP 787
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 501 TAHLD------IETEVELKRAMLPVFDHHLVffaTHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQGGTY 565
Cdd:TIGR00957 788 LSAVDahvgkhIFEHVIGPEGVLKNKTRILV---THGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
347-567 |
1.29e-22 |
|
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: 97.71 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 347 SQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQR------SFVYipQAPY 420
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkkiSMVF--QSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 421 LF-HASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAFLDDSrR 493
Cdd:cd03294 113 LLpHRTVLENVAFglevqgVPRAEREERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDP-D 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 494 VLLFDEPTAHLD--IETE-----VELKRAMlpvfdHHLVFFATHRLhwmNEM----DYILVMDHGKIVQQGTPAE-LEQQ 561
Cdd:cd03294 181 ILLMDEAFSALDplIRREmqdelLRLQAEL-----QKTIVFITHDL---DEAlrlgDRIAIMKDGRLVQVGTPEEiLTNP 252
|
....*.
gi 1834933330 562 GGTYVR 567
Cdd:cd03294 253 ANDYVR 258
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
334-562 |
1.41e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.39 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFV 413
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YIPQ------------------APYLfhaSLRDNLAfyapGASEEAVMQAAAKAGltdwIATLPDGLATQIgegargvSG 475
Cdd:PRK11231 80 LLPQhhltpegitvrelvaygrSPWL---SLWGRLS----AEDNARVNQAMEQTR----INHLADRRLTDL-------SG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 476 GQAQRIALARAFLDDSRRVLLfDEPTAHLDIETEVELKRAMLPVFDHHLVFFAThrLHWMNEM----DYILVMDHGKIVQ 551
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLL-DEPTTYLDINHQVELMRLMRELNTQGKTVVTV--LHDLNQAsrycDHLVVLANGHVMA 218
|
250
....*....|.
gi 1834933330 552 QGTPAELEQQG 562
Cdd:PRK11231 219 QGTPEEVMTPG 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
347-547 |
2.41e-22 |
|
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: 95.48 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 347 SQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQI---NVRDTAVPHLDKQAWQR-SFVYIPQAPYLF 422
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRySVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 423 HASLRDNLAFYAPGASE--EAVMQAAAkagLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSRRVLLfDEP 500
Cdd:cd03290 92 NATVEENITFGSPFNKQryKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL-DDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1834933330 501 TAHLDIETEVELKRAMLPVF---DHHLVFFATHRLHWMNEMDYILVMDHG 547
Cdd:cd03290 168 FSALDIHLSDHLMQEGILKFlqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
341-558 |
2.78e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.93 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTL---INTL----GGFLSpQDGqINVRDtavPHLDKQAWQRSFV 413
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKLeeitSGDLI-VDG-LKVND---PKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YIPQAPYLF-HASLRDNLAFyAP----GASEEAVMQAA----AKAGLTDWIATLPDGLatqigegargvSGGQAQRIALA 484
Cdd:PRK09493 81 MVFQQFYLFpHLTALENVMF-GPlrvrGASKEEAEKQArellAKVGLAERAHHYPSEL-----------SGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834933330 485 RAfLDDSRRVLLFDEPTAHLDIETEVELKRAMLPVFDHHL-VFFATHRLHWMNEMDYILV-MDHGKIVQQGTPAEL 558
Cdd:PRK09493 149 RA-LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMtMVIVTHEIGFAEKVASRLIfIDKGRIAEDGDPQVL 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
335-568 |
3.11e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.01 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPhlDKQAWQ--RSF 412
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS--EETVWDvrRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 413 VYIPQAP--YLFHASLRDNLAFyapgASE----------EAVMQAAAKAGLTDWiatlpdglATQigEGARgVSGGQAQR 480
Cdd:PRK13635 84 GMVFQNPdnQFVGATVQDDVAF----GLEnigvpreemvERVDQALRQVGMEDF--------LNR--EPHR-LSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 481 IALArAFLDDSRRVLLFDEPTAHLD-------IETEVELKR-AMLPVFDhhlvffATHRLHWMNEMDYILVMDHGKIVQQ 552
Cdd:PRK13635 149 VAIA-GVLALQPDIIILDEATSMLDprgrrevLETVRQLKEqKGITVLS------ITHDLDEAAQADRVIVMNKGEILEE 221
|
250
....*....|....*.
gi 1834933330 553 GTPAELEQQGGTYVRL 568
Cdd:PRK13635 222 GTPEEIFKSGHMLQEI 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
334-558 |
3.11e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 98.23 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFV 413
Cdd:PRK10851 2 SIEIANIKKSFGRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YipQAPYLF-HASLRDNLAF--------YAPGASE--EAVMQaaakagLTDWI--ATLPDGLATQIgegargvSGGQAQR 480
Cdd:PRK10851 80 F--QHYALFrHMTVFDNIAFgltvlprrERPNAAAikAKVTQ------LLEMVqlAHLADRYPAQL-------SGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 481 IALARAfLDDSRRVLLFDEPTAHLDIETEVELKRaMLPVFDHHLVF---FATH-RLHWMNEMDYILVMDHGKIVQQGTPA 556
Cdd:PRK10851 145 VALARA-LAVEPQILLLDEPFGALDAQVRKELRR-WLRQLHEELKFtsvFVTHdQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
..
gi 1834933330 557 EL 558
Cdd:PRK10851 223 QV 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
335-561 |
5.70e-22 |
|
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: 94.94 E-value: 5.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAV---PHLDKQAWQRS 411
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAPYL----------------FHASLRDNLAFYAPGASEEAvMQAAAKAGLTDWIATLPDGLatqigegargvSG 475
Cdd:cd03256 80 IGMIFQQFNLierlsvlenvlsgrlgRRSTWRSLFGLFPKEEKQRA-LAALERVGLLDKAYQRADQL-----------SG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 476 GQAQRIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFD----------HHLVFFATHrlhwmneMDYILVMD 545
Cdd:cd03256 148 GQQQRVAIARALMQQP-KLILADEPVASLDPASSRQVMDLLKRINReegitvivslHQVDLAREY-------ADRIVGLK 219
|
250
....*....|....*.
gi 1834933330 546 HGKIVQQGTPAELEQQ 561
Cdd:cd03256 220 DGRIVFDGPPAELTDE 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
331-558 |
8.07e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.46 E-value: 8.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 331 ADDTLALNKVNVSYGESQTPTLK---DITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAV-PHLDKQ 406
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQENELValnNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 407 AWQR-----------------SFVYipQAP--YLFHASLRDNLAF--YAPGASEEAVMQAAA----KAGL-TDWIATLPD 460
Cdd:PRK13631 98 ELITnpyskkiknfkelrrrvSMVF--QFPeyQLFKDTIEKDIMFgpVALGVKKSEAKKLAKfylnKMGLdDSYLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 461 GLatqigegargvSGGQAQRIALArAFLDDSRRVLLFDEPTAHLDIETEVELKRAMLPV-FDHHLVFFATHRLHWMNEM- 538
Cdd:PRK13631 176 GL-----------SGGQKRRVAIA-GILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVLEVa 243
|
250 260
....*....|....*....|
gi 1834933330 539 DYILVMDHGKIVQQGTPAEL 558
Cdd:PRK13631 244 DEVIVMDKGKILKTGTPYEI 263
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
335-553 |
8.60e-22 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 93.86 E-value: 8.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPhlDKQAWQRSFVY 414
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLF-HASLRDNLAF------YAPGASEEAVMQAAAKAGltdwIATLPDGLATQIgegargvSGGQAQRIALARAF 487
Cdd:cd03301 77 VFQNYALYpHMTVYDNIAFglklrkVPKDEIDERVREVAELLQ----IEHLLDRKPKQL-------SGGQRQRVALGRAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 488 LDDSrRVLLFDEPTAHLDIETEVELkRAMLPVFDHHL---VFFATH-RLHWMNEMDYILVMDHGKIVQQG 553
Cdd:cd03301 146 VREP-KVFLMDEPLSNLDAKLRVQM-RAELKRLQQRLgttTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
352-557 |
1.28e-21 |
|
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: 94.04 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAV----PHldkQAWQ----RSFvyipQAPYLF- 422
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglpPH---EIARlgigRTF----QIPRLFp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 423 HASLRDNL-----------AFYAPGASEEAVMQAAAKagltDWIATLpdGLATQIGEGARGVSGGQAQRIALARAFLDDS 491
Cdd:cd03219 89 ELTVLENVmvaaqartgsgLLLARARREEREARERAE----ELLERV--GLADLADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 492 rRVLLFDEPTAHLDIETEVELKRAMLPVFDHHL-VFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAE 557
Cdd:cd03219 163 -KLLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
337-558 |
2.48e-21 |
|
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: 93.03 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGES--QTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDK---QAWQRS 411
Cdd:cd03258 4 LKNVSKVFGDTggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAPYLFHA-SLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALA 484
Cdd:cd03258 84 IGMIFQHFNLLSSrTVFENVALpleiagVPKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 485 RAfLDDSRRVLLFDEPTAHLDIETE---VELKRAMLPVFDHHLVFFaTHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:cd03258 153 RA-LANNPKVLLCDEATSALDPETTqsiLALLRDINRELGLTIVLI-THEMEVVKRIcDRVAVMEKGEVVEEGTVEEV 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
238-533 |
2.56e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.96 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 238 MTSTFALDFFTTlsiaiiavflGFGLmnnTIQLLPALIIltlAPDYFA------------------------PIRNFAN- 292
Cdd:COG4178 262 IRRQRNLTFFTT----------GYGQ---LAVIFPILVA---APRYFAgeitlgglmqaasafgqvqgalswFVDNYQSl 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 293 -DYHATLNGKNTLTAVLDILQRPTPTDRDLLPvrqptwQADDTLALNKVNVsygesQTPT----LKDITFSVHGFQKVGI 367
Cdd:COG4178 326 aEWRATVDRLAGFEEALEAADALPEAASRIET------SEDGALALEDLTL-----RTPDgrplLEDLSLSLKPGERLLI 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 368 IGASGSGKSTLINTLGGFLSPQDGQInvrdtAVPHLDKqawqrsFVYIPQAPYLFHASLRDNLAFyaPGA----SEEAVM 443
Cdd:COG4178 395 TGPSGSGKSTLLRAIAGLWPYGSGRI-----ARPAGAR------VLFLPQRPYLPLGTLREALLY--PATaeafSDAELR 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 444 QAAAKAGLTDwiatlpdgLATQIGEGA---RGVSGGQAQRIALARAFLddSR-RVLLFDEPTAHLDIETEVELK---RAM 516
Cdd:COG4178 462 EALEAVGLGH--------LAERLDEEAdwdQVLSLGEQQRLAFARLLL--HKpDWLFLDEATSALDEENEAALYqllREE 531
|
330 340
....*....|....*....|....
gi 1834933330 517 LP-----VFDHH--LVFFATHRLH 533
Cdd:COG4178 532 LPgttviSVGHRstLAAFHDRVLE 555
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
335-558 |
3.59e-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: 92.74 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDkqAWQRS--- 411
Cdd:COG0410 4 LEVENLHAGYGGIHV--LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP--PHRIArlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAPYLFhASL--RDNL--AFYAPGAseeavmQAAAKAGLtDWIATL-PDgLATQIGEGARGVSGGQAQRIALARA 486
Cdd:COG0410 80 IGYVPEGRRIF-PSLtvEENLllGAYARRD------RAEVRADL-ERVYELfPR-LKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 487 FLddSR-RVLLFDEPTAHL------DI-ETEVELKRAMLPVF--DHHLVF---FAthrlhwmnemDYILVMDHGKIVQQG 553
Cdd:COG0410 151 LM--SRpKLLLLDEPSLGLapliveEIfEIIRRLNREGVTILlvEQNARFaleIA----------DRAYVLERGRIVLEG 218
|
....*
gi 1834933330 554 TPAEL 558
Cdd:COG0410 219 TAAEL 223
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
17-301 |
3.66e-21 |
|
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: 94.15 E-value: 3.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 17 AIMAVLTFVQAFMIIFQAKYLSVAIVNLWQLKSVRTIVLPLLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMAK 96
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 97 LFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLTPWIVLIYIAFIQWKEALFLLAIYPLIIFFMIILG- 175
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 176 -LAAQAKADRQYAGyqRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTLSIAI 254
Cdd:cd07346 162 rIRKASREVRESLA--ELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1834933330 255 IAVFLGFGLMNNTIQlLPALI-ILTLAPDYFAPIRNFANDYHATLNGK 301
Cdd:cd07346 240 VLLYGGYLVLQGSLT-IGELVaFLAYLGMLFGPIQRLANLYNQLQQAL 286
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
349-559 |
7.27e-21 |
|
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: 97.29 E-value: 7.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 349 TPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQInvrdtavphldKQAWQRSFVyiPQAPYLFHASLRD 428
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHSGRISFS--PQTSWIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 429 NLAFyapGAS-EEAVMQAAAKA-GLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSRRVLLfDEPTAHLDI 506
Cdd:TIGR01271 506 NIIF---GLSyDEYRYTSVIKAcQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLL-DSPFTHLDV 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 507 ETEVEL-KRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELE 559
Cdd:TIGR01271 582 VTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQ 635
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
337-555 |
8.59e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 8.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGESqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYI- 415
Cdd:PRK13644 4 LENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 416 ---PQAPYLFHaSLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALArA 486
Cdd:PRK13644 83 fqnPETQFVGR-TVEEDLAFgpenlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTL-----------SGGQGQCVALA-G 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 487 FLDDSRRVLLFDEPTAHLDIET-EVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTP 555
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEP 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
332-508 |
9.33e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 9.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 332 DDTLALNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAvphldkqawqrS 411
Cdd:COG0488 313 KKVLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV-----------K 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAPYLFH--ASLRDNLAFYAPGASEEAVMQAAAKAGLTdwiatlPDGLATQIGEgargVSGGQAQRIALARAFLD 489
Cdd:COG0488 380 IGYFDQHQEELDpdKTVLDELRDGAPGGTEQEVRGYLGRFLFS------GDDAFKPVGV----LSGGEKARLALAKLLLS 449
|
170
....*....|....*....
gi 1834933330 490 DSrRVLLFDEPTAHLDIET 508
Cdd:COG0488 450 PP-NVLLLDEPTNHLDIET 467
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
335-558 |
1.32e-20 |
|
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: 91.21 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQtPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVY 414
Cdd:cd03295 1 IEFENVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLF-HASLRDNLAFyAP---GASEEAVMQAAAKA-GLTDwiatLPDglATQIGEGARGVSGGQAQRIALARAFLD 489
Cdd:cd03295 80 VIQQIGLFpHMTVEENIAL-VPkllKWPKEKIRERADELlALVG----LDP--AEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834933330 490 DSRrVLLFDEPTAHLDIETEVELKRAMLPVFD--HHLVFFATHRlhwMNEM----DYILVMDHGKIVQQGTPAEL 558
Cdd:cd03295 153 DPP-LLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHD---IDEAfrlaDRIAIMKNGEIVQVGTPDEI 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
335-562 |
1.41e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.56 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSY--GESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQR-- 410
Cdd:PRK10535 5 LELKDIRRSYpsGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 411 --SFVYIPQAPYLF-HASLRDNL---AFYApgASEEAVMQAAAKAGLTDWiatlpdGLATQIGEGARGVSGGQAQRIALA 484
Cdd:PRK10535 85 reHFGFIFQRYHLLsHLTAAQNVevpAVYA--GLERKQRLLRAQELLQRL------GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 485 RAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDH-HLVFFATHRLHWMNEMDYILVMDHGKIVQQgTPAELEQQG 562
Cdd:PRK10535 157 RALMNGG-QVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIVRN-PPAQEKVNV 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
341-557 |
1.54e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 91.33 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLdkQAWQRSFV--YIPQa 418
Cdd:COG4559 6 NLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAW--SPWELARRraVLPQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 419 pylfHASLrdNLAFYA--------------PGASEEAVMQAAAKAGLtdwiatlpDGLATQIgegARGVSGGQAQRIALA 484
Cdd:COG4559 83 ----HSSL--AFPFTVeevvalgraphgssAAQDRQIVREALALVGL--------AHLAGRS---YQTLSGGEQQRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 485 RAFL------DDSRRVLLFDEPTAHLDI-------ETEVELKRAMLPVF----DHHLV-FFAthrlhwmnemDYILVMDH 546
Cdd:COG4559 146 RVLAqlwepvDGGPRWLFLDEPTSALDLahqhavlRLARQLARRGGGVVavlhDLNLAaQYA----------DRILLLHQ 215
|
250
....*....|.
gi 1834933330 547 GKIVQQGTPAE 557
Cdd:COG4559 216 GRLVAQGTPEE 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
352-572 |
1.77e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.79 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAP--YLFHASLRDN 429
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 430 LAFyAP---GASEEAVMQAAAKA----GLTDWIATLPDGLatqigegargvSGGQAQRIALArAFLDDSRRVLLFDEPTA 502
Cdd:PRK13652 100 IAF-GPinlGLDEETVAHRVSSAlhmlGLEELRDRVPHHL-----------SGGEKKRVAIA-GVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 503 HLDIETEVELKRAM--LPVFDHHLVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAELEQQGGTYVRLRSEM 572
Cdd:PRK13652 167 GLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLDL 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
339-549 |
2.18e-20 |
|
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: 89.77 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 339 KVNVSYGeSQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQA---WQRSFVYI 415
Cdd:cd03292 5 NVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 416 PQ-APYLFHASLRDNLAF-----YAPGAS-EEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAFL 488
Cdd:cd03292 84 FQdFRLLPDRNVYENVAFalevtGVPPREiRKRVPAALELVGLSHKHRALPAEL-----------SGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 489 DDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDHHL-VFFATHRLHWMNEMDY-ILVMDHGKI 549
Cdd:cd03292 153 NSP-TILIADEPTGNLDPDTTWEIMNLLKKINKAGTtVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
332-561 |
2.85e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.48 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 332 DDTLALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQawQRS 411
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAPYLF-HASLRDNLAF--YAPGASEEAVMQAAAKA-GLTDwIATLPDGLATQIgegargvSGGQAQRIALARAf 487
Cdd:PRK11432 80 ICMVFQSYALFpHMSLGENVGYglKMLGVPKEERKQRVKEAlELVD-LAGFEDRYVDQI-------SGGQQQRVALARA- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 488 LDDSRRVLLFDEPTAHLDieteVELKRAM---------------LPVFDHHLVFFATHrlhwmnemDYILVMDHGKIVQQ 552
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLD----ANLRRSMrekirelqqqfnitsLYVTHDQSEAFAVS--------DTVIVMNKGKIMQI 218
|
....*....
gi 1834933330 553 GTPAELEQQ 561
Cdd:PRK11432 219 GSPQELYRQ 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
18-287 |
3.02e-20 |
|
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: 90.78 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 18 IMAVLTFVQAFMIIFQAKYLSVAIVNLWQLKSVRT--IVLPLLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMA 95
Cdd:pfam00664 3 LAILLAILSGAISPAFPLVLGRILDVLLPDGDPETqaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 96 KLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLTPWIVLIYIAFIQWKEALFLLAIYPLIIFFMIILG 175
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 176 LAAQAKADRQYAGYQRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTLSIAII 255
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALA 242
|
250 260 270
....*....|....*....|....*....|..
