|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-592 |
0e+00 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 1231.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 1 MRKLGTMWPTLKRLLAYGSPWRKPLSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVAGLGVAYVGLQLAAAG 80
Cdd:PRK10790 1 MRSFSQLWPTLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVAGLAAAYVGLQLLAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 81 LHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAM 160
Cdd:PRK10790 81 LHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 161 FSLDWRMALVAITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMA 240
Cdd:PRK10790 161 FSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 241 RMQTLRLDGFLLRPLLSLFSALVLCGLLMLFGLSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFE 320
Cdd:PRK10790 241 RMQTLRLDGFLLRPLLSLFSALILCGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 321 LMDRPRQAYGHDERPLQSGAIAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRL 400
Cdd:PRK10790 321 LMDGPRQQYGNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 401 DGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVG 480
Cdd:PRK10790 401 DGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 481 QKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRE 560
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQ 560
|
570 580 590
....*....|....*....|....*....|..
gi 1541475627 561 LLEAKGRYWQMYQLQLAGEELAASVREEESLS 592
Cdd:PRK10790 561 LLAAQGRYWQMYQLQLAGEELAASVREEESLS 592
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-579 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 575.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 1 MRKlgTMWPTLKRLLAYGSPWRKPLSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSylPLRLVAGLGVAYVGLQLAAAG 80
Cdd:COG1132 1 MSK--SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG--DLSALLLLLLLLLGLALLRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 81 LHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAM 160
Cdd:COG1132 77 LSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 161 FSLDWRMALVAITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMA 240
Cdd:COG1132 157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 241 RMQTLRLDGfLLRPLLSLFSALVLCGLLMLFG-LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVF 319
Cdd:COG1132 237 NLRAARLSA-LFFPLMELLGNLGLALVLLVGGlLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 320 ELMDRPRQ-AYGHDERPLQ--SGAIAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQG 396
Cdd:COG1132 316 ELLDEPPEiPDPPGAVPLPpvRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 397 EIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGR-DYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGN 475
Cdd:COG1132 396 RILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 476 NLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVER 555
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
570 580
....*....|....*....|....
gi 1541475627 556 GTHRELLEAKGRYWQMYQLQLAGE 579
Cdd:COG1132 556 GTHEELLARGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-576 |
6.58e-128 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 391.89 E-value: 6.58e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 10 TLKRLLAYGSPWRKPLSVAVLLLWIAAIAEVSGPLLISYFIDN-MVAKSYLPLR-LVAGLGVAYvglqLAAAGLHYAQSL 87
Cdd:COG2274 143 GLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRvLPNQDLSTLWvLAIGLLLAL----LFEGLLRLLRSY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 88 LFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVtNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRM 167
Cdd:COG2274 219 LLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 168 ALVAITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRL 247
Cdd:COG2274 298 ALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 248 dGFLLRPLLSLFSALVLCGLLML-FGLSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDRPR 326
Cdd:COG2274 378 -SNLLSTLSGLLQQLATVALLWLgAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 327 QAYGHD---ERPLQSGAIAFDNVSFAYRED-RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDG 402
Cdd:COG2274 457 EREEGRsklSLPRLKGDIELENVSFRYPGDsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 403 RPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGR-DYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQ 481
Cdd:COG2274 537 IDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDpDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQ 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 482 KQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHREL 561
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
570
....*....|....*
gi 1541475627 562 LEAKGRYWQMYQLQL 576
Cdd:COG2274 697 LARKGLYAELVQQQL 711
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-566 |
3.96e-112 |
|
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: 346.36 E-value: 3.96e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 12 KRLLAYGSPWRKPLSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSyLPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNR 91
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGG-APLSALLPLLGLLLAVLLLRALLAWLRERAAFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 92 AAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVA 171
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 172 ITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLdGFL 251
Cdd:COG4988 165 LVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRV-AFL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 252 LRPLLSLFSALVLCGLLMLFGLSSSG---TIEVGVLYAFIS---YLgrlnePLIELTTQ--QSMlqQAVVAGERVFELMD 323
Cdd:COG4988 244 SSAVLEFFASLSIALVAVYIGFRLLGgslTLFAALFVLLLApefFL-----PLRDLGSFyhARA--NGIAAAEKIFALLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 324 RPRQAYGHDERPL---QSGAIAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRL 400
Cdd:COG4988 317 APEPAAPAGTAPLpaaGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 401 DGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGR-DYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSV 479
Cdd:COG4988 397 NGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 480 GQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHR 559
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHE 556
|
....*..
gi 1541475627 560 ELLEAKG 566
Cdd:COG4988 557 ELLAKNG 563
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
10-577 |
2.06e-106 |
|
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: 331.68 E-value: 2.06e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 10 TLKRLLAYGSPWRKPLSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVAGLGVayVGLQLAAAGLHYAQSLLF 89
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVV--IGLAVLRGICSFVSTYLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 90 NRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMAL 169
Cdd:TIGR02203 79 SWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 170 VAITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDG 249
Cdd:TIGR02203 159 IVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 250 fLLRPLLSLFSALVLCGLLMLFG-LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDRPRQA 328
Cdd:TIGR02203 239 -ISSPITQLIASLALAVVLFIALfQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 329 -YGHDERPLQSGAIAFDNVSFAYR-EDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLA 406
Cdd:TIGR02203 318 dTGTRAIERARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 407 SLSHNVLRKGVAMVQQDPVVLADTFYANVTLGR--DYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQL 484
Cdd:TIGR02203 398 DYTLASLRRQVALVSQDVVLFNDTIANNIAYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 485 LALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEA 564
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
570
....*....|...
gi 1541475627 565 KGRYWQMYQLQLA 577
Cdd:TIGR02203 558 NGLYAQLHNMQFR 570
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
25-318 |
1.09e-105 |
|
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: 320.10 E-value: 1.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 105 MDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMII 184
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 185 YQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGfLLRPLLSLFSALVL 264
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFA-LFRPLVELLSSLAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 265 CGLLMLFGLSS-SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18544 240 ALVLWYGGGQVlSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-587 |
1.01e-100 |
|
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: 317.92 E-value: 1.01e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 6 TMWPTLKRLLAYGSPWRKPLSV--AVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVA---GLGVAYVGLQLAAAG 80
Cdd:COG5265 14 PRLDLLLRLLLLLLLPPYLRRRrrALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVvpvGLLLAYGLLRLLSVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 81 LHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSeFDIQ----PVGQVISRVTNDTE-VIRDLYVTVVATVLRsAALIGA 155
Cdd:COG5265 94 FGELRDALFARVTQRAVRRLALEVFRHLHALSLR-FHLErqtgGLSRDIERGTKGIEfLLRFLLFNILPTLLE-IALVAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 156 MLVAMFslDWRMALVaitifpaVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEViNGMSV--------IQQFRQQARFG 227
Cdd:COG5265 172 ILLVKY--DWWFALI-------TLVTVVLYIAFTVVVTEWRTKFRREMNEADSEA-NTRAVdsllnyetVKYFGNEAREA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 228 ERMGEAsrshyMARMQTLRLdgfllRPLLSLF------SALVLCGLLMLFGLS----SSGTIEVGVLYAFISYLGRLNEP 297
Cdd:COG5265 242 RRYDEA-----LARYERAAV-----KSQTSLAllnfgqALIIALGLTAMMLMAaqgvVAGTMTVGDFVLVNAYLIQLYIP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 298 LIELTTQQSMLQQAVVAGERVFELMDRPRQAYGH-DERPLQS--GAIAFDNVSFAYREDRLVLQDITLDVPSRGFVALVG 374
Cdd:COG5265 312 LNFLGFVYREIRQALADMERMFDLLDQPPEVADApDAPPLVVggGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 375 HTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGR-DYSQEQVWEVLEKV 453
Cdd:COG5265 392 PSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRpDASEEEVEAAARAA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 454 QLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAV-RDHTTLVvIA 532
Cdd:COG5265 472 QIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVaRGRTTLV-IA 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 533 HRLSTIVDADTILVLHRGQAVERGTHRELLEAKGRYWQMYQLQLAGEELAASVRE 587
Cdd:COG5265 551 HRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEALAA 605
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
10-574 |
2.96e-98 |
|
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: 310.54 E-value: 2.96e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 10 TLKRLLAYGSPWRKPLSVAVLLLWIAAIAEVSgpLLI--SYFIdnmVAKSYLPLrlVAGLGVAYVGLQLAA---AGLHYA 84
Cdd:COG4987 2 DLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIG--LLAlsGWLI---AAAALAPP--ILNLFVPIVGVRAFAigrTVFRYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 85 QSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLD 164
Cdd:COG4987 75 ERLVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 165 WRMALV-AITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQ 243
Cdd:COG4987 155 PALALVlALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 244 TLRLDGfLLRPLLSLFSAL-VLCGLLMLFGLSSSGTIEVGVLYAFI-SYLGrLNEPLIELTTQQSMLQQAVVAGERVFEL 321
Cdd:COG4987 235 LARLSA-LAQALLQLAAGLaVVAVLWLAAPLVAAGALSGPLLALLVlAALA-LFEALAPLPAAAQHLGRVRAAARRLNEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 322 MDRPRQAY--GHDERPLQSGAIAFDNVSFAYR-EDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEI 398
Cdd:COG4987 313 LDAPPAVTepAEPAPAPGGPSLELEDVSFRYPgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 399 RLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGR-DYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNL 477
Cdd:COG4987 393 TLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARpDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 478 SVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGT 557
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
570
....*....|....*..
gi 1541475627 558 HRELLEAKGRYWQMYQL 574
Cdd:COG4987 553 HEELLAQNGRYRQLYQR 569
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
339-566 |
1.80e-97 |
|
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: 296.44 E-value: 1.80e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 339 GAIAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVA 418
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 419 MVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEK-VQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQV 497
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKeAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 498 LILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEAKG 566
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
9-571 |
3.00e-91 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 296.25 E-value: 3.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 9 PTLKRLLAYGSPWRKPLSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLP--LRLVAGLGVayvgLQLAAAGLHYAQS 86
Cdd:TIGR00958 147 DLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPalASAIFFMCL----LSIASSVSAGLRG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 87 LLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWR 166
Cdd:TIGR00958 223 GSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPR 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 167 MALVAITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQF----RQQARFGERMgeaSRSHYMARM 242
Cdd:TIGR00958 303 LTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFaaeeGEASRFKEAL---EETLQLNKR 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 243 QTLRLDGFLLrpLLSLFSALVLCGLLMLFG-LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFEL 321
Cdd:TIGR00958 380 KALAYAGYLW--TTSVLGMLIQVLVLYYGGqLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 322 MDRPRQ-------AYGHDErplqsGAIAFDNVSFAY--REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYP 392
Cdd:TIGR00958 458 LDRKPNipltgtlAPLNLE-----GLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 393 VTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLG-RDYSQEQVWEVLEKVQLADLARGFSDGINTRLG 471
Cdd:TIGR00958 533 PTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVG 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 472 EQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAavRDHTTLVVIAHRLSTIVDADTILVLHRGQ 551
Cdd:TIGR00958 613 EKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGS 690
|
570 580
....*....|....*....|
gi 1541475627 552 AVERGTHRELLEAKGRYWQM 571
Cdd:TIGR00958 691 VVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-576 |
2.59e-86 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 279.60 E-value: 2.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 8 WPTLKRLLAYGSPWRKPLSVAVLLLWIAAIAEVS-----GPLLISYF--IDNMVAKsYLPLrlvaglgvAYVGLQLAAAG 80
Cdd:PRK11176 10 WQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFmlsllKPLLDDGFgkADRSVLK-WMPL--------VVIGLMILRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 81 LHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAM 160
Cdd:PRK11176 81 TSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 161 FSLDWRMALVAITIFPAVLIVM-IIYQRYSTpIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASrsHYM 239
Cdd:PRK11176 161 FYYSWQLSLILIVIAPIVSIAIrVVSKRFRN-ISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVS--NRM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 240 aRMQTLRL---DGfLLRPLLSLFSALVLCGLLMLFGLSS------SGTIEVgvlyAFISYLGrLNEPLIELTTQQSMLQQ 310
Cdd:PRK11176 238 -RQQGMKMvsaSS-ISDPIIQLIASLALAFVLYAASFPSvmdtltAGTITV----VFSSMIA-LMRPLKSLTNVNAQFQR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 311 AVVAGERVFELMD-RPRQAYGHDERPLQSGAIAFDNVSFAYRE-DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLM 388
Cdd:PRK11176 311 GMAACQTLFAILDlEQEKDEGKRVIERAKGDIEFRNVTFTYPGkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 389 GYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGRD--YSQEQVWEVLEKVQLADLARGFSDGI 466
Cdd:PRK11176 391 RFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeqYSREQIEEAARMAYAMDFINKMDNGL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 467 NTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILV 546
Cdd:PRK11176 471 DTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILV 550
|
570 580 590
....*....|....*....|....*....|
gi 1541475627 547 LHRGQAVERGTHRELLEAKGRYWQMYQLQL 576
Cdd:PRK11176 551 VEDGEIVERGTHAELLAQNGVYAQLHKMQF 580
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
341-575 |
6.83e-84 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 261.78 E-value: 6.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMV 420
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDPVVLADTFYANVTLGR-DYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLI 499
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 500 LDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEAKGRYWQMYQLQ 575
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
11-576 |
8.28e-83 |
|
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: 270.42 E-value: 8.28e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 11 LKRLLAYGSPWRKPLSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPL--RLVAGLGVAYVGLQLAAAGLHYAQSLL 88
Cdd:TIGR02204 6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLlnRYFAFLLVVALVLALGTAARFYLVTWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 89 FNRaavgVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMA 168
Cdd:TIGR02204 86 GER----VVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 169 LVAITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLD 248
Cdd:TIGR02204 162 SLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 249 GFLLRPLLSL-FSALVLC----GLLMLFGLSSSGTIEVGVLYAFIS--YLGRLNEPLIELttqqsmlQQAVVAGERVFEL 321
Cdd:TIGR02204 242 ALLTAIVIVLvFGAIVGVlwvgAHDVIAGKMSAGTLGQFVFYAVMVagSIGTLSEVWGEL-------QRAAGAAERLIEL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 322 MdrprQAYGHDERPLQ--------SGAIAFDNVSFAY--REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYY 391
Cdd:TIGR02204 315 L----QAEPDIKAPAHpktlpvplRGEIEFEQVNFAYpaRPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 392 PVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGR-DYSQEQVWEVLEKVQLADLARGFSDGINTRL 470
Cdd:TIGR02204 391 DPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRpDATDEEVEAAARAAHAHEFISALPEGYDTYL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 471 GEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRG 550
Cdd:TIGR02204 471 GERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQG 550
|
570 580
....*....|....*....|....*.