gi 1834933330 256 AVFLGFGLMNNTIQLLPALIILTLAPDYFAPI 287
Cdd:pfam00664 243 LWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
349-561 |
3.40e-20 |
|
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: 91.07 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 349 TPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQInvrdtavphldKQAWQRSFVyiPQAPYLFHASLRD 428
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGRISFS--SQFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 429 NLAFyapGAS-EEAVMQAAAKA-GLTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSRRVLLfDEPTAHLDI 506
Cdd:cd03291 117 NIIF---GVSyDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL-DSPFGYLDV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1834933330 507 ETEVEL-KRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQ 561
Cdd:cd03291 193 FTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
337-508 |
3.60e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAvphldkqawqrSFVYIP 416
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QAPYLF-HASLRDNL---------------AFYAPGASEEAVMQAAAK-----AGLTDW-----IATLPDGLATQIGEGA 470
Cdd:COG0488 68 QEPPLDdDLTVLDTVldgdaelraleaeleELEAKLAEPDEDLERLAElqeefEALGGWeaearAEEILSGLGFPEEDLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1834933330 471 RGV---SGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIET 508
Cdd:COG0488 148 RPVselSGGWRRRVALARALLSEP-DLLLLDEPTNHLDLES 187
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
334-530 |
3.92e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.31 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSY--GESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAV--PHLDkqawq 409
Cdd:COG4525 3 MLTVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgPGAD----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 410 RSFVYIPQA--PYLfhaSLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRI 481
Cdd:COG4525 78 RGVVFQKDAllPWL---NVLDNVAFglrlrgVPKAERRARAEELLALVGLADFARRRIWQL-----------SGGMRQRV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 482 ALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFD--HHLVFFATH 530
Cdd:COG4525 144 GIARALAADP-RFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITH 193
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
215-565 |
5.76e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 94.71 E-value: 5.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 215 YADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTLSIAIIAVFLG-FGLMNNTIQL---LPALIILTLAPDYFAPIRNF 290
Cdd:PTZ00265 1043 YFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGsFLIRRGTILVddfMKSLFTFLFTGSYAGKLMSL 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 291 ANDyhaTLNGKNTLTAVLDILQRPTPTD-RDLLPVR-QPTWQADDTLALNKVNVSY-GESQTPTLKDITFSVHGFQKVGI 367
Cdd:PTZ00265 1123 KGD---SENAKLSFEKYYPLIIRKSNIDvRDNGGIRiKNKNDIKGKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAI 1199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 368 IGASGSGKSTLINTLGGF------------------------------------------------------LSPQDGQI 393
Cdd:PTZ00265 1200 VGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKI 1279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 394 NVRDTAVPHLDKQAWQRSFVYIPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGV 473
Cdd:PTZ00265 1280 LLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSL 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 474 SGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDH--HLVFFATHRLHWMNEMDYILVMDH----G 547
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREP-KILLLDEATSSLDSNSEKLIEKTIVDIKDKadKTIITIAHRIASIKRSDKIVVFNNpdrtG 1438
|
410 420
....*....|....*....|
gi 1834933330 548 KIVQ-QGTPAE-LEQQGGTY 565
Cdd:PTZ00265 1439 SFVQaHGTHEElLSVQDGVY 1458
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
334-571 |
6.64e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.47 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKqawqRSFV 413
Cdd:COG4152 1 MLELKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR----RRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YIP-------------QAPYLfhASLRdnlafyapGASEeavmqAAAKAGLTDWIATLpdGLATQIGEGARGVSGGQAQR 480
Cdd:COG4152 75 YLPeerglypkmkvgeQLVYL--ARLK--------GLSK-----AEAKRRADEWLERL--GLGDRANKKVEELSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 481 IALARAFLDDSrRVLLFDEPTAHLD------IETEV-ELKRAMLPvfdhhlVFFATHRLHWMNEM-DYILVMDHGKIVQQ 552
Cdd:COG4152 138 VQLIAALLHDP-ELLILDEPFSGLDpvnvelLKDVIrELAAKGTT------VIFSSHQMELVEELcDRIVIINKGRKVLS 210
|
250 260
....*....|....*....|
gi 1834933330 553 GTPAEL-EQQGGTYVRLRSE 571
Cdd:COG4152 211 GSVDEIrRQFGRNTLRLEAD 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
352-558 |
9.47e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.96 E-value: 9.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVR----DTAVPHLDKQAWQRS------FVYipQAPYL 421
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditiDTARSLSQQKGLIRQlrqhvgFVF--QNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 422 F-HASLRDNL---AFYAPGASEEAVMQAA----AKAGLTDWIATLPdglatqigegaRGVSGGQAQRIALARAfLDDSRR 493
Cdd:PRK11264 97 FpHRTVLENIiegPVIVKGEPKEEATARArellAKVGLAGKETSYP-----------RRLSGGQQQRVAIARA-LAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834933330 494 VLLFDEPTAHLDIET--EV--------ELKRAMLPVfdhhlvffaTHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:PRK11264 165 VILFDEPTSALDPELvgEVlntirqlaQEKRTMVIV---------THEMSFARDVaDRAIFMDQGRIVEQGPAKAL 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
334-560 |
1.27e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 85.45 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVR----DTAVPHLDKQ--A 407
Cdd:PRK11124 2 SIQLNGINCFYGAHQA--LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAgnhfDFSKTPSDKAirE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 408 WQRSFVYIPQAPYLF-HASLRDNLaFYAP----GASEEAVMQAA----AKAGLTDWIATLPDGLatqigegargvSGGQA 478
Cdd:PRK11124 80 LRRNVGMVFQQYNLWpHLTVQQNL-IEAPcrvlGLSKDQALARAekllERLRLKPYADRFPLHL-----------SGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 479 QRIALARAFLDDSRrVLLFDEPTAHLD--IETEV-----ELKR-AMLPVFDHHLVFF----ATHrlhwmnemdyILVMDH 546
Cdd:PRK11124 148 QRVAIARALMMEPQ-VLLFDEPTAALDpeITAQIvsiirELAEtGITQVIVTHEVEVarktASR----------VVYMEN 216
|
250
....*....|....
gi 1834933330 547 GKIVQQGTPAELEQ 560
Cdd:PRK11124 217 GHIVEQGDASCFTQ 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
334-558 |
1.38e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.97 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFV 413
Cdd:PRK09536 3 MIDVSDLSVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YIPQAPYL-FHASLRD--------NLAFYAPG--ASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIA 482
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQvvemgrtpHRSRFDTWteTDRAAVERAMERTGVAQFADRPVTSL-----------SGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 483 LARAfLDDSRRVLLFDEPTAHLDIETEV---ELKRAMlpVFDHHLVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:PRK09536 150 LARA-LAQATPVLLLDEPTASLDINHQVrtlELVRRL--VDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADV 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
334-560 |
1.79e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 85.06 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRD------TAVPHLDKQA 407
Cdd:COG4161 2 SIQLKNINCFYGSHQA--LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 408 WQRSFVYIPQAPYLF-HASLRDNLaFYAP----GASEEAVMQAAAKA----GLTDWIATLPDGLatqigegargvSGGQA 478
Cdd:COG4161 80 LRQKVGMVFQQYNLWpHLTVMENL-IEAPckvlGLSKEQAREKAMKLlarlRLTDKADRFPLHL-----------SGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 479 QRIALARAFLDDSRrVLLFDEPTAHLD--IETEV-----ELKR-AMLPVFDHHLVFFAThrlhwmNEMDYILVMDHGKIV 550
Cdd:COG4161 148 QRVAIARALMMEPQ-VLLFDEPTAALDpeITAQVveiirELSQtGITQVIVTHEVEFAR------KVASQVVYMEKGRII 220
|
250
....*....|
gi 1834933330 551 QQGTPAELEQ 560
Cdd:COG4161 221 EQGDASHFTQ 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
352-557 |
1.82e-18 |
|
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: 85.09 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLdkQAWQ-------RSFvyipQAPYLF-H 423
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGL--PPHRiarlgiaRTF----QNPRLFpE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 424 ASLRDNLA-----------------FYAPGASEEAVMQAAAkagltDWIATLpdGLATQIGEGARGVSGGQAQRIALARA 486
Cdd:COG0411 94 LTVLENVLvaaharlgrgllaallrLPRARREEREARERAE-----ELLERV--GLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 487 FLddSR-RVLLFDEPTAHLDI-ETE------VELKRAM-LPVF--DHH--LVffathrlhwMNEMDYILVMDHGKIVQQG 553
Cdd:COG0411 167 LA--TEpKLLLLDEPAAGLNPeETEelaeliRRLRDERgITILliEHDmdLV---------MGLADRIVVLDFGRVIAEG 235
|
....
gi 1834933330 554 TPAE 557
Cdd:COG0411 236 TPAE 239
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
362-553 |
1.93e-18 |
|
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: 84.27 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 362 FQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAV------PHLDKQawQRSFVYIPQAPYLF-HASLRDNLAFYA 434
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINLPPQ--QRKIGLVFQQYALFpHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 435 PGASEEAVMQAAAKagLTDWIATlpDGLATQigeGARGVSGGQAQRIALARAFLdDSRRVLLFDEPTAHLDIETEVELK- 513
Cdd:cd03297 101 KRKRNREDRISVDE--LLDLLGL--DHLLNR---YPAQLSGGEKQRVALARALA-AQPELLLLDEPFSALDRALRLQLLp 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1834933330 514 --RAMLPVFDHHlVFFATHRLHWMNEM-DYILVMDHGKIVQQG 553
Cdd:cd03297 173 elKQIKKNLNIP-VIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
336-557 |
2.00e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.21 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 336 ALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYI 415
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 416 PQAPylfhaslrdNLAF-----------YAPGAS-----EEAVMQAAAKAGLTdwiatlpdGLAtqiGEGARGVSGGQAQ 479
Cdd:PRK13548 82 PQHS---------SLSFpftveevvamgRAPHGLsraedDALVAAALAQVDLA--------HLA---GRDYPQLSGGEQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 480 RIALARAFL-----DDSRRVLLFDEPTAHLDI---ETEVELKRAmlpvfdhhlvfFATHR-------LHWMNEM----DY 540
Cdd:PRK13548 142 RVQLARVLAqlwepDGPPRWLLLDEPTSALDLahqHHVLRLARQ-----------LAHERglavivvLHDLNLAaryaDR 210
|
250
....*....|....*..
gi 1834933330 541 ILVMDHGKIVQQGTPAE 557
Cdd:PRK13548 211 IVLLHQGRLVADGTPAE 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
335-550 |
2.66e-18 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 82.09 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGesQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVphldkqawqrsfvy 414
Cdd:cd03216 1 LELRGITKRFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 ipqapylfhaslrdnlAFYAPgaseeavmQAAAKAGltdwIATLPdglatQIgegargvSGGQAQRIALARAFLDDSRrV 494
Cdd:cd03216 65 ----------------SFASP--------RDARRAG----IAMVY-----QL-------SVGERQMVEIARALARNAR-L 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834933330 495 LLFDEPTAHLDiETEVELkramlpVFDH--------HLVFFATHRLHWMNEM-DYILVMDHGKIV 550
Cdd:cd03216 104 LILDEPTAALT-PAEVER------LFKVirrlraqgVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
352-558 |
2.76e-18 |
|
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: 88.20 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGfLSPQDGQINVRDTAVPHLDKQAWQ--RSFVYIP-QAPYlfhASL-- 426
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALRplRRRMQVVfQDPF---GSLsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 427 --------RDNLAFYAPGAS----EEAVMQAAAKAGLTdwiatlPDGLATQIGEgargVSGGQAQRIALARAF-LDDsrR 493
Cdd:COG4172 378 rmtvgqiiAEGLRVHGPGLSaaerRARVAEALEEVGLD------PAARHRYPHE----FSGGQRQRIAIARALiLEP--K 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 494 VLLFDEPTAHLD--IETEV-----ELKRamlpvfDHHLVF-FATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:COG4172 446 LLVLDEPTSALDvsVQAQIldllrDLQR------EHGLAYlFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQV 513
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
349-560 |
4.66e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.45 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 349 TPTLKDITFSVHG------------FQKV-GIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYI 415
Cdd:PRK10575 11 TFALRNVSFRVPGrtllhplsltfpAGKVtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 416 PQA-PYLFHASLRDNLAF--Y----APG----ASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALA 484
Cdd:PRK10575 91 PQQlPAAEGMTVRELVAIgrYpwhgALGrfgaADREKVEEAISLVGLKPLAHRLVDSL-----------SGGERQRAWIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 485 RAFLDDSrRVLLFDEPTAHLDIETEVELkRAMLPVFDHHLVFFATHRLHWMNEM----DYILVMDHGKIVQQGTPAELEQ 560
Cdd:PRK10575 160 MLVAQDS-RCLLLDEPTSALDIAHQVDV-LALVHRLSQERGLTVIAVLHDINMAarycDYLVALRGGEMIAQGTPAELMR 237
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
341-558 |
5.02e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.50 E-value: 5.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGES-----QTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRD------TAVPHLDKQAWQ 409
Cdd:PRK13641 7 NVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpeTGNKNLKKLRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 410 RSFVY-IPQAPYLFHASLRDnlAFYAP---GASEEAVMQAAAKagltdWIATLpdGLATQIGEGAR-GVSGGQAQRIALA 484
Cdd:PRK13641 87 VSLVFqFPEAQLFENTVLKD--VEFGPknfGFSEDEAKEKALK-----WLKKV--GLSEDLISKSPfELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 485 rAFLDDSRRVLLFDEPTAHLDIETEVElkraMLPVFDH-----HLVFFATHRLHWMNE-MDYILVMDHGKIVQQGTPAEL 558
Cdd:PRK13641 158 -GVMAYEPEILCLDEPAAGLDPEGRKE----MMQLFKDyqkagHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
337-558 |
5.06e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 85.51 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGESQTPT--LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDK---QAWQRS 411
Cdd:COG1135 4 LENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelRAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAPYLFHA-SLRDNLAFyaP----GASEEavmQAAAKA-------GLTDWIATLPDGLatqigegargvSGGQAQ 479
Cdd:COG1135 84 IGMIFQHFNLLSSrTVAENVAL--PleiaGVPKA---EIRKRVaellelvGLSDKADAYPSQL-----------SGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 480 RIALARAfLDDSRRVLLFDEPTAHLDIETEVE----LKRAmlpvfDHHL---VFFATHrlhwmnEMDYI-------LVMD 545
Cdd:COG1135 148 RVGIARA-LANNPKVLLCDEATSALDPETTRSildlLKDI-----NRELgltIVLITH------EMDVVrricdrvAVLE 215
|
250
....*....|...
gi 1834933330 546 HGKIVQQGTPAEL 558
Cdd:COG1135 216 NGRIVEQGPVLDV 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
355-516 |
7.26e-18 |
|
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: 82.16 E-value: 7.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 355 ITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVpHLDKQAWQRSFVYIPQAPYLFHA-SLRDNLAFY 433
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTlSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 434 APGASEEAVMQAAAKAGLTdwiaTLPDGLATQIgegargvSGGQAQRIALARAFLdDSRRVLLFDEPTAHLDIETEVELK 513
Cdd:cd03231 98 HADHSDEQVEEALARVGLN----GFEDRPVAQL-------SAGQQRRVALARLLL-SGRPLWILDEPTTALDKAGVARFA 165
|
...
gi 1834933330 514 RAM 516
Cdd:cd03231 166 EAM 168
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
337-557 |
7.69e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 85.38 E-value: 7.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYip 416
Cdd:PRK09452 17 LRGISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVF-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QAPYLF-HASLRDNLAF-----YAPGAS-EEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAFLD 489
Cdd:PRK09452 93 QSYALFpHMTVFENVAFglrmqKTPAAEiTPRVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834933330 490 DSrRVLLFDEPTAHLDI----ETEVELK---RAMLPVFdhhlvFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAE 557
Cdd:PRK09452 162 KP-KVLLLDESLSALDYklrkQMQNELKalqRKLGITF-----VFVTHDQEEALTMsDRIVVMRDGRIEQDGTPRE 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
335-508 |
1.43e-17 |
|
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: 82.10 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTPT--LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQR-- 410
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 411 ----SFVYipQApylFH--ASL--RDNLAFYAPGASEEAVMQAAAKA----GLTDWIATLPDGLatqigegargvSGGQA 478
Cdd:COG4181 89 arhvGFVF--QS---FQllPTLtaLENVMLPLELAGRRDARARARALlervGLGHRLDHYPAQL-----------SGGEQ 152
|
170 180 190
....*....|....*....|....*....|.
gi 1834933330 479 QRIALARAFLddSRRVLLF-DEPTAHLDIET 508
Cdd:COG4181 153 QRVALARAFA--TEPAILFaDEPTGNLDAAT 181
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
352-553 |
2.50e-17 |
|
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: 80.87 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHlDKQAWQRSFVYIPQAPYLF-HASLRDNL 430
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYdRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 431 AFYapgASEEAVMQAAAKAGLTDWIATLpdGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETev 510
Cdd:cd03266 100 EYF---AGLYGLKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDP-PVLLLDEPTTGLDVMA-- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1834933330 511 elKRAMLPVFDH-----HLVFFATHRLHWMNEM-DYILVMDHGKIVQQG 553
Cdd:cd03266 172 --TRALREFIRQlralgKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
366-558 |
2.52e-17 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 81.78 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 366 GIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQ-APYLFHASLRDNLAF----------YA 434
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVEQdSDTAVPLTVRDVVALgriphrslwaGD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 435 PGASEEAVMQAAAKAGLTDwiatlpdgLATQigeGARGVSGGQAQRIALARAFLDDSRrVLLFDEPTAHLDIETEVELKR 514
Cdd:TIGR03873 111 SPHDAAVVDRALARTELSH--------LADR---DMSTLSGGERQRVHVARALAQEPK-LLLLDEPTNHLDVRAQLETLA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1834933330 515 AMLPVFDHHL-VFFATHRL-HWMNEMDYILVMDHGKIVQQGTPAEL 558
Cdd:TIGR03873 179 LVRELAATGVtVVAALHDLnLAASYCDHVVVLDGGRVVAAGPPREV 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
335-561 |
3.27e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.47 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYgESQTP----TLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQA--- 407
Cdd:PRK13643 2 IKFEKVNYTY-QPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 408 -WQRSFVYIPQAP--YLFHASLRDNLAFYAPG---ASEEAVMQAAAKAGLTdwiatlpdGLATQIGEGAR-GVSGGQAQR 480
Cdd:PRK13643 81 pVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgiPKEKAEKIAAEKLEMV--------GLADEFWEKSPfELSGGQMRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 481 IALArAFLDDSRRVLLFDEPTAHLDIETEVELKRAMLPVFDH-HLVFFATHRLHWMNE-MDYILVMDHGKIVQQGTPAEL 558
Cdd:PRK13643 153 VAIA-GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDV 231
|
...