gi 1541475627 551 QAVERGTHRELLEAKGRYWQMYQLQL 576
Cdd:TIGR02204 551 RIVAQGTHAELIAKGGLYARLARLQF 576
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
341-572 |
7.93e-77 |
|
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: 243.29 E-value: 7.93e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRED-RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAM 419
Cdd:cd03251 1 VEFKNVTFRYPGDgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDPVVLADTFYANVTLGR-DYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVL 498
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 499 ILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEAKGRYWQMY 572
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
341-575 |
1.18e-76 |
|
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: 243.22 E-value: 1.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAY--REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVA 418
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 419 MVQQDPVVLADTFYANVTLGRDY-SQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQV 497
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 498 LILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEAKGRYWQMYQLQ 575
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-547 |
1.86e-75 |
|
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: 249.51 E-value: 1.86e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 22 RKPLSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSyLPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLR 101
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQAWLLARVVDGLISAG-EPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 102 TDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIrDLYVTVVATVLRSAALIG-AMLVAMFSLDWRMALVAITIFPAVLI 180
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEAL-DGYFARYLPQLVLAVIVPlAILAAVFPQDWISGLILLLTAPLIPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 181 VMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLdGFLLRPLLSLFS 260
Cdd:TIGR02857 160 FMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRI-AFLSSAVLELFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 261 AL------VLCGLLMLFGLSSSGTIEVGVLYAFISYLgrlnePLIELTTQQSMLQQAVVAGERVFELMDRPRQAyGHDER 334
Cdd:TIGR02857 239 TLsvalvaVYIGFRLLAGDLDLATGLFVLLLAPEFYL-----PLRQLGAQYHARADGVAAAEALFAVLDAAPRP-LAGKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 335 PL---QSGAIAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHN 411
Cdd:TIGR02857 313 PVtaaPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 412 VLRKGVAMVQQDPVVLADTFYANVTLGR-DYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARV 490
Cdd:TIGR02857 393 SWRDQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARA 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 491 LIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVL 547
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
339-557 |
1.84e-72 |
|
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: 231.61 E-value: 1.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 339 GAIAFDNVSFAYRED-RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGV 417
Cdd:cd03244 1 GDIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 418 AMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQV 497
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 498 LILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGT 557
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
109-568 |
1.93e-67 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 232.53 E-value: 1.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 109 LRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLrSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMIIYQRY 188
Cdd:TIGR03796 238 LRLPVRFFAQRHAGDIASRVQLNDQVAEFLSGQLATTAL-DAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 189 STPIVRRVRAYLADINdgfNEVINGMSVIQQFRqqARFGERMGEASRSHYMAR----MQTLRLDGFLLRPLLSLFSALVL 264
Cdd:TIGR03796 317 RVDANRRLQQDAGKLT---GVAISGLQSIETLK--ASGLESDFFSRWAGYQAKllnaQQELGVLTQILGVLPTLLTSLNS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 265 CGLLMLFGLSS-SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDRPR---------QAYGHDER 334
Cdd:TIGR03796 392 ALILVVGGLRVmEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRNPVdplleepegSAATSEPP 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 335 PLQSGAIAFDNVSFAY-REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL 413
Cdd:TIGR03796 472 RRLSGYVELRNITFGYsPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 414 RKGVAMVQQDPVVLADTFYANVTL-GRDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLI 492
Cdd:TIGR03796 552 ANSVAMVDQDIFLFEGTVRDNLTLwDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALV 631
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 493 ETPQVLILDEATASIDSGTEQAIQQALAavRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEAKGRY 568
Cdd:TIGR03796 632 RNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAY 705
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
29-572 |
4.53e-66 |
|
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: 228.86 E-value: 4.53e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 29 VLLLWIAAIAEVSGPLLISYFIDNMVaKSYLPLRLVAGLGVAYVGLQLA---AAGLHYAQSLLFNRAAvgvvQQLRTDVM 105
Cdd:TIGR01193 158 IVNIVIAAIIVTLISIAGSYYLQKII-DTYIPHKMMGTLGIISIGLIIAyiiQQILSYIQIFLLNVLG----QRLSIDII 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 106 DAALRQ----PLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALI--GAMLVAMFSLDWRMALVAItifPAVL 179
Cdd:TIGR01193 233 LSYIKHlfelPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVivGLFLVRQNMLLFLLSLLSI---PVYA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 180 IVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVI-----QQFRQQ---ARFGERMGEASRSHYMARMQTLrldgfl 251
Cdd:TIGR01193 310 VIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIksltsEAERYSkidSEFGDYLNKSFKYQKADQGQQA------ 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 252 lrplLSLFSALVLCGLLMLFG--LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFE--LMDRP-R 326
Cdd:TIGR01193 384 ----IKAVTKLILNVVILWTGayLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDSEfI 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 327 QAYGHDERPLQSGAIAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLA 406
Cdd:TIGR01193 460 NKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 407 SLSHNVLRKGVAMVQQDPVVLADTFYANVTLG--RDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQL 484
Cdd:TIGR01193 540 DIDRHTLRQFINYLPQEPYIFSGSILENLLLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 485 LALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDhTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEA 564
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
....*...
gi 1541475627 565 KGRYWQMY 572
Cdd:TIGR01193 699 NGFYASLI 706
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
341-551 |
8.64e-64 |
|
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: 206.85 E-value: 8.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRE-DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAM 419
Cdd:cd03228 1 IEFKNVSFSYPGrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDPVVLADTFYANVtlgrdysqeqvwevlekvqladlargfsdgintrlgeqgnnLSVGQKQLLALARVLIETPQVLI 499
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 500 LDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQ 551
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
67-571 |
3.25e-62 |
|
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: 223.28 E-value: 3.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 67 LGVaYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATV 146
Cdd:TIGR00957 1008 LSV-YGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMF 1086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 147 LRSA-ALIGAMLVAMFSldwrMALVAITIFPAVLIVMIIyQRYSTPIVRRVR----AYLADINDGFNEVINGMSVIQQFR 221
Cdd:TIGR00957 1087 MGSLfNVIGALIVILLA----TPIAAVIIPPLGLLYFFV-QRFYVASSRQLKrlesVSRSPVYSHFNETLLGVSVIRAFE 1161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 222 QQARF----GERMGEASRSHYMA----RMQTLRLDgfLLRPLLSLFSALvlcgllmlFGLSSSGTIEVGVLYAFISYLGR 293
Cdd:TIGR00957 1162 EQERFihqsDLKVDENQKAYYPSivanRWLAVRLE--CVGNCIVLFAAL--------FAVISRHSLSAGLVGLSVSYSLQ 1231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 294 LNEPLIELTTQQSMLQQAVVAGERVFELMDRPRQA--YGHDERPL----QSGAIAFDNVSFAYRED-RLVLQDITLDVPS 366
Cdd:TIGR00957 1232 VTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEApwQIQETAPPsgwpPRGRVEFRNYCLRYREDlDLVLRHINVTIHG 1311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 367 RGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGRDYSQEQV 446
Cdd:TIGR00957 1312 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEV 1391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 447 WEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHT 526
Cdd:TIGR00957 1392 WWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC 1471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1541475627 527 TLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEAKGRYWQM 571
Cdd:TIGR00957 1472 TVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
29-575 |
2.56e-60 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 210.34 E-value: 2.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 29 VLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVAGLGVAyVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAA 108
Cdd:PRK10789 1 VALLIIIAMLQLIPPKVVGIIVDGVTEQHMTTGQILMWIGTM-VLIAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 109 LRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFS-LDWRMALVAITIFPavlIVMIIYQR 187
Cdd:PRK10789 80 SRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTqISWQLTLLALLPMP---VMAIMIKR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 188 YSTPIVRRVR---AYLADINDGFNEVINGMSVIQQF----RQQARFGERMGEASRSHymarMQTLRLDGfllRPLLSLFS 260
Cdd:PRK10789 157 YGDQLHERFKlaqAAFSSLNDRTQESLTSIRMIKAFgledRQSALFAADAEDTGKKN----MRVARIDA---RFDPTIYI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 261 ALVLCGLLMLFGLS---SSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMD-RPRQAYGHDERPL 336
Cdd:PRK10789 230 AIGMANLLAIGGGSwmvVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAeAPVVKDGSEPVPE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 337 QSGAIAFDNVSFAYRE-DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRK 415
Cdd:PRK10789 310 GRGELDVNIRQFTYPQtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 416 GVAMVQQDPVVLADTFYANVTLGR-DYSQEQVWEVlekVQLA----DLARgFSDGINTRLGEQGNNLSVGQKQLLALARV 490
Cdd:PRK10789 390 RLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHV---ARLAsvhdDILR-LPQGYDTEVGERGVMLSGGQKQRISIARA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 491 LIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEAKGRYWQ 570
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRD 545
|
....*
gi 1541475627 571 MYQLQ 575
Cdd:PRK10789 546 MYRYQ 550
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
341-575 |
7.66e-60 |
|
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: 199.25 E-value: 7.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRED-RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAM 419
Cdd:cd03252 1 ITFEHVRFRYKPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDPVVLADTFYANVTLGRD-YSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVL 498
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 499 ILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEAKGRYWQMYQLQ 575
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
339-551 |
2.81e-58 |
|
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: 194.61 E-value: 2.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 339 GAIAFDNVSFAY--REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKG 416
Cdd:cd03248 10 GIVKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 VAMVQQDPVVLADTFYANVTLG-RDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETP 495
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 496 QVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQ 551
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-589 |
3.87e-58 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 204.81 E-value: 3.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEvsgPLLISYFIDNMVAKS--YLPLRLVAGLG----VAYVGLQLAAAGLHYAQsllfnRAAVgvvq 98
Cdd:PRK13657 24 LAVANVLLAAATFAE---PILFGRIIDAISGKGdiFPLLAAWAGFGlfniIAGVLVARHADRLAHRR-----RLAV---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 99 qlRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVI--------RDLYVTVVATVLrsaaligaMLVAMFSLDWRMALV 170
Cdd:PRK13657 92 --LTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALfglwlefmREHLATLVALVV--------LLPLALFMNWRLSLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 171 aitifpavLIVM-IIYQRYSTPIVRR-------VRAYLADINDGFNEVINGMSVIQQF-RQQArfgermgEASRSHYMAR 241
Cdd:PRK13657 162 --------LVVLgIVYTLITTLVMRKtkdgqaaVEEHYHDLFAHVSDAIGNVSVVQSYnRIEA-------ETQALRDIAD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 242 ----MQTLRLDGFLLRPLLSLFSAL--VLCGLLMLFGLSSSGTIEVGVLYAFISY----LGRLNEP---LIELTTQQSML 308
Cdd:PRK13657 227 nllaAQMPVLSWWALASVLNRAASTitMLAILVLGAALVQKGQLRVGEVVAFVGFatllIGRLDQVvafINQVFMAAPKL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 309 QQAVVAGERVFELMDRPrqayghDERPLQ--SGAIAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASL 386
Cdd:PRK13657 307 EEFFEVEDAVPDVRDPP------GAIDLGrvKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 387 LMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGR-DYSQEQVWEVLEKVQLADLARGFSDG 465
Cdd:PRK13657 381 LQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRpDATDEEMRAAAERAQAHDFIERKPDG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 466 INTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTIL 545
Cdd:PRK13657 461 YDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRIL 540
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1541475627 546 VLHRGQAVERGTHRELLEAKGRYWQMYQLQ-LAGEELAASVREEE 589
Cdd:PRK13657 541 VFDNGRVVESGSFDELVARGGRFAALLRAQgMLQEDERRKQPAAE 585
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-566 |
1.22e-57 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 209.83 E-value: 1.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 8 WPTLKRL-LAYGSPWrkplSVAVLLL--WIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVaglgVAYVGLQLAAAGLHYA 84
Cdd:PLN03232 898 WNVLMRYnKAVGGLW----VVMILLVcyLTTEVLRVSSSTWLSIWTDQSTPKSYSPGFYI----VVYALLGFGQVAVTFT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 85 QSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDT-EVIRD------LYVTVVATVLRSAALIGamL 157
Cdd:PLN03232 970 NSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIgDIDRNvanlmnMFMNQLWQLLSTFALIG--T 1047
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 158 VAMFSLdWRMALVAITIFPAVLIvmiiYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSH 237
Cdd:PLN03232 1048 VSTISL-WAIMPLLILFYAAYLY----YQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNN 1122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 238 YMARMQTLRLDGFLLRPLLSLFSALVLcgLLMLFGLSSSGTIEVGVLYA-----FISYLGRLNEPLIELTTQQSMLQQAV 312
Cdd:PLN03232 1123 IRFTLANTSSNRWLTIRLETLGGVMIW--LTATFAVLRNGNAENQAGFAstmglLLSYTLNITTLLSGVLRQASKAENSL 1200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 313 VAGERVFELMDRPRQAYGHDE--RPLQS----GAIAFDNVSFAYR-EDRLVLQDITLDVPSRGFVALVGHTGSGKSTLAS 385
Cdd:PLN03232 1201 NSVERVGNYIDLPSEATAIIEnnRPVSGwpsrGSIKFEDVHLRYRpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLN 1280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 386 LLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARGFSDG 465
Cdd:PLN03232 1281 ALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFG 1360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 466 INTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTIL 545
Cdd:PLN03232 1361 LDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKIL 1440
|
570 580
....*....|....*....|.
gi 1541475627 546 VLHRGQAVERGTHRELLEAKG 566
Cdd:PLN03232 1441 VLSSGQVLEYDSPQELLSRDT 1461
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-535 |
6.38e-57 |
|
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: 199.89 E-value: 6.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 11 LKRLLAYGSPWRKPLSVAVLLLWIAAIAEVSGPLLISYFIdnmvAKSYLPLRLVAgLGVAYVGLQLAAAG---LHYAQSL 87
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLI----SRAAEMPPVLY-LSVAAVAVRAFGIGravFRYLERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 88 LFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRM 167
Cdd:TIGR02868 76 VGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 168 ALV-AITIFPAVLIVMIIYQ---RYSTPIVRRVRAYLADindGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQ 243
Cdd:TIGR02868 156 ALIlAAGLLLAGFVAPLVSLraaRAAEQALARLRGELAA---QLTDALDGAAELVASGALPAALAQVEEADRELTRAERR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 244 TLRLDGfLLRPLLSLFSAL-VLCGLLMLFGLSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM 322
Cdd:TIGR02868 233 AAAATA-LGAALTLLAAGLaVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 323 DRPR-QAYGHDERPLQSGA----IAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGE 397
Cdd:TIGR02868 312 DAAGpVAEGSAPAAGAVGLgkptLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 398 IRLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGR-DYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNN 476
Cdd:TIGR02868 392 VTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGGAR 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 477 LSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRL 535
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
339-556 |
6.90e-56 |
|
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: 188.18 E-value: 6.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 339 GAIAFDNVSFAYRED-RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGV 417
Cdd:cd03245 1 GRIEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 418 AMVQQDPVVLADTFYANVTLGRDYSQEQvwEVLEKVQLA---DLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIET 494
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDE--RILRAAELAgvtDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 495 PQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERG 556
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
25-318 |
5.13e-55 |
|
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: 188.14 E-value: 5.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSylPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAG--DLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 105 MDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMII 184
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 185 YQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLdGFLLRPLLSLFSALVL 264
Cdd:cd07346 159 FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARL-SALFSPLIGLLTALGT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 265 CGLLMLFGLS-SSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd07346 238 ALVLLYGGYLvLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
122-573 |
2.88e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 193.89 E-value: 2.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 122 GQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVM-IIYQRYSTPIVRRVRAYL 200
Cdd:PRK11160 117 GDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDLTLALTLGGILLLLLLLLpLLFYRLGKKPGQDLTHLR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 201 ADINDGFNEVINGMSVIQQFRQQARFGERMgEASRSHYMARMQTL-RLDGfLLRPLLSLFSALVLCglLMLFgLSSSGT- 278
Cdd:PRK11160 197 AQYRVQLTEWLQGQAELTLFGAEDRYRQQL-EQTEQQWLAAQRRQaNLTG-LSQALMILANGLTVV--LMLW-LAAGGVg 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 279 --------IEVGVLYAFISYlgrlnEPLIELTTQQSMLQQAVVAGERVFELMD-RPRQAYGHDERP-LQSGAIAFDNVSF 348