gi 1834933330 559 EQQ 561
Cdd:PRK13643 232 FQE 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
335-505 |
3.35e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.91 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGEsqTPTLKDITFSV-HGFQKVgIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFV 413
Cdd:PRK10247 8 LQLQNVGYLAGD--AKILNNISFSLrAGEFKL-ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YIPQAPYLFHASLRDNLAF------YAPgaSEEAVMQAAAKAGLTDWIatlpdgLATQIGEgargVSGGQAQRIALAR-- 485
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFpwqirnQQP--DPAIFLDDLERFALPDTI------LTKNIAE----LSGGEKQRISLIRnl 152
|
170 180
....*....|....*....|
gi 1834933330 486 AFLDdsrRVLLFDEPTAHLD 505
Cdd:PRK10247 153 QFMP---KVLLLDEITSALD 169
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
332-558 |
4.18e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.77 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 332 DDTLALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQD---GQINVRDTAVPhlDKQAW 408
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLT--AKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 409 Q-RSFVYIP-QAP--YLFHASLRDNLAFyapGASEEA---------VMQAAAKAGLTDWIATLPDGLatqigegargvSG 475
Cdd:PRK13640 81 DiREKVGIVfQNPdnQFVGATVGDDVAF---GLENRAvprpemikiVRDVLADVGMLDYIDSEPANL-----------SG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 476 GQAQRIALArAFLDDSRRVLLFDEPTAHLDIETEVE-LKRAMLPVFDHHL-VFFATHRLHWMNEMDYILVMDHGKIVQQG 553
Cdd:PRK13640 147 GQKQRVAIA-GILAVEPKIIILDESTSMLDPAGKEQiLKLIRKLKKKNNLtVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
....*
gi 1834933330 554 TPAEL 558
Cdd:PRK13640 226 SPVEI 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
352-558 |
4.93e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.37 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAP-----------Y 420
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnprqrisQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 421 LFHASLRDNLAFYAPgASEEAVMQAAAKAGL-TDWIATLPDGLATqigegargvsgGQAQRIALARAFLDDSrRVLLFDE 499
Cdd:PRK15112 109 ILDFPLRLNTDLEPE-QREKQIIETLRQVGLlPDHASYYPHMLAP-----------GQKQRLGLARALILRP-KVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834933330 500 PTAHLDIETEVELKRAMLPVFDHHLV--FFATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADV 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
335-553 |
1.49e-16 |
|
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: 78.77 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTptLKDITFSV-HGFqkVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHlDKQAWQRSFV 413
Cdd:cd03264 1 LQLENLTKRYGKKRA--LDGVSLTLgPGM--YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YIPQAPYLF-HASLRDNLAFYA------PGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARA 486
Cdd:cd03264 76 YLPQEFGVYpNFTVREFLDYIAwlkgipSKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 487 FLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEM-DYILVMDHGKIVQQG 553
Cdd:cd03264 145 LVGDP-SILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
354-558 |
1.55e-16 |
|
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: 80.87 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 354 DITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQ---DGQINVRDTAVPHLDKQAWQ----RSFVYIPQAPYlfhASL 426
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRkirgREIQMIFQDPM---TSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 427 ------RDNLA---FYAPGASEEAVMQAAAKA----GLTDWIATL---PDGLatqigegargvSGGQAQRIALARAFLDD 490
Cdd:COG0444 100 npvmtvGDQIAeplRIHGGLSKAEARERAIELlervGLPDPERRLdryPHEL-----------SGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 491 SrRVLLFDEPTAHLD--IETEV-----ELKR----AMLpvfdhhlvfFATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:COG0444 169 P-KLLIADEPTTALDvtIQAQIlnllkDLQRelglAIL---------FITHDLGVVAEIaDRVAVMYAGRIVEEGPVEEL 238
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
352-530 |
1.64e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDkqawqrsfvYIPQAPYLFHA------- 424
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---------VAEACHYLGHRnamkpal 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 425 SLRDNLAFYAP--GASEEAVMQAAAKAGLTDwIATLPdglatqigegARGVSGGQAQRIALARaFLDDSRRVLLFDEPTA 502
Cdd:PRK13539 89 TVAENLEFWAAflGGEELDIAAALEAVGLAP-LAHLP----------FGYLSAGQKRRVALAR-LLVSNRPIWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|...
gi 1834933330 503 HLDIETEVELKRAMLpvfdHHL-----VFFATH 530
Cdd:PRK13539 157 ALDAAAVALFAELIR----AHLaqggiVIAATH 185
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
335-553 |
1.94e-16 |
|
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: 78.03 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLdKQAWQRSFVY 414
Cdd:cd03268 1 LKTNDLTKTYGKKRV--LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IpQAPYLF-HASLRDNLAFYA--PGASEEAVMQAaakagltdwIATLpdGLATQIGEGARGVSGGQAQRIALARAFLDDS 491
Cdd:cd03268 78 I-EAPGFYpNLTARENLRLLArlLGIRKKRIDEV---------LDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 492 rRVLLFDEPTAHLDIETEVELKRAMLPVFDH-HLVFFATHRLHWMNEM-DYILVMDHGKIVQQG 553
Cdd:cd03268 146 -DLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
57-560 |
1.98e-16 |
|
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: 82.54 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 57 LLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVL 136
Cdd:COG4615 51 LLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 137 DLSLTpWIVLIYIAFIQWKeaLFLLAIypLIIFFMIILGLAAQAKADRQYA----GYQRLSNHFVDTLRGLptlKQLGLN 212
Cdd:COG4615 131 SVALV-LGCLAYLAWLSPP--LFLLTL--VLLGLGVAGYRLLVRRARRHLRrareAEDRLFKHFRALLEGF---KELKLN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 213 K----TYADNVYQVS----EDYRKKTMSTLTIAMTSTFALdFFTTLSiAIIAVFLGFGLMNNTIQLLPALIILTLApdyf 284
Cdd:COG4615 203 RrrrrAFFDEDLQPTaeryRDLRIRADTIFALANNWGNLL-FFALIG-LILFLLPALGWADPAVLSGFVLVLLFLR---- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 285 APIRNFANDYHATLNGKNTLTAVLDILQRPTPTDRDLLPVRQPTWQAD-DTLALNKVNVSYGESQTP---TLKDITFSVH 360
Cdd:COG4615 277 GPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGDegfTLGPIDLTIR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 361 GFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPYLFhaslrDNLAFYAPGASEE 440
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DRLLGLDGEADPA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 441 AVmqaaakaglTDWIATLpdGLA--TQIGEGA---RGVSGGQAQRIALARAFLDDsRRVLLFDEPTAHLDIE------TE 509
Cdd:COG4615 432 RA---------RELLERL--ELDhkVSVEDGRfstTDLSQGQRKRLALLVALLED-RPILVFDEWAADQDPEfrrvfyTE 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 510 V--ELKRAmlpvfdHHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQ 560
Cdd:COG4615 500 LlpELKAR------GKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAALAA 546
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
337-568 |
2.41e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.39 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGESQT-PTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPhlDKQAW--QRSFV 413
Cdd:PRK13650 7 VKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT--EENVWdiRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YIPQAP--YLFHASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWiatlpdglatQIGEGARgVSGGQAQRIALAR 485
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFglenkgIPHEEMKERVNEALELVGMQDF----------KEREPAR-LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 486 AFlddSRR--VLLFDEPTAHLDIETEVELKRAMLPVFDHH--LVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAELEQQ 561
Cdd:PRK13650 154 AV---AMRpkIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
....*..
gi 1834933330 562 GGTYVRL 568
Cdd:PRK13650 231 GNDLLQL 237
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
345-554 |
2.78e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.32 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 345 GESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQA----WQRSFVYIpqapY 420
Cdd:PRK11629 18 GSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaelRNQKLGFI----Y 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 421 LFHASLRD-----NLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAFLD 489
Cdd:PRK11629 94 QFHHLLPDftaleNVAMplligkKKPAEINSRALEMLAAVGLEHRANHRPSEL-----------SGGERQRVAIARALVN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834933330 490 DSRRVLLfDEPTAHLDIETE-------VELKRAMLPVFdhhLVffATHRLHWMNEMDYILVMDHGKIVQQGT 554
Cdd:PRK11629 163 NPRLVLA-DEPTGNLDARNAdsifqllGELNRLQGTAF---LV--VTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
356-505 |
3.17e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.09 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 356 TFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDtaVPHLDKQAWQRSFVYIPQAPYLF-HASLRDNLAF-Y 433
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG--QDHTTTPPSRRPVSMLFQENNLFsHLTVAQNIGLgL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834933330 434 APG-----ASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAFLdDSRRVLLFDEPTAHLD 505
Cdd:PRK10771 97 NPGlklnaAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLV-REQPILLLDEPFSALD 161
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
335-508 |
5.81e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 74.79 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESqtPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAvphldkqawqrSFVY 414
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQapylfhaslrdnlafyapgaseeavmqaaakagltdwiatlpdglatqigegargVSGGQAQRIALARAFLDDSrRV 494
Cdd:cd03221 68 FEQ-------------------------------------------------------LSGGEKMRLALAKLLLENP-NL 91
|
170
....*....|....
gi 1834933330 495 LLFDEPTAHLDIET 508
Cdd:cd03221 92 LLLDEPTNHLDLES 105
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
352-553 |
6.69e-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: 6.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQD---GQINVRDTAvphLDKQAWQRSFVYIPQ----APYLfha 424
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQP---RKPDQFQKCVAYVRQddilLPGL--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 425 SLRDNLAFYAPGASEEAVMQAAAKAglTDWIATLPDGLATQIG-EGARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAH 503
Cdd:cd03234 97 TVRETLTYTAILRLPRKSSDAIRKK--RVEDVLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDP-KVLILDEPTSG 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 504 LD-------IETEVELKRA--------------MLPVFDHhlvffathrlhwmnemdyILVMDHGKIVQQG 553
Cdd:cd03234 174 LDsftalnlVSTLSQLARRnriviltihqprsdLFRLFDR------------------ILLLSSGEIVYSG 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
341-558 |
7.68e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 7.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLD-KQAWQRSFVYIPQAP 419
Cdd:PRK15439 16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 420 YLF-HASLRDNLAFYAPGaseeavmQAAAKAGLTDWIATLPDGLATQIGEGARGVSGGQAQRIalARAFLDDSrRVLLFD 498
Cdd:PRK15439 96 LLFpNLSVKENILFGLPK-------RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEI--LRGLMRDS-RILILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 499 EPTAHLD-IETEVELKRA-MLPVFDHHLVFFaTHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:PRK15439 166 EPTASLTpAETERLFSRIrELLAQGVGIVFI-SHKLPEIRQLaDRISVMRDGTIALSGKTADL 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
335-549 |
9.03e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.41 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVphldKQAWQRSFVY 414
Cdd:PRK11247 13 LLLNAVSKRYGERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL----AEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGL----TDWIATLpdglatqigegargvSGGQAQRIALARAfLDD 490
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLadraNEWPAAL---------------SGGQKQRVALARA-LIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834933330 491 SRRVLLFDEPTAHLDIETEVELKRAMLPVFDHH--LVFFATHRLHWMNEM-DYILVMDHGKI 549
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
332-558 |
9.07e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.48 E-value: 9.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 332 DDTLALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRS 411
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAP----------YLFHASLRDNLAFYApgASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRI 481
Cdd:PRK13648 85 IGIVFQNPdnqfvgsivkYDVAFGLENHAVPYD--EMHRRVSEALKQVDMLERADYEPNAL-----------SGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 482 ALArAFLDDSRRVLLFDEPTAHLDIETEVELKRAMLPV-FDHHLVFFA-THRLHWMNEMDYILVMDHGKIVQQGTPAEL 558
Cdd:PRK13648 152 AIA-GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISiTHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
335-557 |
1.01e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.19 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSygesqtPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGfLSPQDGQINVRDTAVPHLDKQAWQRSFVY 414
Cdd:COG4138 1 LQLNDVAVA------GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAELARHRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQ---APYL---FHAslrdnLAFYAPG-----ASEEAVMQAAAKAGLTDWiatlpdgLATQIGEgargVSGGQAQRIAL 483
Cdd:COG4138 74 LSQqqsPPFAmpvFQY-----LALHQPAgasseAVEQLLAQLAEALGLEDK-------LSRPLTQ----LSGGEWQRVRL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 484 ARAFL------DDSRRVLLFDEPTAHLDIETEV-------ELKRAMLPVF--DHHLvffaTHRLHwmnEMDYILVMDHGK 548
Cdd:COG4138 138 AAVLLqvwptiNPEGQLLLLDEPMNSLDVAQQAaldrllrELCQQGITVVmsSHDL----NHTLR---HADRVWLLKQGK 210
|
....*....
gi 1834933330 549 IVQQGTPAE 557
Cdd:COG4138 211 LVASGETAE 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
341-561 |
1.41e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.44 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYG------ESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVR--DTAvphLDKQAWQ-RS 411
Cdd:PRK13633 9 NVSYKyesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDglDTS---DEENLWDiRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 ---FVYipQAP--YLFHASLRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQR 480
Cdd:PRK13633 86 kagMVF--QNPdnQIVATIVEEDVAFgpenlgIPPEEIRERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 481 IALArAFLDDSRRVLLFDEPTAHLD-------IETEVELKRAmlpvfDHHLVFFATHRLHWMNEMDYILVMDHGKIVQQG 553
Cdd:PRK13633 153 VAIA-GILAMRPECIIFDEPTAMLDpsgrrevVNTIKELNKK-----YGITIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
....*...
gi 1834933330 554 TPAELEQQ 561
Cdd:PRK13633 227 TPKEIFKE 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-558 |
1.42e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.61 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGF--LSPQ---DGQINVRDTAV--PHLDKQA 407
Cdd:COG1117 12 IEVRNLNVYYGDKQA--LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 408 WQRSFVYIPQAPYLFHASLRDNLAfYAP--------GASEEAVMQAAAKAGLtdWiatlpDGLATQIGEGARGVSGGQAQ 479
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNVA-YGLrlhgikskSELDEIVEESLRKAAL--W-----DEVKDRLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 480 RIALARAfLDDSRRVLLFDEPTAHLD-IETE------VELKramlpvfDHHLVFFATHRlhwmneM-------DYILVMD 545
Cdd:COG1117 162 RLCIARA-LAVEPEVLLMDEPTSALDpISTAkieeliLELK-------KDYTIVIVTHN------MqqaarvsDYTAFFY 227
|
250
....*....|...
gi 1834933330 546 HGKIVQQGTPAEL 558
Cdd:COG1117 228 LGELVEFGPTEQI 240
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
320-575 |
1.60e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.34 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 320 DLLPVRQPTWQADDTLALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTA 399
Cdd:PRK11607 3 DAIPRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 400 VPHLdkQAWQRSFVYIPQAPYLF-HASLRDNLAFyapGASEEAVmqaaAKAGLTDWIATLPDGLATQ--IGEGARGVSGG 476
Cdd:PRK11607 83 LSHV--PPYQRPINMMFQSYALFpHMTVEQNIAF---GLKQDKL----PKAEIASRVNEMLGLVHMQefAKRKPHQLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 477 QAQRIALARAfLDDSRRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLV--FFATH-RLHWMNEMDYILVMDHGKIVQQG 553
Cdd:PRK11607 154 QRQRVALARS-LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVtcVMVTHdQEEAMTMAGRIAIMNRGKFVQIG 232
|
250 260
....*....|....*....|..
gi 1834933330 554 TPAELEQQGGTyvRLRSEMEGA 575
Cdd:PRK11607 233 EPEEIYEHPTT--RYSAEFIGS 252
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
331-560 |
2.01e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.85 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 331 ADDTLALNKVNVSYGESQTpTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVphldKQAWQR 410
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT----RQALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 411 SFV-YIPQApylfhaslrDNLAFYAPGASEEAVMQaaAKAGLTDWI--------ATLPDGLA---------TQIGEgarg 472
Cdd:PRK15056 78 NLVaYVPQS---------EEVDWSFPVLVEDVVMM--GRYGHMGWLrrakkrdrQIVTAALArvdmvefrhRQIGE---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 473 VSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDH-HLVFFATHRLHWMNEM-DYIlVMDHGKIV 550
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQG-QVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFcDYT-VMVKGTVL 220
|
250
....*....|....*.
gi 1834933330 551 QQG------TPAELEQ 560
Cdd:PRK15056 221 ASGptettfTAENLEL 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
352-558 |
2.14e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 76.98 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSF------VYipQAP--YLFH 423
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLrkkvgiVF--QFPehQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 424 ASLRDNLAFyAP---GASEEAVMQAAAKA----GLTdwiatlPDGLATQIGEgargVSGGQAQRIALArAFLDDSRRVLL 496
Cdd:PRK13634 101 ETVEKDICF-GPmnfGVSEEDAKQKAREMielvGLP------EELLARSPFE----LSGGQMRRVAIA-GVLAMEPEVLV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834933330 497 FDEPTAHLDIETEVELKRamlpvfdhhlVFFATHR---------LHWMNEM----DYILVMDHGKIVQQGTPAEL 558
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMME----------MFYKLHKekglttvlvTHSMEDAaryaDQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
343-558 |
2.30e-15 |
|
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: 75.48 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 343 SYGesQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHlDKQAWQRSFVYIPQAPylf 422
Cdd:cd03265 9 KYG--DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDL--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 423 haSLRDNLAFYapgasEEAVMQAA----AKAGLTDWIATLPDGLAtqIGEGA----RGVSGGQAQRIALARAFLdDSRRV 494
Cdd:cd03265 83 --SVDDELTGW-----ENLYIHARlygvPGAERRERIDELLDFVG--LLEAAdrlvKTYSGGMRRRLEIARSLV-HRPEV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 495 LLFDEPTAHLDIETEV---ELKRAMLPVFDhHLVFFAThrlHWMNEM----DYILVMDHGKIVQQGTPAEL 558
Cdd:cd03265 153 LFLDEPTIGLDPQTRAhvwEYIEKLKEEFG-MTILLTT---HYMEEAeqlcDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
335-553 |
2.87e-15 |
|
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: 75.01 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAwqrsFVY 414
Cdd:cd03269 1 LEVENVTKRFGRVTA--LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR----IGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLF-HASLRDNLAFYapgASEEAVMQAAAKAGLTDWIATLpdGLATQIGEGARGVSGGQAQRIALARAFLDDSrR 493
Cdd:cd03269 75 LPEERGLYpKMKVIDQLVYL---AQLKGLKKEEARRRIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDP-E 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 494 VLLFDEPTAHLD------IETEV-ELKRAMLPvfdhhlVFFATHRLHWMNEM-DYILVMDHGKIVQQG 553
Cdd:cd03269 149 LLILDEPFSGLDpvnvelLKDVIrELARAGKT------VILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
335-567 |
3.04e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.77 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGesqtptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQ----- 409
Cdd:PRK10070 33 QILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 410 ------RSFVYIPQAPYLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIAL 483
Cdd:PRK10070 107 kiamvfQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 484 ARAfLDDSRRVLLFDEPTAHLD--IETEVELKRAMLPVFDHHLVFFATHRL-HWMNEMDYILVMDHGKIVQQGTPAE-LE 559
Cdd:PRK10070 176 ARA-LAINPDILLMDEAFSALDplIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEiLN 254
|
....*...
gi 1834933330 560 QQGGTYVR 567
Cdd:PRK10070 255 NPANDYVR 262
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
352-557 |
6.69e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.47 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQI-----NVRDTAV--PHLDKQAwqrSFVYipQAP--YLF 422
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvDITDKKVklSDIRKKV---GLVF--QYPeyQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 423 HASLRDNLAFyAP---GASEEA----VMQAAAKAGLTdwIATLPDGLATQIgegargvSGGQAQRIALArAFLDDSRRVL 495
Cdd:PRK13637 98 EETIEKDIAF-GPinlGLSEEEienrVKRAMNIVGLD--YEDYKDKSPFEL-------SGGQKRRVAIA-GVVAMEPKIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 496 LFDEPTAHLDIETEVELkraMLPVFDHHLVFFATHRL--HWMNEM----DYILVMDHGKIVQQGTPAE 557
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEI---LNKIKELHKEYNMTIILvsHSMEDVaklaDRIIVMNKGKCELQGTPRE 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
350-558 |
7.58e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 74.84 E-value: 7.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 350 PTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLD---KQAWQRSFVYIPQ-APYLFHA- 424
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQdSPSAVNPr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 425 -----SLRDNLAFYApgaSEEAVMQAAAKAGLTDWIAtLPDGLATQIgegARGVSGGQAQRIALARAfLDDSRRVLLFDE 499
Cdd:TIGR02769 105 mtvrqIIGEPLRHLT---SLDESEQKARIAELLDMVG-LRSEDADKL---PRQLSGGQLQRINIARA-LAVKPKLIVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 500 PTAHLDIETE---VELKRAMLPVFDHHLVFFaTHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:TIGR02769 177 AVSNLDMVLQaviLELLRKLQQAFGTAYLFI-THDLRLVQSFcQRVAVMDKGQIVEECDVAQL 238
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
343-558 |
9.08e-15 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 74.45 E-value: 9.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 343 SYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTL---INtlggFLS-PQDGQINV-----------RDTAVPHLDKQA 407
Cdd:COG4598 17 SFGDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFlrcIN----LLEtPDSGEIRVggeeirlkpdrDGELVPADRRQL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 408 wQR-----SFVYipQAPYLF-HASLRDNLAFyAP----GAS-EEAVMQAAA---KAGLTDWIATLPDGLatqigegargv 473
Cdd:COG4598 91 -QRirtrlGMVF--QSFNLWsHMTVLENVIE-APvhvlGRPkAEAIERAEAllaKVGLADKRDAYPAHL----------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 474 SGGQAQRIALARAfLDDSRRVLLFDEPTAHLDIE--TEVeLK---------RAMLPVfdhhlvffaTHrlhwmnEMDY-- 540
Cdd:COG4598 156 SGGQQQRAAIARA-LAMEPEVMLFDEPTSALDPElvGEV-LKvmrdlaeegRTMLVV---------TH------EMGFar 218
|
250 260
....*....|....*....|...
gi 1834933330 541 -----ILVMDHGKIVQQGTPAEL 558
Cdd:COG4598 219 dvsshVVFLHQGRIEEQGPPAEV 241
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
350-526 |
9.87e-15 |
|
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: 73.62 E-value: 9.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 350 PTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRD--------TAVPHLDKQAWQRSFVY------- 414
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwvdlaQASPREILALRRRTIGYvsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYLFHA--SLRDNlafyapGASEEAvmqAAAKAGltDWIATL--PDGL-----ATqigegargVSGGQAQRIALAR 485
Cdd:COG4778 105 IPRVSALDVVaePLLER------GVDREE---ARARAR--ELLARLnlPERLwdlppAT--------FSGGEQQRVNIAR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 486 AFLDDsRRVLLFDEPTAHLD-------IETEVELKR---AMLPVFdHHLVF 526
Cdd:COG4778 166 GFIAD-PPLLLLDEPTASLDaanravvVELIEEAKArgtAIIGIF-HDEEV 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
335-558 |
1.59e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.85 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVS-----YGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVpHLDKQAWQ 409
Cdd:PRK10619 1 MSENKLNVIdlhkrYGEHEV--LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI-NLVRDKDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 410 RSFVYIPQAPYLFHASLR---DNLAFYAPGASEEAVMQAAAKA-GLTDWIATLPDGL---ATQIGEGARG-----VSGGQ 477
Cdd:PRK10619 78 QLKVADKNQLRLLRTRLTmvfQHFNLWSHMTVLENVMEAPIQVlGLSKQEARERAVKylaKVGIDERAQGkypvhLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 478 AQRIALARAfLDDSRRVLLFDEPTAHLDIETEVELKRAMLPVFDH-HLVFFATHRLHWMNEM-DYILVMDHGKIVQQGTP 555
Cdd:PRK10619 158 QQRVSIARA-LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAP 236
|
...
gi 1834933330 556 AEL 558
Cdd:PRK10619 237 EQL 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
352-558 |
1.95e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.83 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLD-KQAWQRSFVYIPQ----APYLfhaSL 426
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQelnlVPNL---SV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 427 RDNLAFyapgaseeavMQAAAKAGLTDWIAT------------LPDGLATQIGEgargVSGGQAQRIALARAFLDDSrRV 494
Cdd:COG1129 97 AENIFL----------GREPRRGGLIDWRAMrrrarellarlgLDIDPDTPVGD----LSVAQQQLVEIARALSRDA-RV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 495 LLFDEPTAHLDiETEVE--------LKR---AMLpvfdhhlvfFATHRlhwMNEM----DYILVMDHGKIVQQGTPAEL 558
Cdd:COG1129 162 LILDEPTASLT-EREVErlfriirrLKAqgvAII---------YISHR---LDEVfeiaDRVTVLRDGRLVGTGPVAEL 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
339-553 |
1.98e-14 |
|
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: 71.81 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 339 KVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQ--DGQINVRDTAvphLDKQAWQRSFVYIP 416
Cdd:cd03213 12 TVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRP---LDKRSFRKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QAPYLfHASL--RDNLAFyapgaseeavmqaAAKagltdwiatlpdglatqigegARGVSGGQAQRIALARAFLdDSRRV 494
Cdd:cd03213 89 QDDIL-HPTLtvRETLMF-------------AAK---------------------LRGLSGGERKRVSIALELV-SNPSL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834933330 495 LLFDEPTAHLDIETE---VELKRAMlpVFDHHLVFFATHRLHwmNEM----DYILVMDHGKIVQQG 553
Cdd:cd03213 133 LFLDEPTSGLDSSSAlqvMSLLRRL--ADTGRTIICSIHQPS--SEIfelfDKLLLLSQGRVIYFG 194
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
335-558 |
2.82e-14 |
|
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: 72.81 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSP-----------QDGQINVRDtavphl 403
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtygndvrlfgeRRGGEDVWE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 404 dkqaWQRSFVYIPQApylFHASLRDNL--------AFYA-----PGASEEAVMQAAakagltDWIATLpdGLATQIGEGA 470
Cdd:COG1119 76 ----LRKRIGLVSPA---LQLRFPRDEtvldvvlsGFFDsiglyREPTDEQRERAR------ELLELL--GLAHLADRPF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 471 RGVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMlpvfDH-------HLVfFATHRLH-WMNEMDYIL 542
Cdd:COG1119 141 GTLSQGEQRRVLIARALVKDP-ELLILDEPTAGLDLGARELLLALL----DKlaaegapTLV-LVTHHVEeIPPGITHVL 214
|
250
....*....|....*.
gi 1834933330 543 VMDHGKIVQQGTPAEL 558
Cdd:COG1119 215 LLKDGRVVAAGPKEEV 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
332-558 |
7.46e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.19 E-value: 7.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 332 DDTLALNKVNVSYGESqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDK--QAWQ 409
Cdd:PRK13636 3 DYILKVEELNYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 410 RSFVYIPQAP--YLFHASLRDNLAFYAPGAS------EEAVMQAAAKAGltdwIATLPDglatqigEGARGVSGGQAQRI 481
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSASVYQDVSFGAVNLKlpedevRKRVDNALKRTG----IEHLKD-------KPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 482 ALArAFLDDSRRVLLFDEPTAHLD---IETEVELKRAMLPVFDHHLVfFATHRLHWMN-EMDYILVMDHGKIVQQGTPAE 557
Cdd:PRK13636 151 AIA-GVLVMEPKVLVLDEPTAGLDpmgVSEIMKLLVEMQKELGLTII-IATHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228
|
.
gi 1834933330 558 L 558
Cdd:PRK13636 229 V 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-558 |
7.76e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 71.62 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVrDTAVPHLDKQAWQ-------RSFVYIPQAPYLF-H 423
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV-DGKVLYFGKDIFQidaiklrKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 424 ASLRDNLAF--YAPGASE-----EAVMQAAAKAGLTDWIATLPDGLATQIgegargvSGGQAQRIALARAfLDDSRRVLL 496
Cdd:PRK14246 105 LSIYDNIAYplKSHGIKEkreikKIVEECLRKVGLWKEVYDRLNSPASQL-------SGGQQQRLTIARA-LALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 497 FDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEI 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
350-572 |
7.83e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.96 E-value: 7.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 350 PTLKDIT--FSVHGFqkVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQ--AWQRSFVYIPQAP--YLFH 423
Cdd:PRK13638 15 PVLKGLNldFSLSPV--TGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 424 ASLRDNLAFYAP--GASEEAVMQAAAKAgltdwiATLPDGLATQiGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEPT 501
Cdd:PRK13638 93 TDIDSDIAFSLRnlGVPEAEITRRVDEA------LTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQA-RYLLLDEPT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 502 AHLDIETEVEL---KRAMLPVFDHhlVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAE-------LEQQGGT---YVR 567
Cdd:PRK13638 165 AGLDPAGRTQMiaiIRRIVAQGNH--VIISSHDIDLIYEIsDAVYVLRQGQILTHGAPGEvfacteaMEQAGLTqpwLVK 242
|
....*
gi 1834933330 568 LRSEM 572
Cdd:PRK13638 243 LHTQL 247
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
336-573 |
9.02e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.05 E-value: 9.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 336 ALNKVNVSYGESQtptlkdITfsvhgfqkvGIIGASGSGKSTLINTLGGFLSPQDGQINV--RDTAVpHLDkqAWQRSFV 413
Cdd:TIGR01257 945 AVDRLNITFYENQ------IT---------AFLGHNGAGKTTTLSILTGLLPPTSGTVLVggKDIET-NLD--AVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YIPQAPYLFH-ASLRDNLAFYA--PGASEEAVmQAAAKAGLTDwiatlpDGLATQIGEGARGVSGGQAQRIALARAFLDD 490
Cdd:TIGR01257 1007 MCPQHNILFHhLTVAEHILFYAqlKGRSWEEA-QLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 491 SRRVLLfDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAELEQQGGT--YVR 567
Cdd:TIGR01257 1080 AKVVVL-DEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTPLFLKNCFGTgfYLT 1158
|
....*.
gi 1834933330 568 LRSEME 573
Cdd:TIGR01257 1159 LVRKMK 1164
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
352-558 |
1.00e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.64 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAW---QRSFVYIPQ-APYLFH---- 423
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkafRRDIQMVFQdSISAVNprkt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 424 --ASLRDNLAFYAPGASEEAVMQAAAKAGLTDWIATLPDGLATQigegargVSGGQAQRIALARAfLDDSRRVLLFDEPT 501
Cdd:PRK10419 108 vrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ-------LSGGQLQRVCLARA-LAVEPKLLILDEAV 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 502 AHLDIETEVELKRaMLPVFDHHL---VFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:PRK10419 180 SNLDLVLQAGVIR-LLKKLQQQFgtaCLFITHDLRLVERFcQRVMVMDNGQIVETQPVGDK 239
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
335-558 |
1.06e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVy 414
Cdd:PRK13537 8 IDFRNVEKRYGD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQAPYL---FhaSLRDNLAFYAPGASEEAVMQAAAKAGLTDWiATLPDGLATQIGEgargVSGGQAQRIALARAFLDDS 491
Cdd:PRK13537 85 VPQFDNLdpdF--TVRENLLVFGRYFGLSAAAARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 492 rRVLLFDEPTAHLDIETE---VELKRAMLPvfDHHLVFFAThrlHWMNEM----DYILVMDHGKIVQQGTPAEL 558
Cdd:PRK13537 158 -DVLVLDEPTTGLDPQARhlmWERLRSLLA--RGKTILLTT---HFMEEAerlcDRLCVIEEGRKIAEGAPHAL 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
346-558 |
1.08e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 71.66 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 346 ESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAP--YLFH 423
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 424 ASLRDNLAF--YAPGASEEAVMQAAAKAGLTdwiatlPDGLATQIGEGARgVSGGQAQRIALArAFLDDSRRVLLFDEPT 501
Cdd:PRK13642 97 ATVEDDVAFgmENQGIPREEMIKRVDEALLA------VNMLDFKTREPAR-LSGGQKQRVAVA-GIIALRPEIIILDEST 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 502 AHLDIETEVELKRAMLPVFD--HHLVFFATHRLHWMNEMDYILVMDHGKIVQQGTPAEL 558
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
350-532 |
1.32e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.57 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 350 PTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPhldkqawqrsfVYIPQapylfHASLRDN 429
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARV-----------AYVPQ-----RSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 430 LafyaPGASEEAVM-------------QAAAKAGLTDWIATLpdGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLL 496
Cdd:NF040873 70 L----PLTVRDLVAmgrwarrglwrrlTRDDRAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEA-DLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1834933330 497 FDEPTAHLDIETEVEL----------KRAMLPV-FDHHLVFFATHRL 532
Cdd:NF040873 143 LDEPTTGLDAESRERIiallaeeharGATVVVVtHDLELVRRADPCV 189
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
335-530 |
1.73e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.50 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGesQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVphlDKQAWQRSFVY 414
Cdd:PRK11248 2 LQISHLYADYG--GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV---EGPGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQA--PYLfhaSLRDNLAF------YAPGASEEAVMQAAAKAGLtdwiatlpdglatqIGEGARGV---SGGQAQRIAL 483
Cdd:PRK11248 77 QNEGllPWR---NVQDNVAFglqlagVEKMQRLEIAHQMLKKVGL--------------EGAEKRYIwqlSGGQRQRVGI 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1834933330 484 ARAFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDH--HLVFFATH 530
Cdd:PRK11248 140 ARALAANP-QLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
337-508 |
1.87e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.81 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKvNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQ------- 409
Cdd:PRK10584 12 LKK-SVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 410 ----RSFVYIP--------QAPYLfhasLRdnlafyapGASEEAVMQAAAKagltdwiatlpdgLATQIGEGAR------ 471
Cdd:PRK10584 91 gfvfQSFMLIPtlnalenvELPAL----LR--------GESSRQSRNGAKA-------------LLEQLGLGKRldhlpa 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 1834933330 472 GVSGGQAQRIALARAFldDSRRVLLF-DEPTAHLDIET 508
Cdd:PRK10584 146 QLSGGEQQRVALARAF--NGRPDVLFaDEPTGNLDRQT 181
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
349-558 |
2.38e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 349 TPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVpHLDKQAWQRSFV-YIPQAP--YLFHAS 425
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-NAENEKWVRSKVgLVFQDPddQVFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 426 LRDNLAF------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALArAFLDDSRRVLLFDE 499
Cdd:PRK13647 97 VWDDVAFgpvnmgLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIA-GVLAMDPDVIVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834933330 500 PTAHLDIETEVELkRAMLPVFDHH--LVFFATHRLHWMNE-MDYILVMDHGKIVQQGTPAEL 558
Cdd:PRK13647 165 PMAYLDPRGQETL-MEILDRLHNQgkTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLL 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
341-558 |
2.75e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.81 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQ-TP----TLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVP-HLDK----QAWQR 410
Cdd:PRK13645 11 NVSYTYAKkTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPaNLKKikevKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 411 SFVYIPQAP--YLFHASLRDNLAFyAP---GASEEAVMQAAAKagLTDwIATLPDGLATQigeGARGVSGGQAQRIALAR 485
Cdd:PRK13645 91 EIGLVFQFPeyQLFQETIEKDIAF-GPvnlGENKQEAYKKVPE--LLK-LVQLPEDYVKR---SPFELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834933330 486 AFLDDSrRVLLFDEPTAHLDIETEVELKRAMLPVFDHH--LVFFATHRL-HWMNEMDYILVMDHGKIVQQGTPAEL 558
Cdd:PRK13645 164 IIAMDG-NTLVLDEPTGGLDPKGEEDFINLFERLNKEYkkRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
337-557 |
4.10e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.60 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSY--GESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQ---AWQRS 411
Cdd:PRK11153 4 LKNISKVFpqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 FVYIPQAPYLFhaSLR---DNLAFyaP----GASEEAVMQAAAK----AGLTDWIATLPDGLatqigegargvSGGQAQR 480
Cdd:PRK11153 84 IGMIFQHFNLL--SSRtvfDNVAL--PlelaGTPKAEIKARVTEllelVGLSDKADRYPAQL-----------SGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 481 IALARAfLDDSRRVLLFDEPTAHLDIETevelKRAMLPVF-----DHHL-VFFATHrlhwmnEMDYI-------LVMDHG 547
Cdd:PRK11153 149 VAIARA-LASNPKVLLCDEATSALDPAT----TRSILELLkdinrELGLtIVLITH------EMDVVkricdrvAVIDAG 217
|
250
....*....|
gi 1834933330 548 KIVQQGTPAE 557
Cdd:PRK11153 218 RLVEQGTVSE 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
353-544 |
4.59e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.37 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 353 KDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDT-AVPHLDKQAWQRSFVYIPQAPYLFHASLRDNLA 431
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 432 F---------YAPGASEE------------------------------------------------AVMQAAAKAGLTDW 454
Cdd:PTZ00265 482 YslyslkdleALSNYYNEdgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDF 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 455 IATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAM--LPVFDHHLVFFATHRL 532
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNP-KILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRL 640
|
250
....*....|..
gi 1834933330 533 HWMNEMDYILVM 544
Cdd:PTZ00265 641 STIRYANTIFVL 652
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
352-508 |
5.27e-13 |
|
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: 67.46 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRS-FVYIP---QAPYLFH-ASL 426
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrKREGLVLdLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 427 RDNLAfyapgaseeavmqaaakagltdwiatLPDGLatqigegargvSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDI 506
Cdd:cd03215 96 AENIA--------------------------LSSLL-----------SGGNQQKVVLARWLARDP-RVLILDEPTRGVDV 137
|
..
gi 1834933330 507 ET 508
Cdd:cd03215 138 GA 139
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
347-557 |
7.27e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.81 E-value: 7.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 347 SQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGfLSPQDGQINVRDTAVPHLD--KQAWQRSFVyIPQAPYLFHA 424
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSaaELARHRAYL-SQQQTPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 425 SLRDNLAFYAP-----GASEEAVMQAAAKAGLTdwiatlpDGLATQIGEgargVSGGQAQRIALARAFLDDSR------R 493
Cdd:PRK03695 85 PVFQYLTLHQPdktrtEAVASALNEVAEALGLD-------DKLGRSVNQ----LSGGEWQRVRLAAVVLQVWPdinpagQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 494 VLLFDEPTAHLDIETEVELKRAMlpvfdHHL------VFFATHRL-HWMNEMDYILVMDHGKIVQQGTPAE 557
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLL-----SELcqqgiaVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
337-558 |
9.45e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.06 E-value: 9.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGEsqTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPhlDKQAWQRSFVYIP 416
Cdd:PRK11000 6 LRNVTKAYGD--VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QAPYLF-HASLRDNLAF---YAPGASEEA---VMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAFLD 489
Cdd:PRK11000 82 QSYALYpHLSVAENMSFglkLAGAKKEEInqrVNQVAEVLQLAHLLDRKPKAL-----------SGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 490 DSRrVLLFDEPTAHLDIETEVE-----------LKRAMLPVfdhhlvffaTH-RLHWMNEMDYILVMDHGKIVQQGTPAE 557
Cdd:PRK11000 151 EPS-VFLLDEPLSNLDAALRVQmrieisrlhkrLGRTMIYV---------THdQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
.