Cdd:PRK11160 272 gnaqpgalIALFVFAALAAF-----EALMPVAGAFQHLGQVIASARRINEITEqKPEVTFPTTSTAaADQVSLTLNNVSF 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 349 AYREDRL-VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVL 427
Cdd:PRK11160 347 TYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLF 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 428 ADTFYANVTLGR-DYSQEQVWEVLEKVQLADLARGfSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATAS 506
Cdd:PRK11160 427 SATLRDNLLLAApNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 507 IDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEAKGRYWQMYQ 573
Cdd:PRK11160 506 LDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
213-573 |
4.96e-52 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 187.74 E-value: 4.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 213 GMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLdGFLLRPLLSLFSALVLCGLLMLFGLSSSGTIEVG------VLYA 286
Cdd:PRK11174 211 GLETLRLFNRGEAETESIRSASEDFRQRTMEVLRM-AFLSSAVLEFFASISIALVAVYFGFSYLGELNFGhygtgvTLFA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 287 --FISYLG-RLNEPLIELTTQQSMLQQAVVAGERVFELMDRPRQAYGHDERPLQSGA----IAFDNVSFAYrEDRLVLQD 359
Cdd:PRK11174 290 gfFVLILApEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEKELASNDpvtiEAEDLEILSP-DGKTLAGP 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 360 ITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVtQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGR 439
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 440 -DYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQA 518
Cdd:PRK11174 448 pDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 519 LAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEAKGRYWQMYQ 573
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
27-318 |
7.11e-52 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 179.59 E-value: 7.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 27 VAVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVagLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMD 106
Cdd:cd18545 4 LALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLI--IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 107 AALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMIIYQ 186
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 187 RYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDgFLLRPLLSLFSALVLCg 266
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLN-ALFWPLVELISALGTA- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 267 LLMLFG--LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18545 240 LVYWYGgkLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
25-318 |
3.68e-50 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 174.98 E-value: 3.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDN-MVAKSYLPLRLVAGlgvAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTD 103
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSgVRAGDLGVLLLAAA---AYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 104 VMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMI 183
Cdd:cd18546 78 VFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 184 IYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLrPLLSLFSALV 263
Cdd:cd18546 158 WFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYF-PGVELLGNLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 264 LcGLLMLFG--LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18546 237 T-AAVLLVGawRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
8-562 |
1.21e-48 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 183.02 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 8 WPTLKRLL-AYGSPWrkplSVAVLLLWIAA--IAEVSGPLLISYFIDNMVAKSYLPL---RLVAGLGVAYVGLQLAAAGL 81
Cdd:PLN03130 901 WKVLERYKnALGGAW----VVMILFLCYVLteVFRVSSSTWLSEWTDQGTPKTHGPLfynLIYALLSFGQVLVTLLNSYW 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 82 HYAQSLlfnRAAvgvvQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDT-------EVIRDLYVTVVATVLRSAALIG 154
Cdd:PLN03130 977 LIMSSL---YAA----KRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLgdidrnvAVFVNMFLGQIFQLLSTFVLIG 1049
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 155 amLVAMFSLdWRMALVAITIFPAVLIvmiiYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARfgermgeas 234
Cdd:PLN03130 1050 --IVSTISL-WAIMPLLVLFYGAYLY----YQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDR--------- 1113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 235 rshyMARMQTLRLDGFLLRPLLSLFS------ALVLCGLLML-----FGLSSSGTIEVGVLYA-----FISYLGRLNEPL 298
Cdd:PLN03130 1114 ----MAEINGRSMDNNIRFTLVNMSSnrwlaiRLETLGGLMIwltasFAVMQNGRAENQAAFAstmglLLSYALNITSLL 1189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 299 IELTTQQSMLQQAVVAGERVFELMDRPRQA--YGHDERPL----QSGAIAFDNVSFAYRED-RLVLQDITLDVPSRGFVA 371
Cdd:PLN03130 1190 TAVLRLASLAENSLNAVERVGTYIDLPSEAplVIENNRPPpgwpSSGSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVG 1269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 372 LVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLE 451
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLE 1349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 452 KVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVI 531
Cdd:PLN03130 1350 RAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLII 1429
|
570 580 590
....*....|....*....|....*....|.
gi 1541475627 532 AHRLSTIVDADTILVLHRGQAVERGTHRELL 562
Cdd:PLN03130 1430 AHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
341-563 |
3.07e-48 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 167.89 E-value: 3.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMV 420
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDP-------VVLADTFYA--NVTLGRDYSQEQVWEVLEKVQLADLARgfsdgintrlgEQGNNLSVGQKQLLALARVL 491
Cdd:COG1122 81 FQNPddqlfapTVEEDVAFGpeNLGLPREEIRERVEEALELVGLEHLAD-----------RPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 492 IETPQVLILDEATASIDSGTEQAIQQALAAVRD-HTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLE 563
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
337-557 |
5.71e-46 |
|
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: 161.04 E-value: 5.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 337 QSGAIAFDNVSFAYRED-RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRK 415
Cdd:cd03369 3 EHGEIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 416 GVAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLekvqladlargfsdgintRLGEQGNNLSVGQKQLLALARVLIETP 495
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 496 QVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGT 557
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
25-318 |
6.46e-46 |
|
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: 163.75 E-value: 6.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNM-VAKSYLPLRLVAglgVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTD 103
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIfVEKDLEALLLVP---LAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 104 VMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMI 183
Cdd:cd18552 78 LFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 184 IYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGfLLRPLLSLFSALV 263
Cdd:cd18552 158 RIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARA-LSSPLMELLGAIA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 264 LCGLLMLFG-LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18552 237 IALVLWYGGyQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
25-318 |
4.31e-45 |
|
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: 161.80 E-value: 4.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLP--------LRLVAGLGVAYvglqLAAAGLHYAQSLLFNRAAVGV 96
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGggvdfsglLRILLLLLGLY----LLSALFSYLQNRLMARVSQRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 97 VQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFP 176
Cdd:cd18547 77 VYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 177 AVLIVMIIYQRYSTPIVRRVRAYLADINdGF-NEVINGMSVIQQFRQQARFGERMGEASRSHY--MARMQTLrldGFLLR 253
Cdd:cd18547 157 LSLLVTKFIAKRSQKYFRKQQKALGELN-GYiEEMISGQKVVKAFNREEEAIEEFDEINEELYkaSFKAQFY---SGLLM 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 254 PLLSLFSALVLcGLLMLFG--LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18547 233 PIMNFINNLGY-VLVAVVGglLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-318 |
4.76e-45 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 161.91 E-value: 4.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSYL-------------PLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNR 91
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLpgllglapllgpdPLALLLLAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 92 AAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVA 171
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 172 ITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLdGFL 251
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARL-QAL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 252 LRPLLSLFSALVLCgLLMLFG--LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18564 240 LSPVVDVLVAVGTA-LVLWFGawLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
72-564 |
1.54e-43 |
|
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: 163.77 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 72 VGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSefdiqpvgqviSRVTNDTEVIRDLyvTVVATVLRSAA 151
Cdd:COG4618 67 LGLYAVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRAALR-----------GGGGAAAQALRDL--DTLRQFLTGPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 152 LIGAM--------LVAMFSLDWRMALVAItIFPAVLIVM-IIYQRYSTPIVRRVRAYLADINDGFN------EVINGMSV 216
Cdd:COG4618 134 LFALFdlpwapifLAVLFLFHPLLGLLAL-VGALVLVALaLLNERLTRKPLKEANEAAIRANAFAEaalrnaEVIEAMGM 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 217 IQQFRQqaRFGERMGEASRSHYMA--RMQTLrldGFLLRPLLSLFSALVLC--GLLMLFGLSSSGTIEVG-VLyafisyL 291
Cdd:COG4618 213 LPALRR--RWQRANARALALQARAsdRAGGF---SALSKFLRLLLQSAVLGlgAYLVIQGEITPGAMIAAsIL------M 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 292 GRLNEPLIELTTQQSMLQQAVVAGERVFELMDRPRQAYGHDERPLQSGAIAFDNVSFAY-REDRLVLQDITLDVPSRGFV 370
Cdd:COG4618 282 GRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMPLPRPKGRLSVENLTVVPpGSKRPILRGVSFSLEPGEVL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 371 ALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVL 450
Cdd:COG4618 362 GVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAA 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 451 EKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDH-TTLV 529
Cdd:COG4618 442 KLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVV 521
|
490 500 510
....*....|....*....|....*....|....*
gi 1541475627 530 VIAHRLSTIVDADTILVLHRGQAVERGTHRELLEA 564
Cdd:COG4618 522 VITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
343-551 |
1.87e-43 |
|
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: 154.16 E-value: 1.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 343 FDNVSFAY-REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQ 421
Cdd:cd03225 2 LKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 422 QDP-------VVLADTFYA--NVTLGRDYSQEQVWEVLEKVQLADLArgfsdgiNTRLgeqgNNLSVGQKQLLALARVLI 492
Cdd:cd03225 82 QNPddqffgpTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEGLR-------DRSP----FTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 493 ETPQVLILDEATASIDSGTEQAIQQALAAVRD-HTTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
27-318 |
4.12e-43 |
|
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: 156.05 E-value: 4.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 27 VAVLLLWIAAIAEVSGPLLISYFIDNMVAKSylPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMD 106
Cdd:cd18542 3 LAILALLLATALNLLIPLLIRRIIDSVIGGG--LRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 107 AALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMIIYQ 186
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 187 RYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLrPLLSLFSALVLcG 266
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYW-PLMDFLSGLQI-V 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 267 LLMLFG--LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18542 239 LVLWVGgyLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
334-563 |
4.05e-41 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 160.33 E-value: 4.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 334 RPLQSGAIAFDNVSFAYRED-RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNV 412
Cdd:PTZ00243 1302 HPVQAGSLVFEGVQMRYREGlPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 413 LRKGVAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLI 492
Cdd:PTZ00243 1382 LRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 493 ETPQVLIL-DEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLE 563
Cdd:PTZ00243 1462 KKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
341-552 |
1.08e-38 |
|
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: 140.04 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRE-DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAM 419
Cdd:cd03246 1 LEVENVSFRYPGaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDpvvladtfyanvtlgrdysqeqvwevlekVQLadlargFSDGINtrlgeqGNNLSVGQKQLLALARVLIETPQVLI 499
Cdd:cd03246 81 LPQD-----------------------------DEL------FSGSIA------ENILSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 500 LDEATASIDSGTEQAIQQALAAVR-DHTTLVVIAHRLSTIVDADTILVLHRGQA 552
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-318 |
1.44e-38 |
|
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: 143.45 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNmVAKSYLPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDL-VTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 105 MDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMII 184
Cdd:cd18778 80 YDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 185 YQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGfLLRPLLSLFSALVL 264
Cdd:cd18778 160 YSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWA-IFHPLMEFLTSLGT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 265 CgLLMLFG--LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18778 239 V-LVLGFGgrLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
339-565 |
9.89e-38 |
|
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: 140.43 E-value: 9.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 339 GAIAFDNVSFAYRED-RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGV 417
Cdd:cd03288 18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 418 AMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQV 497
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 498 LILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEAK 565
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
341-551 |
1.00e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 138.80 E-value: 1.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMV 420
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDPVVLADTFYANVTL-----GRDYSQEQVWEVLEKVQLADLArgfsdgintrLGEQGNNLSVGQKQLLALARVLIETP 495
Cdd:COG4619 80 PQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDI----------LDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 496 QVLILDEATASIDSGTEQAIQQALAAVRDH--TTLVVIAH------RLstivdADTILVLHRGQ 551
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSHdpeqieRV-----ADRVLTLEAGR 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
341-561 |
1.10e-37 |
|
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: 139.24 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRlVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPV-----TQGEIRLDGRPLASLSHNV--L 413
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVleL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 414 RKGVAMVQQDPVVLADTFYANVTLG--------RDYSQEQVWEVLEKVQLADLArgfsdgiNTRLGeqGNNLSVGQKQLL 485
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiklKEELDERVEEALRKAALWDEV-------KDRLH--ALGLSGGQQQRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 486 ALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAH------RLstivdADTILVLHRGQAVERGTHR 559
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFGPTE 225
|
..
gi 1541475627 560 EL 561
Cdd:cd03260 226 QI 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
340-551 |
1.69e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.07 E-value: 1.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYReDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASlshnvLRKGVAM 419
Cdd:COG1121 6 AIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDPVVLADtFYAN----VTLGRDYSQ-----------EQVWEVLEKVQLADLArgfsdgiNTRLGEqgnnLSVGQKQL 484
Cdd:COG1121 80 VPQRAEVDWD-FPITvrdvVLMGRYGRRglfrrpsradrEAVDEALERVGLEDLA-------DRPIGE----LSGGQQQR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 485 LALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREyFDRVLLLNRGL 216
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-318 |
4.38e-37 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 139.57 E-value: 4.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDN--MVAKSYLPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRT 102
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDvlIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 103 DVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVM 182
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 183 IIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLrPLLSLFsaL 262
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFF-PLLTFL--T 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 263 VLCGLLMLF--GLS-SSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18563 238 SLGTLIVWYfgGRQvLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
25-298 |
1.38e-36 |
|
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: 137.77 E-value: 1.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 105 MDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMII 184
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 185 YQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSALVL 264
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 1541475627 265 CGLLMLFGLSSSGTIEVGVLYAFISYLGRLNEPL 298
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
340-591 |
2.13e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 142.73 E-value: 2.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYREDRL-VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVT---QGEIRLDGRPLASLSHNVLRK 415
Cdd:COG1123 4 LLEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 416 GVAMVQQDPVV----------LADTFyANVTLGRDYSQEQVWEVLEKVQLADLARGFSDgintrlgeqgnNLSVGQKQLL 485
Cdd:COG1123 84 RIGMVFQDPMTqlnpvtvgdqIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 486 ALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDH--TTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELL 562
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEIL 231
|
250 260
....*....|....*....|....*....
gi 1541475627 563 EAKGRYWQMYQLQLAGEELAASVREEESL 591
Cdd:COG1123 232 AAPQALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
341-564 |
4.26e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 141.58 E-value: 4.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAY----REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNV---L 413
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 414 RKGVAMVQQDPV-----------VLADTFYANVTLGRDYSQEQVWEVLEKVQL-ADLARgfsdgintRLGEQgnnLSVGQ 481
Cdd:COG1123 341 RRRVQMVFQDPYsslnprmtvgdIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLAD--------RYPHE---LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 482 KQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTH 558
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
....*.