gi 1834933330 558 L 558
Cdd:PRK11000 221 L 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
334-562 |
1.01e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFV 413
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 yIPQAPYL-FHASLRDNLAFYAPGASEEAVMQAAAKAGLTDWiATLPDGLATQIGEgargVSGGQAQRIALARAFLDDSr 492
Cdd:PRK13536 119 -VPQFDNLdLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEF-ARLESKADARVSD----LSGGMKRRLTLARALINDP- 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 493 RVLLFDEPTAHLDIETE---VELKRAMLPvfDHHLVFFAThrlHWMNEM----DYILVMDHGKIVQQGTPAEL--EQQG 562
Cdd:PRK13536 192 QLLILDEPTTGLDPHARhliWERLRSLLA--RGKTILLTT---HFMEEAerlcDRLCVLEAGRKIAEGRPHALidEHIG 265
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
355-558 |
1.15e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.09 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 355 ITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQR-SFVYIPQAPYLF----------- 422
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARmGVVRTFQHVRLFremtvienllv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 423 --HASLRDNL---AFYAPG---ASEEAVMQAAA---KAGLTDwIATLPDGlatqigegarGVSGGQAQRIALARAFLDDS 491
Cdd:PRK11300 104 aqHQQLKTGLfsgLLKTPAfrrAESEALDRAATwleRVGLLE-HANRQAG----------NLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 492 rRVLLFDEPTAHLDIETEVELKRAMLPVFDHH--LVFFATHRLHW-MNEMDYILVMDHGKIVQQGTPAEL 558
Cdd:PRK11300 173 -EILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLvMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
335-532 |
1.25e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.88 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLG--GFLSPQ---DGQI--NVRDTAVPHLDKQA 407
Cdd:PRK14239 6 LQVSDLSVYYNKKKA--LNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIvyNGHNIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 408 WQRSFVYIPQAPYLFHASLRDNLAF--YAPGASEEAVMQAAAKAGLTDwiATLPDGLATQIGEGARGVSGGQAQRIALAR 485
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVYglRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIAR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1834933330 486 AfLDDSRRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRL 532
Cdd:PRK14239 162 V-LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
354-530 |
1.61e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 354 DITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQawqrsfvYIPQAPYLFHA-------SL 426
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYLGHQpgiktelTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 427 RDNLAFYAPGA---SEEAVMQAAAKAGLTDWiATLPdglatqigegARGVSGGQAQRIALARAFLDDsRRVLLFDEP-TA 502
Cdd:PRK13538 92 LENLRFYQRLHgpgDDEALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALARLWLTR-APLWILDEPfTA 159
|
170 180 190
....*....|....*....|....*....|...
gi 1834933330 503 hLDIETEVELKRamlpVFDHHL-----VFFATH 530
Cdd:PRK13538 160 -IDKQGVARLEA----LLAQHAeqggmVILTTH 187
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
352-558 |
1.67e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 67.94 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVYIPQAPY----------- 420
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDPNtslnprlnigq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 421 LFHASLRDNLAFYAPgASEEAVMQAAAKAGLtdwiatLPDGLATQIGEgargVSGGQAQRIALARAFLDDSrRVLLFDEP 500
Cdd:COG4167 109 ILEEPLRLNTDLTAE-EREERIFATLRLVGL------LPEHANFYPHM----LSSGQKQRVALARALILQP-KIIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 501 TAHLDIETEVELKRAMLPV-FDHHLVF-FATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:COG4167 177 LAALDMSVRSQIINLMLELqEKLGISYiYVSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEV 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
326-532 |
2.11e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.50 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 326 QPTWQADDTLALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLI---NTLGGFLSP--QDGQINVRDTAV 400
Cdd:PRK14243 2 STLNGTETVLRTENLNVYYGSFLA--VKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 401 --PHLDKQAWQRSFVYIPQAPYLFHASLRDNLAFYA-----PGASEEAVMQAAAKAGLtdWiatlpDGLATQIGEGARGV 473
Cdd:PRK14243 80 yaPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGAringyKGDMDELVERSLRQAAL--W-----DEVKDKLKQSGLSL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 474 SGGQAQRIALARAfLDDSRRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRL 532
Cdd:PRK14243 153 SGGQQQRLCIARA-IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
336-547 |
2.23e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.37 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 336 ALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGfLSPQDGQINVrDTAVPHLDKQAWQR----- 410
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRV-EGRVEFFNQNIYERrvnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 411 ------SFVYiPQaPYLFHASLRDNLAF------YAPGASEEAVMQAAAKAgltdwiATLPDGLATQIGEGARGVSGGQA 478
Cdd:PRK14258 85 rlrrqvSMVH-PK-PNLFPMSVYDNVAYgvkivgWRPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 479 QRIALARAfLDDSRRVLLFDEPTAHLDIETEVELKRAM--LPVFDHHLVFFATHRLHWMNEMDYILVMDHG 547
Cdd:PRK14258 157 QRLCIARA-LAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
347-561 |
2.38e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 347 SQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLD-KQAWQRSFVYIP-----QApy 420
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVPedrkgEG-- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 421 LF-HASLRDNLAFyapgaseeAVMQAAAKAGL----------TDWIATL---PDGLATQIGEgargVSGGQAQRIALARA 486
Cdd:COG1129 341 LVlDLSIRENITL--------ASLDRLSRGGLldrrreralaEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 487 FLDDSrRVLLFDEPTAHLDIETEVELkramlpvfdhhlvffatHRLhwMNEM---------------------DYILVMD 545
Cdd:COG1129 409 LATDP-KVLILDEPTRGIDVGAKAEI-----------------YRL--IRELaaegkavivisselpellglsDRILVMR 468
|
250
....*....|....*.
gi 1834933330 546 HGKIVQQGTPAELEQQ 561
Cdd:COG1129 469 EGRIVGELDREEATEE 484
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
341-561 |
2.47e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 67.46 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYG-ESQTP----TLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRS---- 411
Cdd:PRK13649 7 NVSYTyQAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQirkk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 --FVYIPQAPYLFHASLRDNLAFyAP---GAS-EEAVMQAAAKAGLTdwiatlpdGLATQI-GEGARGVSGGQAQRIALA 484
Cdd:PRK13649 87 vgLVFQFPESQLFEETVLKDVAF-GPqnfGVSqEEAEALAREKLALV--------GISESLfEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 485 rAFLDDSRRVLLFDEPTAHLDIETEVELKRamlpvfdhhlVFFATHRL--------HWMNEM----DYILVMDHGKIVQQ 552
Cdd:PRK13649 158 -GILAMEPKILVLDEPTAGLDPKGRKELMT----------LFKKLHQSgmtivlvtHLMDDVanyaDFVYVLEKGKLVLS 226
|
....*....
gi 1834933330 553 GTPAELEQQ 561
Cdd:PRK13649 227 GKPKDIFQD 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
355-558 |
2.97e-12 |
|
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: 69.06 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 355 ITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVR------DTAVPHLDKQAWQRSFVYIPQAPY-LF-HASL 426
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvDMTKPGPDGRGRAKRYIGILHQEYdLYpHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 427 RDNL--AFYAPGASEEAVMQAA---AKAGLTDWIAT-----LPDGLatqigegargvSGGQAQRIALARAFLDDSRRVLL 496
Cdd:TIGR03269 383 LDNLteAIGLELPDELARMKAVitlKMVGFDEEKAEeildkYPDEL-----------SEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834933330 497 fDEPTAHLDIETEVELKRAMLPVFD--HHLVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:TIGR03269 452 -DEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVcDRAALMRDGKIVKIGDPEEI 515
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
341-567 |
3.70e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.11 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQ-TP----TLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRS---- 411
Cdd:PRK13646 7 NVSYTYQKgTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPvrkr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 412 --FVY-IPQAPyLFHASLRDNLAFyAPGASEEAVMQAAAKAglTDWIATLpdGLATQIGEGAR-GVSGGQAQRIALArAF 487
Cdd:PRK13646 87 igMVFqFPESQ-LFEDTVEREIIF-GPKNFKMNLDEVKNYA--HRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIV-SI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 488 LDDSRRVLLFDEPTAHLDIETEVELKRAM--LPVFDHHLVFFATHRlhwMNEM----DYILVMDHGKIVQQGTPAELEQQ 561
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHD---MNEVaryaDEVIVMKEGSIVSQTSPKELFKD 236
|
....*.
gi 1834933330 562 gGTYVR 567
Cdd:PRK13646 237 -KKKLA 241
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
346-557 |
4.37e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.03 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 346 ESQTPT----LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQIN-----------------------VRDT 398
Cdd:PRK13651 13 NKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekekvleklvIQKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 399 AVPHLD--KQAWQRSFVYIPQAPY-LFHASLRDNLAFYAP--GASEEAVMQAAAK----AGL-TDWIATLPDGLatqige 468
Cdd:PRK13651 93 RFKKIKkiKEIRRRVGVVFQFAEYqLFEQTIEKDIIFGPVsmGVSKEEAKKRAAKyielVGLdESYLQRSPFEL------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 469 gargvSGGQAQRIALArAFLDDSRRVLLFDEPTAHLDIETEVElkraMLPVFDH-----HLVFFATHR----LHWMNEmd 539
Cdd:PRK13651 167 -----SGGQKRRVALA-GILAMEPDFLVFDEPTAGLDPQGVKE----ILEIFDNlnkqgKTIILVTHDldnvLEWTKR-- 234
|
250
....*....|....*...
gi 1834933330 540 yILVMDHGKIVQQGTPAE 557
Cdd:PRK13651 235 -TIFFKDGKIIKDGDTYD 251
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
352-531 |
4.98e-12 |
|
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: 64.48 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVrdtavpHLDKQAWqrsfvYIPQAPYLFHASLRDNLA 431
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM------PEGEDLL-----FLPQRPYLPLGTLREQLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 432 FyaPgaseeavmqaaakagltdWIATLpdglatqigegargvSGGQAQRIALARAFLDDSRRVLLfDEPTAHLDIETEve 511
Cdd:cd03223 86 Y--P------------------WDDVL---------------SGGEQQRLAFARLLLHKPKFVFL-DEATSALDEESE-- 127
|
170 180
....*....|....*....|..
gi 1834933330 512 lkRAMLPVFDHHL--VFFATHR 531
Cdd:cd03223 128 --DRLYQLLKELGitVISVGHR 147
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-558 |
1.00e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 65.32 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 342 VSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGF--LSPQ---DGQINVRDTAVPHLDKQAWQRSFVYIP 416
Cdd:PRK14247 11 VSFGQVEV--LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIELRRRVQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QAPY-LFHASLRDNLAF--------YAPGASEEAVMQAAAKAGLtdWiatlpDGLATQIGEGARGVSGGQAQRIALARAF 487
Cdd:PRK14247 89 QIPNpIPNLSIFENVALglklnrlvKSKKELQERVRWALEKAQL--W-----DEVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834933330 488 LDDSRrVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:PRK14247 162 AFQPE-VLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREV 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
367-553 |
1.26e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.44 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 367 IIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAW----QRSFVYIPQAPYLF-HASLRDNLAFyapGaseea 441
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClppeKRRIGYVFQDARLFpHYKVRGNLRY---G----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 442 vMQAAAKAGLTDWIATLpdGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETevelKRAMLPvFD 521
Cdd:PRK11144 101 -MAKSMVAQFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAP-ELLLMDEPLASLDLPR----KRELLP-YL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1834933330 522 HHL-------VFFATHRLhwmNEM----DYILVMDHGKIVQQG 553
Cdd:PRK11144 172 ERLareinipILYVSHSL---DEIlrlaDRVVVLEQGKVKAFG 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
354-553 |
1.44e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.95 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 354 DITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAW---QRSFV------YIPQAPylfha 424
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaERRRLlrtewgFVHQHP----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 425 slRDNL--AFYAPGASEEAVMQAAAK------AGLTDWIATLPDGLAtQIGEGARGVSGGQAQRIALARAFLDDSRRVLL 496
Cdd:PRK11701 99 --RDGLrmQVSAGGNIGERLMAVGARhygdirATAGDWLERVEIDAA-RIDDLPTTFSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834933330 497 fDEPTAHLDIETE---VELKRAMlpVFDHHL-VFFATH-----RLHwmneMDYILVMDHGKIVQQG 553
Cdd:PRK11701 176 -DEPTGGLDVSVQarlLDLLRGL--VRELGLaVVIVTHdlavaRLL----AHRLLVMKQGRVVESG 234
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
354-558 |
2.03e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 65.52 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 354 DITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQ---RSFVYIPQAPYlfhASLrdNl 430
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRMQMVFQDPY---ASL--N- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 431 afyaP----GASEEAVMQA---AAKAGLTDWIATLPD--GL-ATQIGEGARGVSGGQAQRIALARAfLDDSRRVLLFDEP 500
Cdd:COG4608 110 ----PrmtvGDIIAEPLRIhglASKAERRERVAELLElvGLrPEHADRYPHEFSGGQRQRIGIARA-LALNPKLIVCDEP 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 501 TAHLD--IETEV-----ELKRAmlpvFDHHLVFFAtHRL----HwmneM-DYILVMDHGKIVQQGTPAEL 558
Cdd:COG4608 185 VSALDvsIQAQVlnlleDLQDE----LGLTYLFIS-HDLsvvrH----IsDRVAVMYLGKIVEIAPRDEL 245
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
318-506 |
3.61e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.43 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 318 DRDLLPVRQPTWQADDTLALNKVNVSyGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRD 397
Cdd:COG3845 241 EVLLRVEKAPAEPGEVVLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 398 TAVPHLD-KQAWQRSFVYIPQAPyLFHA-----SLRDNLA---FYAPGASEEAVMQ-AAAKAGLTDWIATL---PDGLAT 464
Cdd:COG3845 320 EDITGLSpRERRRLGVAYIPEDR-LGRGlvpdmSVAENLIlgrYRRPPFSRGGFLDrKAIRAFAEELIEEFdvrTPGPDT 398
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1834933330 465 QigegARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDI 506
Cdd:COG3845 399 P----ARSLSGGNQQKVILARELSRDP-KLLIAAQPTRGLDV 435
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
352-550 |
3.65e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.97 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQI--------NVRDTAVPHLdkqawQRSFVYIPQAPYLF- 422
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditRLKNREVPFL-----RRQIGMIFQDHHLLm 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 423 HASLRDNLA--FYAPGASEE----AVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAFLDDSrRVLL 496
Cdd:PRK10908 93 DRTVYDNVAipLIIAGASGDdirrRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKP-AVLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 497 FDEPTAHLDieteVELKRAMLPVFDHH-----LVFFATHRLHWMNEMDY-ILVMDHGKIV 550
Cdd:PRK10908 161 ADEPTGNLD----DALSEGILRLFEEFnrvgvTVLMATHDIGLISRRSYrMLTLSDGHLH 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
333-555 |
5.42e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 333 DTLALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQInvrdtavphldKQAWQRSF 412
Cdd:PRK09544 3 SLVSLENVSVSFGQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 413 VYIPQAPYLfHASLRDNLAFYA---PGASEEAVMQAAAKAgltdwiatlpdGLATQIGEGARGVSGGQAQRIALARAFLd 489
Cdd:PRK09544 70 GYVPQKLYL-DTTLPLTVNRFLrlrPGTKKEDILPALKRV-----------QAGHLIDAPMQKLSGGETQRVLLARALL- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 490 DSRRVLLFDEPTAHLDIETEVELKRaMLPVFDHHL---VFFATHRLHW-MNEMDYILVMDHgKIVQQGTP 555
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYD-LIDQLRRELdcaVLMVSHDLHLvMAKTDEVLCLNH-HICCSGTP 204
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
349-558 |
6.07e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.17 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 349 TPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQ-RSFVYIP-QAP--YLFHA 424
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvRKTVGIVfQNPddQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 425 SLRDNLAFyAP---GASEEA----VMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALArAFLDDSRRVLLF 497
Cdd:PRK13639 95 TVEEDVAF-GPlnlGLSKEEvekrVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIA-GILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 498 DEPTAHLDIETEVELKRAMLPVFDHHL-VFFATHRLHWMNE-MDYILVMDHGKIVQQGTPAEL 558
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGItIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
352-557 |
6.76e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.79 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWqrsfvyipqapylFHASL--RDN 429
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELGAG-------------FHPELtgREN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 430 LAFYA-----PGASEEAVMQA-AAKAGLTDWIATlPdglatqigegargV---SGGQAQRIALARA-FLD-DsrrVLLFD 498
Cdd:COG1134 109 IYLNGrllglSRKEIDEKFDEiVEFAELGDFIDQ-P-------------VktySSGMRARLAFAVAtAVDpD---ILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 499 EPTAHLDIETEVELKRAMLPVFDHH-LVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAE 557
Cdd:COG1134 172 EVLAVGDAAFQKKCLARIRELRESGrTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEE 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
341-558 |
1.01e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.70 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHL-DKQAWQRSFVYIPQAP 419
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYaSKEVARRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 420 YLFHASLRDNLAF----YAP------GASEEAVMQAAAKAGLTDwiatlpdgLATQigeGARGVSGGQAQRIALARAFLD 489
Cdd:PRK10253 92 TPGDITVQELVARgrypHQPlftrwrKEDEEAVTKAMQATGITH--------LADQ---SVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 490 DSRrVLLFDEPTAHLDIETEVELKRaMLPVFDHHLVFFATHRLHWMNE----MDYILVMDHGKIVQQGTPAEL 558
Cdd:PRK10253 161 ETA-IMLLDEPTTWLDISHQIDLLE-LLSELNREKGYTLAAVLHDLNQacryASHLIALREGKIVAQGAPKEI 231
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
334-558 |
1.03e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 63.32 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 334 TLALNKVNVSYgESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQawQRSFV 413
Cdd:PRK11650 3 GLKLQAVRKSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA--DRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 YIPQAPYLF-HASLRDNLAfYA------PGASEEAVMQAAAKA-GLTDWIATLPdglatqigegaRGVSGGQAQRIALAR 485
Cdd:PRK11650 80 MVFQNYALYpHMSVRENMA-YGlkirgmPKAEIEERVAEAARIlELEPLLDRKP-----------RELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 486 AFLDDSrRVLLFDEPTAHLD----IETEVELKR--------AMlpvfdhhlvfFATH-RLHWMNEMDYILVMDHGKIVQQ 552
Cdd:PRK11650 148 AIVREP-AVFLFDEPLSNLDaklrVQMRLEIQRlhrrlkttSL----------YVTHdQVEAMTLADRVVVMNGGVAEQI 216
|
....*.