gi 1541475627 559 RELLEA 564
Cdd:COG1123 490 EEVFAN 495
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
341-562 |
2.24e-35 |
|
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: 134.09 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRE-DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASlSHNV--LRKGV 417
Cdd:TIGR04520 1 IEVENVSFSYPEsEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD-EENLweIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 418 AMVQQDP-------VVLADTFYA--NVTLGRDYSQEQVWEVLEKVQLADLARgfsdgintrlgEQGNNLSVGQKQLLALA 488
Cdd:TIGR04520 80 GMVFQNPdnqfvgaTVEDDVAFGleNLGVPREEMRKRVDEALKLVGMEDFRD-----------REPHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 489 RVLIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELL 562
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIF 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
340-562 |
3.06e-35 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 133.25 E-value: 3.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYReDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAM 419
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDPVVLAD-TFYANVTLGR-------------DYsqEQVWEVLEKVQLADLArgfsdgiNTRLGEqgnnLSVGQKQLL 485
Cdd:COG1120 80 VPQEPPAPFGlTVRELVALGRyphlglfgrpsaeDR--EAVEEALERTGLEHLA-------DRPVDE----LSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 486 ALARVLIETPQVLILDEATASIDSGTEQAIQQ---ALAAVRDHTTLVVI-----AHRLstivdADTILVLHRGQAVERGT 557
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLEllrRLARERGRTVVMVLhdlnlAARY-----ADRLVLLKDGRIVAQGP 221
|
....*
gi 1541475627 558 HRELL 562
Cdd:COG1120 222 PEEVL 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
341-551 |
4.66e-35 |
|
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: 131.05 E-value: 4.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDR----LVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRplaslshnvlrkg 416
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 VAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVQL-ADLARgFSDGINTRLGEQGNNLSVGQKQLLALARVLIETP 495
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 496 QVLILDEATASIDSGT-----EQAIQQALaavRDHTTLVVIAHRLSTIVDADTILVLHRGQ 551
Cdd:cd03250 147 DIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
357-505 |
5.48e-35 |
|
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: 128.92 E-value: 5.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 357 LQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLAD-TFYANV 435
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 436 TLG-------RDYSQEQVWEVLEKVQLADLArgfsdgiNTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATA 505
Cdd:pfam00005 81 RLGlllkglsKREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
341-554 |
6.26e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.33 E-value: 6.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHN---VLRKGV 417
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 418 AMVQQDPVVLAD-TFYANVTL-------GRDYSQEQVWEVLEKVQLADLARGFSDgintrlgeqgnNLSVGQKQLLALAR 489
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALplrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 490 VLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIA-HRLStIVDA--DTILVLHRGQAVE 554
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLE-LVDRmpKRVLELEDGRLVR 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
340-564 |
9.20e-35 |
|
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: 131.85 E-value: 9.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYR---EDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKG 416
Cdd:COG1124 1 MLEVRNLSVSYGqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 VAMVQQDP-----------VVLADTFYAnvtLGRDYSQEQVWEVLEKVqlaDLARGFSDgintRLGEQgnnLSVGQKQLL 485
Cdd:COG1124 81 VQMVFQDPyaslhprhtvdRILAEPLRI---HGLPDREERIAELLEQV---GLPPSFLD----RYPHQ---LSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 486 ALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLStIVD--ADTILVLHRGQAVERGTHREL 561
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADL 226
|
...
gi 1541475627 562 LEA 564
Cdd:COG1124 227 LAG 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
335-565 |
2.45e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 131.27 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 335 PLQSGAIAFDNVSFAYRED-RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL 413
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 414 RKGVAMVQQDP-------VVLADTFYA--NVTLGRDYSQEQVWEVLEKVQLADLargfsdgintrLGEQGNNLSVGQKQL 484
Cdd:PRK13632 82 RKKIGIIFQNPdnqfigaTVEDDIAFGleNKKVPPKKMKDIIDDLAKKVGMEDY-----------LDKEPQNLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 485 LALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHT--TLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELL 562
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
...
gi 1541475627 563 EAK 565
Cdd:PRK13632 231 NNK 233
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
25-318 |
2.71e-34 |
|
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: 131.76 E-value: 2.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSyLPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGT-LTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 105 MDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMI- 183
Cdd:cd18541 80 FAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 184 ----IYQRYstpivRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGfLLRPLLSLF 259
Cdd:cd18541 160 lgkkIHKRF-----RKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDA-LFFPLIGLL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 260 SALVLCgLLMLFG--LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18541 234 IGLSFL-IVLWYGgrLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
25-318 |
3.34e-34 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 131.45 E-value: 3.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSylPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHG--DRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 105 MDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLyVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMII 184
Cdd:cd18543 79 FAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRF-LAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 185 YQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLrPLLSLFSALVL 264
Cdd:cd18543 158 FRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFW-PLLEALPELGL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 265 CGLLMLFG-LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18543 237 AAVLALGGwLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
71-555 |
3.83e-34 |
|
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: 138.89 E-value: 3.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 71 YVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLY-VTVVATVLRS 149
Cdd:TIGR01271 931 YVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLpLTLFDFIQLT 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 150 AALIGAMLVamfsldwrMALVAITIFPAVLIVMIIYqrystpIVrrVRAYLADINDGFNEV---------------INGM 214
Cdd:TIGR01271 1011 LIVLGAIFV--------VSVLQPYIFIAAIPVAVIF------IM--LRAYFLRTSQQLKQLesearspifshlitsLKGL 1074
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 215 SVIQQFRQQARFGERMGEASRSH---YMARMQTLRLdgFLLR---PLLSLFSALVLCGLlmlfGLSSSGTIEVGVLYAF- 287
Cdd:TIGR01271 1075 WTIRAFGRQSYFETLFHKALNLHtanWFLYLSTLRW--FQMRidiIFVFFFIAVTFIAI----GTNQDGEGEVGIILTLa 1148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 288 ISYLGRLNEPLIELTTQQSMLQQAvvagERVFELMDRPRQ---------------------AYGHDERPLQsGAIAFDNV 346
Cdd:TIGR01271 1149 MNILSTLQWAVNSSIDVDGLMRSV----SRVFKFIDLPQEeprpsggggkyqlstvlvienPHAQKCWPSG-GQMDVQGL 1223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 347 SFAYRED-RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPvTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPV 425
Cdd:TIGR01271 1224 TAKYTEAgRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVF 1302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 426 VLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATA 505
Cdd:TIGR01271 1303 IFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1541475627 506 SIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLhRGQAVER 555
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVI-EGSSVKQ 1431
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
25-318 |
4.76e-34 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 131.02 E-value: 4.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSyLPLRLVAGLgvayVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGG-SSGGLLALL----VALFLLQAVLSALSSYLLGRTGERVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 105 MDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMII 184
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 185 YQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGfLLRPLLSLfsaLVL 264
Cdd:cd18551 156 LGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEA-LIGPLMGL---AVQ 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 265 CGLLMLFGLS----SSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18551 232 LALLVVLGVGgarvASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
22-318 |
2.19e-33 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 129.14 E-value: 2.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 22 RKPLSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLplRLVAGLGVAYVGLQLAAAGLHYaqslLFNRAA----VGVV 97
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTL--DGLTGFILLYLGLILIQALSVF----LFIRLAgkieMGVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 98 QQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPA 177
Cdd:cd18540 75 YDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 178 VLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLrPLLS 257
Cdd:cd18540 155 LAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFL-PIVL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 258 LFSALVLcGLLMLFG--LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18540 234 FLGSIAT-ALVLWYGgiLVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
341-556 |
2.78e-33 |
|
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: 125.50 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRE-DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLShNVLRKGVAM 419
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDPVVLADTFYANVtlgrdysqeqvwevlekvqladlargfsdgintrlgeqGNNLSVGQKQLLALARVLIETPQVLI 499
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 500 LDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERG 556