gi 1834933330 553 GTPAEL 558
Cdd:PRK11650 217 GTPVEV 222
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
15-292 |
1.86e-10 |
|
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: 62.05 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 15 AAAIMAVLTFVQAFMIIFqakylsvAIVNLWQLKSVRTIVLPLLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFM 94
Cdd:cd18552 7 GMILVAATTAALAWLLKP-------LLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 95 AKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLTPwIVLIYIAFIQ-WKEALFLLAIYPLIIFFMII 173
Cdd:cd18552 80 DKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTV-IGLLGVLFYLdWKLTLIALVVLPLAALPIRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 174 LGLAAQAKADRQYAGYQRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTLSIA 253
Cdd:cd18552 159 IGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1834933330 254 IIAVFLGFGLMNNTI---QLLPALIILTLApdyFAPIRNFAN 292
Cdd:cd18552 239 LVLWYGGYQVISGELtpgEFISFITALLLL---YQPIKRLSN 277
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
327-549 |
3.21e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 327 PTWQaddTLALNKVNVSYGEsQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQ 406
Cdd:PRK10522 318 PDWQ---TLELRNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 407 AWQRSFVYIPQAPYLFHASLRDNlafyapgaseeavMQAAAKAGLTDWIATLPDGLATQIgEGAR----GVSGGQAQRIA 482
Cdd:PRK10522 394 DYRKLFSAVFTDFHLFDQLLGPE-------------GKPANPALVEKWLERLKMAHKLEL-EDGRisnlKLSKGQKKRLA 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 483 LARAFLdDSRRVLLFDEPTAHLDIETEVELKRAMLPVFDH--HLVFFATHRLHWMNEMDYILVMDHGKI 549
Cdd:PRK10522 460 LLLALA-EERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
335-558 |
4.04e-10 |
|
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: 62.39 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYG--ESQTPTLKDITFSVHGFQKVGIIGASGSGKS----TLINTLGGFLSPQDGQINVRDTAVPHLDKQAW 408
Cdd:COG4172 7 LSVEDLSVAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 409 QR------SFVYipQAP-----------------YLFHASLRDnlafyapgaseeavmqAAAKAGLTDWIAtlpdglATQ 465
Cdd:COG4172 87 RRirgnriAMIF--QEPmtslnplhtigkqiaevLRLHRGLSG----------------AAARARALELLE------RVG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 466 IGEGARGV-------SGGQAQRIALARAFLDDSRrVLLFDEPTAHLD--IETEV-----ELKR----AMLpvfdhhlvfF 527
Cdd:COG4172 143 IPDPERRLdayphqlSGGQRQRVMIAMALANEPD-LLIADEPTTALDvtVQAQIldllkDLQRelgmALL---------L 212
|
250 260 270
....*....|....*....|....*....|..
gi 1834933330 528 ATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:COG4172 213 ITHDLGVVRRFaDRVAVMRQGEIVEQGPTAEL 244
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
337-574 |
4.74e-10 |
|
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: 62.26 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGeSQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQinvrdtAVPHLDkqawqRSFVYIP 416
Cdd:TIGR03719 7 MNRVSKVVP-PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE------ARPQPG-----IKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QAPYL-FHASLRDNL---------------AFYAPGASEEAVMQAAAK--AGLTDWIATLpDG--LATQIGEGARG---- 472
Cdd:TIGR03719 75 QEPQLdPTKTVRENVeegvaeikdaldrfnEISAKYAEPDADFDKLAAeqAELQEIIDAA-DAwdLDSQLEIAMDAlrcp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 473 --------VSGGQAQRIALARAFLD--DsrrVLLFDEPTAHLDIETEVELkramlpvfDHHL------VFFATHRLHWM- 535
Cdd:TIGR03719 154 pwdadvtkLSGGERRRVALCRLLLSkpD---MLLLDEPTNHLDAESVAWL--------ERHLqeypgtVVAVTHDRYFLd 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1834933330 536 NEMDYILVMDHGkivqQGTPAE------LEQQggtyvRLRSEMEG 574
Cdd:TIGR03719 223 NVAGWILELDRG----RGIPWEgnysswLEQK-----QKRLEQEE 258
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
352-550 |
5.78e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.10 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLdkQAWQRSfVYI------PQ---APYLf 422
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL--PEYKRA-KYIgrvfqdPMmgtAPSM- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 423 haSLRDNLAF-YAPGaseeavmqaaAKAGLT------------DWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLD 489
Cdd:COG1101 98 --TIEENLALaYRRG----------KRRGLRrgltkkrrelfrELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 490 DSrRVLLFDEPTAHLDIET--EV-ELKRAMlpVFDHHL-VFFATHRLHwmNEMDY---ILVMDHGKIV 550
Cdd:COG1101 166 KP-KLLLLDEHTAALDPKTaaLVlELTEKI--VEENNLtTLMVTHNME--QALDYgnrLIMMHEGRII 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
352-553 |
7.59e-10 |
|
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: 59.08 E-value: 7.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWqrsfvyipqapylFHASL--RDN 429
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGG-------------FNPELtgREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 430 LAFYA-----PGASEEAVMQA-AAKAGLTDWIaTLPdglatqigegARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAH 503
Cdd:cd03220 105 IYLNGrllglSRKEIDEKIDEiIEFSELGDFI-DLP----------VKTYSSGMKARLAFAIATALEP-DILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1834933330 504 LDieteVELKRAMLPVFDHHL-----VFFATHRLHWMNEM-DYILVMDHGKIVQQG 553
Cdd:cd03220 173 GD----AAFQEKCQRRLRELLkqgktVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
352-553 |
1.02e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQdGQINVRDTAVPHLDKQA---WQRSFVYIPQAPY-------- 420
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPNsslnprln 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 421 ---LFHASLRDNLAFYAPGASEEAVMQAAAKAGLTdwiatlPDGLATQIGEgargVSGGQAQRIALARAFLDDSRRVLLf 497
Cdd:PRK15134 381 vlqIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLD------PETRHRYPAE----FSGGQRQRIAIARALILKPSLIIL- 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 498 DEPTAHLDIETEVELkRAMLPVF--DHHLVF-FATHRLHWMNEMDY-ILVMDHGKIVQQG 553
Cdd:PRK15134 450 DEPTSSLDKTVQAQI-LALLKSLqqKHQLAYlFISHDLHVVRALCHqVIVLRQGEVVEQG 508
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-553 |
1.32e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 340 VNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFL-----SPQDGQINV--RDTAVPHLDKQAWQRSF 412
Cdd:PRK14267 10 LRVYYGSNHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLfgRNIYSPDVDPIEVRREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 413 VYIPQAPYLF-HASLRDNLAF--------YAPGASEEAVMQAAAKAGLtdWiatlpDGLATQIGEGARGVSGGQAQRIAL 483
Cdd:PRK14267 88 GMVFQYPNPFpHLTIYDNVAIgvklnglvKSKKELDERVEWALKKAAL--W-----DEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 484 ARAfLDDSRRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEM-DYILVMDHGKIVQQG 553
Cdd:PRK14267 161 ARA-LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVG 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
293-549 |
1.59e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 293 DYHATLNGKNTLTAVLDILQRPTPTDRDL-----------LPVRQPTwQADDTLALNKVNVSyGESqtptLKDITFSVHG 361
Cdd:PRK15439 215 DGTIALSGKTADLSTDDIIQAITPAAREKslsasqklwleLPGNRRQ-QAAGAPVLTVEDLT-GEG----FRNISLEVRA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 362 FQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLD-KQAWQRSFVYIP---QAPYLF-HASLR--------D 428
Cdd:PRK15439 289 GEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPedrQSSGLYlDAPLAwnvcalthN 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 429 NLAFYAPGASEEAVMQAAAKA-GLTdwiatlpdglATQIGEGARGVSGGQAQRIALARAfLDDSRRVLLFDEPTAHLDIE 507
Cdd:PRK15439 369 RRGFWIKPARENAVLERYRRAlNIK----------FNHAEQAARTLSGGNQQKVLIAKC-LEASPQLLIVDEPTRGVDVS 437
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1834933330 508 TEVELKRAMLPVFDHHL-VFFATHRLHWMNEM-DYILVMDHGKI 549
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMaDRVLVMHQGEI 481
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
351-558 |
1.71e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 59.72 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 351 TLK---DITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQ--RSFV-YIPQAPYlfhA 424
Cdd:PRK15079 33 TLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavRSDIqMIFQDPL---A 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 425 SLR----------DNLAFYAPGASEEAVMQAA----AKAGLtdwiatLPDglatQIGEGARGVSGGQAQRIALARAFLDD 490
Cdd:PRK15079 110 SLNprmtigeiiaEPLRTYHPKLSRQEVKDRVkammLKVGL------LPN----LINRYPHEFSGGQCQRIGIARALILE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834933330 491 SRRVLLfDEPTAHLD--IETEV-----ELKRAMlpvfDHHLVFFAtHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:PRK15079 180 PKLIIC-DEPVSALDvsIQAQVvnllqQLQREM----GLSLIFIA-HDLAVVKHIsDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
341-567 |
1.71e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.01 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQ---AWQRSFVYIPQ 417
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 418 APYLF-HASLRDNLAF-------YAPGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAFLD 489
Cdd:PRK11831 92 SGALFtDMNVFDNVAYplrehtqLPAPLLHSTVMMKLEAVGLRGAAKLMPSEL-----------SGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 490 DSrRVLLFDEPTAHLD-IETEVELKraMLPVFDHHLVFFATHRLHWMNEM----DYILVMDHGKIVQQGTPAELEQQGGT 564
Cdd:PRK11831 161 EP-DLIMFDEPFVGQDpITMGVLVK--LISELNSALGVTCVVVSHDVPEVlsiaDHAYIVADKKIVAHGSAQALQANPDP 237
|
...
gi 1834933330 565 YVR 567
Cdd:PRK11831 238 RVR 240
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
337-540 |
2.49e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHlDKQAWQRSFVYIP 416
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QA----PYLfhaSLRDNLAF---YAPGASEEAVMQAAAKAG-LTDWiatlPDGLatqigegargVSGGQAQRIALARAFL 488
Cdd:PRK13540 81 HRsginPYL---TLRENCLYdihFSPGAVGITELCRLFSLEhLIDY----PCGL----------LSSGQKRQVALLRLWM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1834933330 489 DDSrRVLLFDEPTAHLDietEVELKRAMLPVFDHH----LVFFATHRLHWMNEMDY 540
Cdd:PRK13540 144 SKA-KLWLLDEPLVALD---ELSLLTIITKIQEHRakggAVLLTSHQDLPLNKADY 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
336-558 |
2.61e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.57 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 336 ALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTL-------GGFLSPQDGQINVRdTAVPHLDKQAW 408
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRYSGDVLLGGR-SIFNYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 409 QRSFVYIPQAPYLFHASLRDNL--AFYAPGASEEAVMQAAAKAGLTDwiATLPDGLATQIGEGARGVSGGQAQRIALARA 486
Cdd:PRK14271 100 RRRVGMLFQRPNPFPMSIMDNVlaGVRAHKLVPRKEFRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 487 fLDDSRRVLLFDEPTAHLDIETEVELKRAMLPVFDHHLVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAEL 558
Cdd:PRK14271 178 -LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQL 249
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
335-504 |
2.85e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.97 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFVY 414
Cdd:PRK11614 6 LSFDKVSAHYGKIQA--LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 I-PQAPYLF-HASLRDNLAFYAPGASEEAVMQAAAkagltdWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSr 492
Cdd:PRK11614 84 IvPEGRRVFsRMTVEENLAMGGFFAERDQFQERIK------WVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQP- 156
|
170
....*....|..
gi 1834933330 493 RVLLFDEPTAHL 504
Cdd:PRK11614 157 RLLLLDEPSLGL 168
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
352-558 |
3.17e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.43 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGF--LSPQDGQINVRdtaVPHLDKQAW--QRSFV-------------- 413
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYH---VALCEKCGYveRPSKVgepcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 ---YIPQAPYLFHASLRDN-------LAFYAPGASEEAVMQAAAKAGLT-----DWIATLPD--GLATQIGEGARGVSGG 476
Cdd:TIGR03269 93 evdFWNLSDKLRRRIRKRIaimlqrtFALYGDDTVLDNVLEALEEIGYEgkeavGRAVDLIEmvQLSHRITHIARDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 477 QAQRIALARAfLDDSRRVLLFDEPTAHLDIETEVELKRAMLP-VFDHHLVFFATHrlHWMNEM----DYILVMDHGKIVQ 551
Cdd:TIGR03269 173 EKQRVVLARQ-LAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTS--HWPEVIedlsDKAIWLENGEIKE 249
|
....*..
gi 1834933330 552 QGTPAEL 558
Cdd:TIGR03269 250 EGTPDEV 256
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
352-557 |
4.75e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.88 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLD-KQAWQRSFVYIPQAPYLFHA-SLRDN 429
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 430 LA---------FYAPGASEEAVMQAAAKAGLT-DwiatlPDGLATQIGEGARgvsggqaQRIALARAFLDDSrRVLLFDE 499
Cdd:COG3845 101 IVlgleptkggRLDRKAARARIRELSERYGLDvD-----PDAKVEDLSVGEQ-------QRVEILKALYRGA-RILILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 500 PTAHL-DIETEvELKRAMlpvfdHHL------VFFATHRLHwmnE-M---DYILVMDHGKIVQQGTPAE 557
Cdd:COG3845 168 PTAVLtPQEAD-ELFEIL-----RRLaaegksIIFITHKLR---EvMaiaDRVTVLRRGKVVGTVDTAE 227
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
347-550 |
6.31e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 347 SQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINV-RDTAVPHLD----KQAWQRSFVYIP----- 416
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVARLQqdppRNVEGTVYDFVAegiee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QAPYL--FHASLRDnlafYAPGASEEAVMQAAAKAGLTD----W---------IATL---PDGLATQIgegargvSGGQA 478
Cdd:PRK11147 94 QAEYLkrYHDISHL----VETDPSEKNLNELAKLQEQLDhhnlWqlenrinevLAQLgldPDAALSSL-------SGGWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834933330 479 QRIALARAFLDDSRrVLLFDEPTAHLDIETeVELKRAMLPVFDHHLVFFATHRLHWMNEMDYILVMDHGKIV 550
Cdd:PRK11147 163 RKAALGRALVSNPD-VLLLDEPTNHLDIET-IEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
335-526 |
6.32e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQInvrdtavphldKQAWQRSFVY 414
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----------KWSENANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 415 IPQapylfhaslrDNLAFYAPGASeeavmqaaakagLTDWI--------------ATLPDGLATQ--IGEGARGVSGGQA 478
Cdd:PRK15064 387 YAQ----------DHAYDFENDLT------------LFDWMsqwrqegddeqavrGTLGRLLFSQddIKKSVKVLSGGEK 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1834933330 479 QRIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRAmLPVFDHHLVF 526
Cdd:PRK15064 445 GRMLFGKLMMQKP-NVLVMDEPTNHMDMESIESLNMA-LEKYEGTLIF 490
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
352-558 |
8.44e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.44 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRSFV-YIPQAPYLFHA-SLRDN 429
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIgYLPQEASIFRRlSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 430 LAFYAPGASEEAVMQAAAKAG--LTDW-IATLPDGLatqigegARGVSGGQAQRIALARAFLDDSRRVLLfDEPTAHLDI 506
Cdd:PRK10895 99 LMAVLQIRDDLSAEQREDRANelMEEFhIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILL-DEPFAGVDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1834933330 507 ETEVELKRAMLPVFDHHL-VFFATHRLHW---MNEMDYILvmDHGKIVQQGTPAEL 558
Cdd:PRK10895 171 ISVIDIKRIIEHLRDSGLgVLITDHNVREtlaVCERAYIV--SQGHLIAHGTPTEI 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
345-558 |
1.14e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.90 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 345 GESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQ--INVRDTAVPHLDKQAWQRSFVYIP-QAPYl 421
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGElyYQGQDLLKADPEAQKLLRQKIQIVfQNPY- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 422 fhASL------RDNLAfyAP-------GASE--EAVMQAAAKAGL-TDWIATLPDGLatqigegargvSGGQAQRIALAR 485
Cdd:PRK11308 103 --GSLnprkkvGQILE--EPllintslSAAErrEKALAMMAKVGLrPEHYDRYPHMF-----------SGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 486 AFLDDSrRVLLFDEPTAHLD--IETEV-----ELKRAMlpvfdhHLVF-FATHRL----HWMNEmdyILVMDHGKIVQQG 553
Cdd:PRK11308 168 ALMLDP-DVVVADEPVSALDvsVQAQVlnlmmDLQQEL------GLSYvFISHDLsvveHIADE---VMVMYLGRCVEKG 237
|
....*
gi 1834933330 554 TPAEL 558
Cdd:PRK11308 238 TKEQI 242
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
365-558 |
1.14e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 57.75 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 365 VGIIGASGSGKSTLINTLgGFLSPQDGQINVRDTAVPH-LDKQAWQRSFVYIPQAPyLFHASL--RDNLAFYA----PGA 437
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNAL-AFRSPKGVKGSGSVLLNGMpIDAKEMRAISAYVQQDD-LFIPTLtvREHLMFQAhlrmPRR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 438 SEEAVMQAAAKAGLTDwiATLPDGLATQIGEGAR--GVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETEVELKRA 515
Cdd:TIGR00955 132 VTKKEKRERVDEVLQA--LGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDP-PLLFCDEPTSGLDSFMAYSVVQV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 516 MLpvfdhHL------VFFATHR--LHWMNEMDYILVMDHGKIVQQGTPAEL 558
Cdd:TIGR00955 209 LK-----GLaqkgktIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
351-523 |
2.17e-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: 55.11 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 351 TLKDITFSVHG--FQK---VGIIGASGSGKSTLINTLGGFLSPQDGQINVrdtavpHLDKQAwqrsfvYIPQapYL---F 422
Cdd:cd03237 9 TLGEFTLEVEGgsISEsevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI------ELDTVS------YKPQ--YIkadY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 423 HASLRDNLAFYAPGASEEAVMQaaakaglTDWIAtlPDGLATQIGEGARGVSGGQAQRIALArAFLDDSRRVLLFDEPTA 502
Cdd:cd03237 75 EGTVRDLLSSITKDFYTHPYFK-------TEIAK--PLQIEQILDREVPELSGGELQRVAIA-ACLSKDADIYLLDEPSA 144
|
170 180
....*....|....*....|.
gi 1834933330 503 HLDIETEVELKRAMLPVFDHH 523
Cdd:cd03237 145 YLDVEQRLMASKVIRRFAENN 165
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
341-516 |
2.18e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRdtavphldkqawqrsfvyIPQAPY 420
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 421 LFHASLRDNLafyAPGASEEAVMQAAAKAGLTD---WIATlPDGLATqigegargvsgGQAQRIALARAfLDDSRRVLLF 497
Cdd:COG2401 97 GREASLIDAI---GRKGDFKDAVELLNAVGLSDavlWLRR-FKELST-----------GQKFRFRLALL-LAERPKLLVI 160
|
170
....*....|....*....
gi 1834933330 498 DEPTAHLDIETEVELKRAM 516
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNL 179
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
342-507 |
3.66e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 342 VSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKqawQRSFVYIPQAPYL 421
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR---SRFMAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 422 FH-ASLRDNLAFYAPGASEEAVM---QAAAKAGLTDWIATLpdglatqigegARGVSGGQAQRIALARAFLDDSRRVLLf 497
Cdd:PRK13543 94 KAdLSTLENLHFLCGLHGRRAKQmpgSALAIVGLAGYEDTL-----------VRQLSAGQKKRLALARLWLSPAPLWLL- 161
|
170
....*....|
gi 1834933330 498 DEPTAHLDIE 507
Cdd:PRK13543 162 DEPYANLDLE 171
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
325-546 |
1.05e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 325 RQPTWQADDTLALNKVNVSYGESQTptLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINV-RDTAVPHL 403
Cdd:PRK10636 303 RAPESLPNPLLKMEKVSAGYGDRII--LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 404 DKQawQRSFVYIPQAPyLFHaslrdnLAFYAPGASEEAvmqaaakagLTDWIATLpdGL-ATQIGEGARGVSGGQAQRIA 482
Cdd:PRK10636 381 AQH--QLEFLRADESP-LQH------LARLAPQELEQK---------LRDYLGGF--GFqGDKVTEETRRFSGGEKARLV 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 483 LArafLDDSRR--VLLFDEPTAHLDIETEVELKRAMLPvFDHHLVfFATHRLHWMNEM--DYILVMDH 546
Cdd:PRK10636 441 LA---LIVWQRpnLLLLDEPTNHLDLDMRQALTEALID-FEGALV-VVSHDRHLLRSTtdDLYLVHDG 503
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
87-270 |
1.40e-07 |
|
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: 53.18 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 87 KTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLTPWIVLIYIAFIQWKEALFLLAIYPL 166
Cdd:cd18541 73 YDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 167 IIFFMIILGLAAQAKADRQYAGYQRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMStltIAMTSTF---A 243
Cdd:cd18541 153 LALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLR---LARVDALffpL 229
|
170 180
....*....|....*....|....*..
gi 1834933330 244 LDFFTTLSIAIIAVFLGFGLMNNTIQL 270
Cdd:cd18541 230 IGLLIGLSFLIVLWYGGRLVIRGTITL 256
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
352-555 |
1.48e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 53.00 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLIN-TLGGFLSpqdgQINVRDTAVP----------HLDKqawqrsFVYIPQAPy 420
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdTLYPALA----RRLHLKKEQPgnhdriegleHIDK------VIVIDQSP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 421 lFHASLRDNLAFYA----------------------------PGAS---------EEAVMQAAAKAGLTDWIATLPD-GL 462
Cdd:cd03271 80 -IGRTPRSNPATYTgvfdeirelfcevckgkrynretlevryKGKSiadvldmtvEEALEFFENIPKIARKLQTLCDvGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 463 A-TQIGEGARGVSGGQAQRIALARAFLDDS--RRVLLFDEPTAHL---DIetevelkRAMLPVFDH-----HLVFFATHR 531
Cdd:cd03271 159 GyIKLGQPATTLSGGEAQRIKLAKELSKRStgKTLYILDEPTTGLhfhDV-------KKLLEVLQRlvdkgNTVVVIEHN 231
|
250 260 270
....*....|....*....|....*....|
gi 1834933330 532 LHWMNEMDYILVM-----DH-GKIVQQGTP 555
Cdd:cd03271 232 LDVIKCADWIIDLgpeggDGgGQVVASGTP 261
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
337-564 |
1.88e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGesQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINV----------RDTAVPHLdkq 406
Cdd:NF033858 4 LEGVSHRYG--KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlggdmadarhRRAVCPRI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 407 awqrsfVYIPQA------PYLfhaSLRDNLAFYA----PGASEeavmQAAAKAGLTDwiATlpdGLATQIGEGARGVSGG 476
Cdd:NF033858 79 ------AYMPQGlgknlyPTL---SVFENLDFFGrlfgQDAAE----RRRRIDELLR--AT---GLAPFADRPAGKLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 477 QAQRIALARAFLDDSrRVLLFDEPTAHLD----------IEtEVELKRAMLPVfdhhLVffAThrlHWMNE---MDYILV 543
Cdd:NF033858 141 MKQKLGLCCALIHDP-DLLILDEPTTGVDplsrrqfwelID-RIRAERPGMSV----LV--AT---AYMEEaerFDWLVA 209
|
250 260
....*....|....*....|.
gi 1834933330 544 MDHGKIVQQGTPAELEQQGGT 564
Cdd:NF033858 210 MDAGRVLATGTPAELLARTGA 230
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
365-541 |
1.92e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 365 VGIIGASGSGKSTLINTLGGFLSPQDGQINvrdtavphldkqaWQRSFVYIPQapYLFHASlrdnlafyaPGASEEAVMQ 444
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-------------PELKISYKPQ--YIKPDY---------DGTVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 445 AAAKAGlTDWIAT-------LPDGLATQIGEgargVSGGQAQRIALARAFLDDSRrVLLFDEPTAHLDIETEV------- 510
Cdd:PRK13409 424 ITDDLG-SSYYKSeiikplqLERLLDKNVKD----LSGGELQRVAIAACLSRDAD-LYLLDEPSAHLDVEQRLavakair 497
|
170 180 190
....*....|....*....|....*....|....
gi 1834933330 511 ---ELKRAMLPVFDHHLVFfathrlhwmneMDYI 541
Cdd:PRK13409 498 riaEEREATALVVDHDIYM-----------IDYI 520
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
354-509 |
2.37e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.60 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 354 DITFSVHGFQKVGIIGASGSGKSTLINTLGGfLSPQDGqinvrdtavPHLDKQAWQRSFvYIPQAPYLFHASLRDNLAFy 433
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYG---------GRLTKPAKGKLF-YVPQRPYMTLGTLRDQIIY- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 434 aPGASEEAVMQAAAKAGLTDWIATLPDGLATQIGEGARGV-------SGGQAQRIALARAFLDDSRRVLLfDEPTAHLDI 506
Cdd:TIGR00954 538 -PDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVqdwmdvlSGGEKQRIAMARLFYHKPQFAIL-DECTSAVSV 615
|
...
gi 1834933330 507 ETE 509
Cdd:TIGR00954 616 DVE 618
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
331-558 |
2.85e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.32 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 331 ADDTLALNKVNVSYGESQ--TPTLKDITFSVHGFQKVGIIGASGSGKST-------LINTLGGFLSPQDGQINVRDTAVP 401
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQqkIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 402 HLDKQAWQR-------SFVYIPQAP-------YLFHASLRDNLAFYAPGASEEAVmqAAAKAGLTDwiATLPDGlATQIG 467
Cdd:PRK10261 89 ELSEQSAAQmrhvrgaDMAMIFQEPmtslnpvFTVGEQIAESIRLHQGASREEAM--VEAKRMLDQ--VRIPEA-QTILS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 468 EGARGVSGGQAQRIALARAfLDDSRRVLLFDEPTAHLDIETEVELKRaMLPVFDHHL---VFFATHRLHWMNEM-DYILV 543
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMA-LSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQKEMsmgVIFITHDMGVVAEIaDRVLV 241
|
250
....*....|....*
gi 1834933330 544 MDHGKIVQQGTPAEL 558
Cdd:PRK10261 242 MYQGEAVETGSVEQI 256
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
352-551 |
5.84e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQInvrdtavpHLDKQawqrsfvyipqaPYLFhASLRDNLA 431
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI--------LIDGQ------------EMRF-ASTTAALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 432 ----------FYAPgasEEAVM------QAAAKAGLTD------WIATLPDGLATQIGEGA--RGVSGGQAQRIALARAF 487
Cdd:PRK11288 79 agvaiiyqelHLVP---EMTVAenlylgQLPHKGGIVNrrllnyEAREQLEHLGVDIDPDTplKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 488 LDDSrRVLLFDEPTAHLDI-ETEV------ELK---RAMLPVfdhhlvffaTHRlhwMNEM----DYILVMDHGKIVQ 551
Cdd:PRK11288 156 ARNA-RVIAFDEPTSSLSArEIEQlfrvirELRaegRVILYV---------SHR---MEEIfalcDAITVFKDGRYVA 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
352-562 |
7.62e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLD-KQAWQRSFVYIPQAPYLFHA-SLRDN 429
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 430 LafYAPGASEEAVMqaaaKAGLTDW--------IATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSrRVLLFDEPT 501
Cdd:PRK09700 101 L--YIGRHLTKKVC----GVNIIDWremrvraaMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA-KVIIMDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 502 AHLdIETEVELKRAMLPVF--DHHLVFFATHRLHWMNEM-DYILVMDHGKIVQQGTPAELEQQG 562
Cdd:PRK09700 174 SSL-TNKEVDYLFLIMNQLrkEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDVSNDD 236
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
341-517 |
1.13e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 341 NVSYGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDtavpHLDkqawqrsFVYIPQapy 420
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGT----KLE-------VAYFDQ--- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 421 lFHASL------RDNLAfyaPGASEeaVMQAAAK----AGLTDWI-----ATLPdglatqigegARGVSGGQAQRIALAR 485
Cdd:PRK11147 390 -HRAELdpektvMDNLA---EGKQE--VMVNGRPrhvlGYLQDFLfhpkrAMTP----------VKALSGGERNRLLLAR 453
|
170 180 190
....*....|....*....|....*....|..
gi 1834933330 486 AFLDDSRrVLLFDEPTAHLDIETeVELKRAML 517
Cdd:PRK11147 454 LFLKPSN-LLILDEPTNDLDVET-LELLEELL 483
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
352-514 |
1.37e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTL--------GGFLSPQDGQINVRDTAVPHLDKQAWQ------RSFVYIPQ 417
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLkneisadgGSYTFPGNWQLAWVNQETPALPQPALEyvidgdREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 418 ApyLFHASLRDNLAFYAPGASEEAVMQA---AAKAgltdwiATLPDGLA---TQIGEGARGVSGGQAQRIALARAFLDDS 491
Cdd:PRK10636 97 Q--LHDANERNDGHAIATIHGKLDAIDAwtiRSRA------ASLLHGLGfsnEQLERPVSDFSGGWRMRLNLAQALICRS 168
|
170 180
....*....|....*....|...
gi 1834933330 492 RrVLLFDEPTAHLDIETEVELKR 514
Cdd:PRK10636 169 D-LLLLDEPTNHLDLDAVIWLEK 190
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
366-508 |
1.39e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.05 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 366 GIIGASGSGKSTLINTLGGFLSPQDGQI----NVRdtavphLDKQAwQRSFVY----IPQAPYLFHASL------RDnlA 431
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVsldpNER------LGKLR-QDQFAFeeftVLDTVIMGHTELwevkqeRD--R 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 432 FYA-PGASEEAVMQAA---------------AKAG---LTDWIAT-LPDGLATQigegargVSGGQAQRIALARAFLDDS 491
Cdd:PRK15064 102 IYAlPEMSEEDGMKVAdlevkfaemdgytaeARAGellLGVGIPEeQHYGLMSE-------VAPGWKLRVLLAQALFSNP 174
|
170
....*....|....*..
gi 1834933330 492 rRVLLFDEPTAHLDIET 508
Cdd:PRK15064 175 -DILLLDEPTNNLDINT 190
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
15-292 |
1.49e-06 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 50.14 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 15 AAAIMAVLTFVQAFmiifqakYLSVAIVNLWQLKSVRTIVLPLLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFM 94
Cdd:cd18570 10 LSLLITLLGIAGSF-------FFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 95 AKLFDLGPSVVAQKGTGNVVTMgLEGIDKIQTYLMLIIGKVLDLSLTPWIVLIYIAFIQWKeaLFLLAIYPLIIFFMIIL 174
Cdd:cd18570 83 KHLLKLPLSFFETRKTGEIISR-FNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWK--LFLITLLIIPLYILIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 175 GLaaqakaDRQYAGYQR--------LSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMSTLTIAMTSTFALDF 246
Cdd:cd18570 160 LF------NKPFKKKNRevmesnaeLNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1834933330 247 FTTLSIAIIavfLGFG---LMNNTIQLLPALIILTLAPDYFAPIRNFAN 292
Cdd:cd18570 234 ISLIGSLLI---LWIGsylVIKGQLSLGQLIAFNALLGYFLGPIENLIN 279
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
365-516 |
1.61e-06 |
|
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: 50.94 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 365 VGIIGASGSGKSTLINTLGGFLSPQDGQInvrDTAVphldkqawqrSFVYIPQapYL---FHASLRDNLAFYAPGASEEA 441
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDL----------KISYKPQ--YIspdYDGTVEEFLRSANTDDFGSS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 442 VMQaaakagltdwiatlpdglaTQIGEG----------ARGVSGGQAQRIALARAFLDDSRrVLLFDEPTAHLDIETEVE 511
Cdd:COG1245 434 YYK-------------------TEIIKPlgleklldknVKDLSGGELQRVAIAACLSRDAD-LYLLDEPSAHLDVEQRLA 493
|
....*
gi 1834933330 512 LKRAM 516
Cdd:COG1245 494 VAKAI 498
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
337-508 |
1.79e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 337 LNKVNVSYGeSQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAvphldkqawqrSFVYIP 416
Cdd:PRK11819 9 MNRVSKVVP-PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGI-----------KVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 417 QAPYLFHA-SLRDNL---------------AFYAPGASEEAVMQAAAK--AGLTDWIATLpDG--LATQI---------- 466
Cdd:PRK11819 77 QEPQLDPEkTVRENVeegvaevkaaldrfnEIYAAYAEPDADFDALAAeqGELQEIIDAA-DAwdLDSQLeiamdalrcp 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1834933330 467 -GEGARGV-SGGQAQRIALARAFLD--DsrrVLLFDEPTAHLDIET 508
Cdd:PRK11819 156 pWDAKVTKlSGGERRRVALCRLLLEkpD---MLLLDEPTNHLDAES 198
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
346-558 |
1.88e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 49.70 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 346 ESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPqdgqiNVRDTA-VPHLDKQAWQ------RSFVYIPQA 418
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA-----GVRQTAgRVLLDGKPVApcalrgRKIATIMQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 419 P-------YLFHASLRDNLAFYAPGASEEAVMQAAAKAGLTDwIATLPDGLATQIgegargvSGGQAQRIALARAFLDDS 491
Cdd:PRK10418 88 PrsafnplHTMHTHARETCLALGKPADDATLTAALEAVGLEN-AARVLKLYPFEM-------SGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834933330 492 RrVLLFDEPTAHLDIETEVE-LKRAMLPVFDHHL-VFFATH------RLhwmneMDYILVMDHGKIVQQGTPAEL 558
Cdd:PRK10418 160 P-FIIADEPTTDLDVVAQARiLDLLESIVQKRALgMLLVTHdmgvvaRL-----ADDVAVMSHGRIVEQGDVETL 228
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
363-531 |
2.06e-06 |
|
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: 47.75 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 363 QKVGIIGASGSGKSTLINTLGGFLSPQDGqinvrdtavphldkqawqrSFVYIPqapylfhaslrdnlafyapgaseeav 442
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGG-------------------GVIYID-------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 443 mqaaakaglTDWIATLPDGLATQIGEGARGVSGGQAQRIALARAFLDDSR-RVLLFDEPTAHLDIETEVELKRAMLPVFD 521
Cdd:smart00382 38 ---------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKpDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170
....*....|....*..
gi 1834933330 522 HHL-------VFFATHR 531
Cdd:smart00382 109 LLLkseknltVILTTND 125
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
57-270 |
2.28e-06 |
|
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: 49.43 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 57 LLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVL 136
Cdd:cd18563 46 VLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 137 DLSLTPWIVLIYIAFIQWKEALFLLAIYPLIIFFMIILGLAAQAKADRQYAGYQRLSNHFVDTLRGLPTLKQLGLNKTYA 216
Cdd:cd18563 126 TNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREI 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 217 DNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTLSIAIIAVFLGFGLMNNTIQL 270
Cdd:cd18563 206 KRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTL 259
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
351-516 |
2.32e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 351 TLKDITFSVHGFQKVG----IIGASGSGKSTLINTLG----GFLSPQDGQINVrDTAVPHLDKQAWQRSFVYIPQAPYLF 422
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGeltvVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITY-DGITPEEIKKHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 423 -HASLRDNLAFYA----PGASEEAVMQAAAKAGLTDWIATLPdGLA----TQIG-EGARGVSGGQAQRIALARAFLDDSr 492
Cdd:TIGR00956 151 pHLTVGETLDFAArcktPQNRPDGVSREEYAKHIADVYMATY-GLShtrnTKVGnDFVRGVSGGERKRVSIAEASLGGA- 228
|
170 180
....*....|....*....|....
gi 1834933330 493 RVLLFDEPTAHLDIETEVELKRAM 516
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRAL 252
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
15-294 |
2.64e-06 |
|
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: 49.31 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 15 AAAIMAVLTFVQAFM--IIFQA--KYLSVAIVNLWQLksVRTIVLPLLLFAGAFLARHLLTLSNNWLlypfVEKTTKTLR 90
Cdd:cd18544 4 ALLLLLLATALELLGplLIKRAidDYIVPGQGDLQGL--LLLALLYLGLLLLSFLLQYLQTYLLQKL----GQRIIYDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 91 KQFMAKLFDLGPSVVAQKGTGNVVT-----------MGLEGIDKIQTYLMLIIGkvldlsltpwiVLIYIAFIQWKEALF 159
Cdd:cd18544 78 RDLFSHIQRLPLSFFDRTPVGRLVTrvtndtealneLFTSGLVTLIGDLLLLIG-----------ILIAMFLLNWRLALI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 160 LLAIYPLIIFFMIILglaaQAKADRQY-AGYQRLS--NHFV-DTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMSTLT 235
Cdd:cd18544 147 SLLVLPLLLLATYLF----RKKSRKAYrEVREKLSrlNAFLqESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIK 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 236 IAMTSTFALDFFTTLSIAIIAVFLGFGLMNNTIQL--LPALIilTLAPDYFAPIRNFANDY 294
Cdd:cd18544 223 LFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLgvLYAFI--QYIQRFFRPIRDLAEKF 281
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
348-508 |
3.89e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 48.47 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 348 QTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFL----SPQD-----GQINVRDTAVPHLDKQAWQRSFVYIPQA 418
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdkSAGShiellGRTVQREGRLARDIRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 419 PYLFHASLRDNLAFYAPGAS--------------EEAVMQAAAKAGLTDW----IATLpdglatqigegargvSGGQAQR 480
Cdd:PRK09984 96 NLVNRLSVLENVLIGALGSTpfwrtcfswftreqKQRALQALTRVGMVHFahqrVSTL---------------SGGQQQR 160
|
170 180
....*....|....*....|....*...
gi 1834933330 481 IALARAFLDDSrRVLLFDEPTAHLDIET 508
Cdd:PRK09984 161 VAIARALMQQA-KVILADEPIASLDPES 187
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
366-562 |
4.07e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 366 GIIGASGSGKSTLINTLGGFLSPQDGQ-------INVRDTAVphldkqawqRSFV-YIPQApylFhaSL------RDNLA 431
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpVDAGDIAT---------RRRVgYMSQA---F--SLygeltvRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 432 FYA------PGASEEAVMQAAAKAGLTDWIATLPDGLatqigegargvSGGQAQRIALARAFLdDSRRVLLFDEPTAHLD 505
Cdd:NF033858 362 LHArlfhlpAAEIAARVAEMLERFDLADVADALPDSL-----------PLGIRQRLSLAVAVI-HKPELLILDEPTSGVD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1834933330 506 -------IETEVELKRAmlpvfDHHLVFFAThrlHWMNEM---DYILVMDHGKIVQQGTPAEL-EQQG 562
Cdd:NF033858 430 pvardmfWRLLIELSRE-----DGVTIFIST---HFMNEAercDRISLMHAGRVLASDTPAALvAARG 489
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
352-393 |
6.67e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.89 E-value: 6.67e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQI 393
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
335-558 |
7.90e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.20 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 335 LALNKVNVSYGESQTP--TLKDITFSVHGFQKVGIIGASGSGKST-------LINtLGGFLSPQDGQINVRD-TAVPHLD 404
Cdd:PRK11022 4 LNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVsslaimgLID-YPGRVMAEKLEFNGQDlQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 405 KQAWQRSFV-YIPQAPYlfhASLrdNLAFYAPGASEEA--VMQAAAKAGLTDWIATL------PDGlATQIGEGARGVSG 475
Cdd:PRK11022 83 RRNLVGAEVaMIFQDPM---TSL--NPCYTVGFQIMEAikVHQGGNKKTRRQRAIDLlnqvgiPDP-ASRLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 476 GQAQRIALARAFLDDSRrVLLFDEPTAHLD-------IETEVELKRA-----MLPVFDHHLVFFATHRlhwmnemdyILV 543
Cdd:PRK11022 157 GMSQRVMIAMAIACRPK-LLIADEPTTALDvtiqaqiIELLLELQQKenmalVLITHDLALVAEAAHK---------IIV 226
|
250
....*....|....*
gi 1834933330 544 MDHGKIVQQGTPAEL 558
Cdd:PRK11022 227 MYAGQVVETGKAHDI 241
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
352-560 |
8.27e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQRsfvyIPqAPYLfhASLRDNLA 431
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNGEPLAA----ID-APRL--ARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 432 FYA----PGASEEAVMQA----AAKAGLTD-------WIATLPDGLATQIGEGARGVSGGQAQRIALARAFL-----DDS 491
Cdd:PRK13547 90 QAAqpafAFSAREIVLLGryphARRAGALThrdgeiaWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwppHDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 492 R---RVLLFDEPTAHLD-------IETEVELKR-----AMLPVFDHHLVffATHrlhwmneMDYILVMDHGKIVQQGTPA 556
Cdd:PRK13547 170 AqppRYLLLDEPTAALDlahqhrlLDTVRRLARdwnlgVLAIVHDPNLA--ARH-------ADRIAMLADGAIVAHGAPA 240
|
....
gi 1834933330 557 ELEQ 560
Cdd:PRK13547 241 DVLT 244
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
352-517 |
8.99e-06 |
|
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: 48.39 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVphldkqawqrsFVYIPQapylFHASLRDNLA 431
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK-----------LAYVDQ----SRDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 432 FY---APGASEEAV----MQAAAKAGLTDWiatlpDGLATQ--IGEgargVSGGQAQRIALARAfLDDSRRVLLFDEPTA 502
Cdd:TIGR03719 403 VWeeiSGGLDIIKLgkreIPSRAYVGRFNF-----KGSDQQkkVGQ----LSGGERNRVHLAKT-LKSGGNVLLLDEPTN 472
|
170
....*....|....*
gi 1834933330 503 HLDIETEVELKRAML 517
Cdd:TIGR03719 473 DLDVETLRALEEALL 487
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
365-506 |
1.22e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.24 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 365 VGIIGASGSGKSTLINTLGGFLSPQDGQINV-----------RDTAV-PHLDKQAWQRSFV-----YIPQAPYLFHASLR 427
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEepswdevlkrfRGTELqDYFKKLANGEIKVahkpqYVDLIPKVFKGTVR 181
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 428 DNLAfyapGASEEAVmqaaakagLTDWIATLpdGLATQIGEGARGVSGGQAQRIALARAFLDDSRrVLLFDEPTAHLDI 506
Cdd:COG1245 182 ELLE----KVDERGK--------LDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDAD-FYFFDEPSSYLDI 245
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
365-505 |
1.44e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.95 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 365 VGIIGASGSGKSTLINTLGGFLSPQD--GQINVRDTavpHLDKQAWQRSFvYIPQAPYLF-HASLRDNLAFYA----PGA 437
Cdd:PLN03211 97 LAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNR---KPTKQILKRTG-FVTQDDILYpHLTVRETLVFCSllrlPKS 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 438 SEEAVMQAAAKAGLTDWiatlpdGLA----TQIGEG-ARGVSGGQAQRIALARAFLDDSrRVLLFDEPTAHLD 505
Cdd:PLN03211 173 LTKQEKILVAESVISEL------GLTkcenTIIGNSfIRGISGGERKRVSIAHEMLINP-SLLILDEPTSGLD 238
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
57-175 |
1.92e-05 |
|
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: 46.71 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 57 LLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVL 136
Cdd:cd18576 39 ALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFL 118
|
90 100 110
....*....|....*....|....*....|....*....
gi 1834933330 137 DLSLTPWIVLIYIAFIQWKEALFLLAIYPLIIFFMIILG 175
Cdd:cd18576 119 RQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFG 157
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
365-516 |
2.25e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 365 VGIIGASGSGKSTLINTLGGFLSPQDGQINvrdtavphldkqaWQR-SFVYIPQAPYLfhaslrdnlafyapgaseeavm 443
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDNDE-------------WDGiTPVYKPQYIDL---------------------- 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 444 qaaakagltdwiatlpdglatqigegargvSGGQAQRIALARAFLDDSRrVLLFDEPTAHLDIETEVELKRAM 516
Cdd:cd03222 73 ------------------------------SGGELQRVAIAAALLRNAT-FYLFDEPSAYLDIEQRLNAARAI 114
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
356-546 |
3.44e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.82 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 356 TFSVHGF------QKVGIIGASGSGKSTLINTLGGFLSPQDGQINVR---DTAVPHLDKQAWQRSFV------------- 413
Cdd:cd03236 14 SFKLHRLpvpregQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPpdwDEILDEFRGSELQNYFTkllegdvkvivkp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 414 -YIPQAPYLFHASLRDNL-AFYAPGASEEAVMQAAAKAGLTDWIATLpdglatqigegargvSGGQAQRIALARAFLDDS 491
Cdd:cd03236 94 qYVDLIPKAVKGKVGELLkKKDERGKLDELVDQLELRHVLDRNIDQL---------------SGGELQRVAIAAALARDA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1834933330 492 RrVLLFDEPTAHLDIETEVELKRAMlpvfdhhlvffatHRLhwMNEMDYILVMDH 546
Cdd:cd03236 159 D-FYFFDEPSSYLDIKQRLNAARLI-------------REL--AEDDNYVLVVEH 197
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
352-399 |
3.47e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 3.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTA 399
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA 87
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
465-558 |
4.91e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 465 QIGEGARGVSGGQAQRIALARAFLDDS--RRVLLFDEPTAHL---DIetevelkRAMLPVFDH-----HLVFFATHRLHW 534
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRStgRTLYILDEPTTGLhfdDI-------KKLLEVLQRlvdkgNTVVVIEHNLDV 894
|
90 100 110
....*....|....*....|....*....|
gi 1834933330 535 MNEMDYILVM-----DH-GKIVQQGTPAEL 558
Cdd:TIGR00630 895 IKTADYIIDLgpeggDGgGTVVASGTPEEV 924
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
352-562 |
1.12e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 43.67 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 352 LKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQ--DGQINVRDTAVPHLDKQAWQRSFVYipqapylfhaslrdn 429
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERARLGIF--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 430 LAFYAPgaseeavmqaAAKAGLT--DWIATLPDGLatqigegargvSGGQAQRIALARAFLDDSRRVLLfDEPTAHLDIE 507
Cdd:cd03217 81 LAFQYP----------PEIPGVKnaDFLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLAIL-DEPDSGLDID 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 508 -----TEV-----ELKRAMLPVfdhhlvffaTHRLHWMNEM--DYILVMDHGKIVQQGTPA---ELEQQG 562
Cdd:cd03217 139 alrlvAEVinklrEEGKSVLII---------THYQRLLDYIkpDRVHVLYDGRIVKSGDKElalEIEKKG 199
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
58-301 |
1.70e-04 |
|
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: 43.68 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 58 LLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTylmLIIGKVLD 137
Cdd:cd18778 44 LLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVER---LIADGIPQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 138 L---SLTPWIVLIYIAFIQWKEALFLLAIYPLIIFFMIILGLAAQAKADRQYAGYQRLSNHFVDTLRGLPTLKQLGLNKT 214
Cdd:cd18778 121 GitnVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 215 YADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTLSIAIIAVFLGFGLMNNTI---QLLPALIILTLapdYFAPIRNFA 291
Cdd:cd18778 201 EAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGELtigDLVAFLLYLGL---FYEPITSLH 277
|
250
....*....|
gi 1834933330 292 NDYHATLNGK 301
Cdd:cd18778 278 GLNEMLQRAL 287
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
144-280 |
1.78e-04 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 43.62 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 144 IVLIYIAFIQWKEALFLLAIYPLIIFFMIILGLAAQAKADRQYAGYQ-RLSNHFVDTLRGLPTLKQLGLNKTYADNVYQV 222
Cdd:cd18585 125 ATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLGKKIGQQLVQLRaELRTELVDGLQGMAELLIFGALERQRQQLEQL 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 223 SEDY--RKKTMSTLTIAMTstfALDFFTTLSIAIIAVFLGFGLMNNTIQ---LLPALIILTLA 280
Cdd:cd18585 205 SDALikEQRRLARLSGLSQ---ALMILLSGLTVWLVLWLGAPLVQNGALdgaLLAMLVFAVLA 264
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
53-270 |
1.88e-04 |
|
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: 43.57 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 53 IVLPLLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLII 132
Cdd:cd18542 38 LWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 133 GKVLDLSLTPWIVLIYIAFIQWKEALFLLAIYPLIIFFMIILGLAAQA---KADRQYAgyqRLSNHFVDTLRGLPTLKQL 209
Cdd:cd18542 118 VELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPafeEIREQEG---ELNTVLQENLTGVRVVKAF 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834933330 210 GLNKTYADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTLSIAIIAVFLGFGLMNNTIQL 270
Cdd:cd18542 195 AREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITL 255
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
365-506 |
2.07e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 365 VGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDK------QAWQRSFV-----------YIPQAPYLFHASLR 427
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRfrgtelQNYFKKLYngeikvvhkpqYVDLIPKVFKGKVR 181
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834933330 428 DnlafyapgaseeaVMQAAAKAGLTDWIATLPdGLATQIGEGARGVSGGQAQRIALARAFLDDSRrVLLFDEPTAHLDI 506
Cdd:PRK13409 182 E-------------LLKKVDERGKLDEVVERL-GLENILDRDISELSGGELQRVAIAAALLRDAD-FYFFDEPTSYLDI 245
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
57-255 |
2.15e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 43.32 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 57 LLLFAGAFLA----RHLLTLSNNWLLYPFVEKTTKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGiDKIQTYLM-LI 131
Cdd:cd18568 41 LNLILIGLLIvgifQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLTrSA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 132 IGKVLDLsLTPWIVLIYIAFIQWKEALFLLAIYPLIIFFMIILGLAAQAKADRQYAGYQRLSNHFVDTLRGLPTLKQLGL 211
Cdd:cd18568 120 LTTILDL-LMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1834933330 212 NKTYADnvyQVSEDYRK---KTMSTLTIAMTSTFALDFFTTLSIAII 255
Cdd:cd18568 199 ERPIRW---RWENKFAKalnTRFRGQKLSIVLQLISSLINHLGTIAV 242
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
474-565 |
2.51e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 474 SGGQAQRIALARaFLddSRR-----VLLFDEPTAHL---DIetevelkramlpvfdHHL--VFfatHRL----------- 532
Cdd:COG0178 828 SGGEAQRVKLAS-EL--SKRstgktLYILDEPTTGLhfhDI---------------RKLleVL---HRLvdkgntvvvie 886
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1834933330 533 HwmNeMDYILVMDH------------GKIVQQGTPAELEQQGGTY 565
Cdd:COG0178 887 H--N-LDVIKTADWiidlgpeggdggGEIVAEGTPEEVAKVKASY 928
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
365-508 |
2.93e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 365 VGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAvphldKQAwqrsfvYIPQApylfhaslRDNLafyapgASEEAVMQ 444
Cdd:PRK11819 353 VGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV-----KLA------YVDQS--------RDAL------DPNKTVWE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 445 AAakAGLTDWIatlpdglatQIGE------------GARG---------VSGGQAQRIALARAfLDDSRRVLLFDEPTAH 503
Cdd:PRK11819 408 EI--SGGLDII---------KVGNreipsrayvgrfNFKGgdqqkkvgvLSGGERNRLHLAKT-LKQGGNVLLLDEPTND 475
|
....*
gi 1834933330 504 LDIET 508
Cdd:PRK11819 476 LDVET 480
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
474-577 |
2.98e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.54 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 474 SGGQAQRIALARAFLDDSrRVLLFDEPTAHLDIETEV-------ELKRAMlpvfdHHLVFFATHRLHWMNEM-DYILVMD 545
Cdd:PRK15134 158 SGGERQRVMIAMALLTRP-ELLIADEPTTALDVSVQAqilqllrELQQEL-----NMGLLFITHNLSIVRKLaDRVAVMQ 231
|
90 100 110
....*....|....*....|....*....|....*
gi 1834933330 546 HGKIVQQGTPAEL---EQQGGTYVRLRSEMEGATV 577
Cdd:PRK15134 232 NGRCVEQNRAATLfsaPTHPYTQKLLNSEPSGDPV 266
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
15-280 |
3.25e-04 |
|
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: 42.85 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 15 AAAIMAVLTFVQAFMIIFQAKYLSVAIVNLWQLKSVRTIVLPLL-LFAGAFLARHLLTLSnnWLLypFVEKTTKTLRKQF 93
Cdd:cd18577 11 AGAALPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYFVyLGIGSFVLSYIQTAC--WTI--TGERQARRIRKRY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 94 MAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVL-DLSLTpwIVLIYIAFI-QWKEALFLLAIYPLIIFFM 171
Cdd:cd18577 87 LKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIqSLSTF--IAGFIIAFIySWKLTLVLLATLPLIAIVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 172 IILGLAAQAKADRQYAGYQRLSNHFVDTLRGLPTLKQLGLNKT----YADNVYQVSEDYRKK------TMSTLTIAMTST 241
Cdd:cd18577 165 GIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKeikrYSKALEKARKAGIKKglvsglGLGLLFFIIFAM 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1834933330 242 FALDFF--TTLSIA-------IIAVFL-----GFGLMnntiQLLPALIILTLA 280
Cdd:cd18577 245 YALAFWygSRLVRDgeispgdVLTVFFavligAFSLG----QIAPNLQAFAKA 293
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
17-270 |
5.32e-04 |
|
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: 42.39 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 17 AIMAVLTFVQAFMIIFQAKYLSVAIVNLWQLKSVRT------IVLPLLLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLR 90
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGgvdfsgLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 91 KQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLDLSLTPWIVLIYIAFIQWKEALFLLAIYPLIIFF 170
Cdd:cd18547 82 KDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 171 MIILGLAAQAKADRQYAGYQRLSNHFVDTLRGLPTLKQLGLNKTYADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTTL 250
Cdd:cd18547 162 TKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINNL 241
|
250 260
....*....|....*....|
gi 1834933330 251 SIAIIAVFLGFGLMNNTIQL 270
Cdd:cd18547 242 GYVLVAVVGGLLVINGALTV 261
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
291-505 |
1.08e-03 |
|
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: 42.31 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 291 ANDYHATLNGKNTLTAVLD---------ILQRPTPTDRDLL-PVRQPTWQADDTLA-----------------LNKVNVS 343
Cdd:TIGR01257 1867 ANPFQWDLIGKNLVAMAVEgvvyflltlLIQHHFFLSRWIAePAKEPIFDEDDDVAeerqriisggnktdilrLNELTKV 1946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 344 YGESQTPTLKDITFSVHGFQKVGIIGASGSGKSTLINTLGGFLSPQDGQINVRDTAVPHLDKQAWQrSFVYIPQapylFH 423
Cdd:TIGR01257 1947 YSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQ-NMGYCPQ----FD 2021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 424 A-----SLRDNLAFYA--PGASEEAVMQaaakagLTDW-IATLpdGLATQIGEGARGVSGGQAQRIALARAfLDDSRRVL 495
Cdd:TIGR01257 2022 AiddllTGREHLYLYArlRGVPAEEIEK------VANWsIQSL--GLSLYADRLAGTYSGGNKRKLSTAIA-LIGCPPLV 2092
|
250
....*....|
gi 1834933330 496 LFDEPTAHLD 505
Cdd:TIGR01257 2093 LLDEPTTGMD 2102
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
58-264 |
1.38e-03 |
|
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: 41.01 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 58 LLFAGAFLARHLLTLSNNWLLYPFVEKTTKTLRKQFMAKLFDLGPSVVAQKGTGNVVTMGLEGIDKIQTYLMLIIGKVLD 137
Cdd:cd18565 58 GLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 138 LSLTPWIVLIYIAFIQWKEALFLLAIYPLIIFFMIILGLAAQAKAD--RQYAGyqRLSNHFVDTLRGLPTLKQLGLNKTY 215
Cdd:cd18565 138 VVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRavREAVG--DLNARLENNLSGIAVIKAFTAEDFE 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1834933330 216 ADNVYQVSEDYRKKTMSTLTIAMTSTFALDFFTtlSIAIIAVFLGFGLM 264
Cdd:cd18565 216 RERVADASEEYRDANWRAIRLRAAFFPVIRLVA--GAGFVATFVVGGYW 262
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
462-569 |
2.90e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.10 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834933330 462 LATQIGEGARGVSGGQAQRIALARAFLDDSRrVLLFDEPTAHLDIETEVEL---KRAMlpVFDHHLVFFATHRLHWMNEM 538
Cdd:NF000106 134 LTEAAGRAAAKYSGGMRRRLDLAASMIGRPA-VLYLDEPTTGLDPRTRNEVwdeVRSM--VRDGATVLLTTQYMEEAEQL 210
|
90 100 110
....*....|....*....|....*....|...
gi 1834933330 539 DYIL-VMDHGKIVQQGTPAELEQQ-GGTYVRLR 569
Cdd:NF000106 211 AHELtVIDRGRVIADGKVDELKTKvGGRTLQIR 243
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
364-411 |
4.84e-03 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 38.16 E-value: 4.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1834933330 364 KVGIIGASGSGKSTLINTLGgflspqdgqiNVRDTAVPHLDK----QAWQRS 411
Cdd:PRK07261 2 KIAIIGYSGSGKSTLARKLS----------QHYNCPVLHLDTlhfqPNWQER 43
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
364-382 |
4.98e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 37.21 E-value: 4.98e-03
|
| PRK08118 |
PRK08118 |
DNA topology modulation protein; |
363-416 |
5.08e-03 |
|
DNA topology modulation protein;
Pssm-ID: 181235 Cd Length: 167 Bit Score: 38.05 E-value: 5.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1834933330 363 QKVGIIGASGSGKSTLINTLGGFLspqdgqinvrDTAVPHLDKQAWQRSFVYIP 416
Cdd:PRK08118 2 KKIILIGSGGSGKSTLARQLGEKL----------NIPVHHLDALFWKPNWEGVP 45
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
474-506 |
6.18e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 6.18e-03
10 20 30
....*....|....*....|....*....|....
gi 1834933330 474 SGGQAQRIALARA-FLDDSrrVLLFDEPTAHLDI 506
Cdd:PLN03073 346 SGGWRMRIALARAlFIEPD--LLLLDEPTNHLDL 377
|
|
| CDC_Septin |
cd01850 |
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ... |
361-382 |
9.56e-03 |
|
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.
Pssm-ID: 206649 Cd Length: 275 Bit Score: 38.30 E-value: 9.56e-03
|
| |