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
343-550 |
1.03e-32 |
|
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: 124.95 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 343 FDNVSFAYReDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASlshnvLRKGVAMVQQ 422
Cdd:cd03235 2 VEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 423 DPVVLAD---TFYANVTLGRD--------YSQEQ---VWEVLEKVQLADLArgfsdgiNTRLGEqgnnLSVGQKQLLALA 488
Cdd:cd03235 76 RRSIDRDfpiSVRDVVLMGLYghkglfrrLSKADkakVDEALERVGLSELA-------DRQIGE----LSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 489 RVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTIVD-ADTILVLHRG 550
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
341-563 |
2.03e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 126.02 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDR-LVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAM 419
Cdd:PRK13648 8 IVFKNVSFQYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDP-------VVLADTFYA--NVTLGRDYSQEQVWEVLEKVQLADLArgfsdgintrlGEQGNNLSVGQKQLLALARV 490
Cdd:PRK13648 88 VFQNPdnqfvgsIVKYDVAFGleNHAVPYDEMHRRVSEALKQVDMLERA-----------DYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 491 LIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLE 563
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
341-556 |
2.06e-32 |
|
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: 124.54 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRL---VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS---HNVLR 414
Cdd:cd03257 2 LEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 415 KGVAMVQQDPV-----------VLADTFYANVTLGRDYS-QEQVWEVLEKVQLADlargfsdginTRLGEQGNNLSVGQK 482
Cdd:cd03257 82 KEIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEArKEAVLLLLVGVGLPE----------EVLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 483 QLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDH--TTLVVIAHRLSTIVD-ADTILVLHRGQAVERG 556
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElgLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
271-572 |
8.04e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 131.69 E-value: 8.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 271 FG--LSSSGTIEVG----VLYAFI---SYLGRLneplielTTQQSMLQQAVVAGERVFELMDRPRQAYGHDERPLQ---- 337
Cdd:PTZ00265 1087 FGsfLIRRGTILVDdfmkSLFTFLftgSYAGKL-------MSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRiknk 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 338 ---SGAIAFDNVSFAY--REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPV------------------- 393
Cdd:PTZ00265 1160 ndiKGKIEIMDVNFRYisRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtne 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 394 -----------------------------------TQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLG 438
Cdd:PTZ00265 1240 qdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG 1319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 439 R-DYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQ 517
Cdd:PTZ00265 1320 KeDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 518 ALAAVRDHT--TLVVIAHRLSTIVDADTILVLHR----GQAVE-RGTHRELLEAKGRYWQMY 572
Cdd:PTZ00265 1400 TIVDIKDKAdkTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQDGVYKKY 1461
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
344-556 |
1.10e-31 |
|
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: 121.00 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYReDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQd 423
Cdd:cd03214 3 ENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 424 pvvladtfyanvtlgrdysqeqvweVLEKVQLADLA-RGFsdgintrlgeqgNNLSVGQKQLLALARVLIETPQVLILDE 502
Cdd:cd03214 81 -------------------------ALELLGLAHLAdRPF------------NELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 503 ATASIDSGTEQAIQQ---ALAAVRDHTTLVVI-----AHRLstivdADTILVLHRGQAVERG 556
Cdd:cd03214 124 PTSHLDIAHQIELLEllrRLARERGKTVVMVLhdlnlAARY-----ADRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
343-551 |
1.46e-31 |
|
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: 119.66 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 343 FDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQ 422
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 423 dpvvladtfyanvtlgrdysqeqvwevlekvqladlargfsdgintrlgeqgnnLSVGQKQLLALARVLIETPQVLILDE 502
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 503 ATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTIVDA-DTILVLHRGQ 551
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
341-563 |
2.65e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.82 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRE-DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAM 419
Cdd:PRK13635 6 IRVEHISFRYPDaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDP-------VVLADTFYA--NVTLGRDYSQEQVWEVLEKVQLADLARgfsdgintrlgEQGNNLSVGQKQLLALARV 490
Cdd:PRK13635 86 VFQNPdnqfvgaTVQDDVAFGleNIGVPREEMVERVDQALRQVGMEDFLN-----------REPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 491 LIETPQVLILDEATASIDSgteQAIQQALAAVRD-----HTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLE 563
Cdd:PRK13635 155 LALQPDIIILDEATSMLDP---RGRREVLETVRQlkeqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
341-566 |
2.71e-31 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 122.95 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRED----RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLAS---LSHNVL 413
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 414 RKGVAMVQQDP-------VVLADTFYA--NVTLGRDYSQEQVWEVLEKVqladlarGFSDGINTRlgeqgN--NLSVGQK 482
Cdd:TIGR04521 81 RKKVGLVFQFPehqlfeeTVYKDIAFGpkNLGLSEEEAEERVKEALELV-------GLDEEYLER-----SpfELSGGQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 483 QLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGT-- 557
Cdd:TIGR04521 149 RRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKekGLTVILVTHSMEDVAEyADRVIVMHKGKIVLDGTpr 228
|
250
....*....|...
gi 1541475627 558 ----HRELLEAKG 566
Cdd:TIGR04521 229 evfsDVDELEKIG 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
341-549 |
3.39e-31 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 121.04 E-value: 3.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDR---LVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHnvlrkGV 417
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 418 AMVQQDPVVLA-DTFYANVTLG-------RDYSQEQVWEVLEKVQLADLARGFSDgintrlgeqgnNLSVGQKQLLALAR 489
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqgvpKAEARERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 490 VLIETPQVLILDEATASIDSGTEQAIQQALAAV--RDHTTLVVIAHRLS-TIVDADTILVLHR 549
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
340-550 |
1.37e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.19 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYR---EDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVlrkg 416
Cdd:COG1116 7 ALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 vAMVQQDPVVLA-DTFYANVTLG-------RDYSQEQVWEVLEKVQLADLARGFSdgintrlgeqgNNLSVGQKQLLALA 488
Cdd:COG1116 83 -GVVFQEPALLPwLTVLDNVALGlelrgvpKAERRERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 489 RVLIETPQVLILDEATASIDSGTEQAIQQALAAV--RDHTTLVVIAH------RLstivdADTILVLHRG 550
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHdvdeavFL-----ADRVVVLSAR 215
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-318 |
1.10e-29 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 118.74 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSylPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQG--DLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 105 MDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMII 184
Cdd:cd18550 79 YAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 185 YQRYSTPIVRRVRAYLADINDGFNEV--INGMSVIQQFRQQARFGERMGEASRShyMARMQT-LRLDGFLLRPLLSLFSA 261
Cdd:cd18550 159 VGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRE--LRDLGVrQALAGRWFFAALGLFTA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 262 LVLCGLLMLFG-LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18550 237 IGPALVYWVGGlLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
28-318 |
2.33e-29 |
|
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: 117.58 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 28 AVLLLWIAAIAEVSGPLLISYFIDN-MVAKSYLPLRLVAGLGVAYVGLQlaaAGLHYAQSLLFNRAAVGVVQQLRTDVMD 106
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAaLGGGDTASLNQIALLLLGLFLLQ---AVFSFFRIYLFARVGERVVADLRKDLYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 107 AALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAA-LIGAmLVAMFSLDWRMALVAITIFPAVLIVMIIY 185
Cdd:cd18576 78 HLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILtLIGG-VVLLFFISWKLTLLMLATVPVVVLVAVLF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 186 QRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLrPL--LSLFSALV 263
Cdd:cd18576 157 GRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFS-SFiiFLLFGAIV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 264 lcgLLMLFGLS--SSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18576 236 ---AVLWYGGRlvLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
341-551 |
6.49e-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: 114.51 E-value: 6.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRL---VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL---- 413
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 414 RKGVAMVQQDPVVLAD-TFYANVTLGRDYSQEQVWEVLEKV-QLADLArgfsdGINTRLGEQGNNLSVGQKQLLALARVL 491
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAeELLERV-----GLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 492 IETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVDADTILVLHRGQ 551
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
28-290 |
8.68e-29 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 116.12 E-value: 8.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 28 AVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLrlVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDA 107
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDV--LNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 108 ALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMIIYQR 187
Cdd:cd18557 79 LLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 188 YSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLrpLLSLFSALVLCGL 267
Cdd:cd18557 159 YIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQ--GITSLLIYLSLLL 236
|
250 260
....*....|....*....|....*
gi 1541475627 268 LMLFG--LSSSGTIEVGVLYAFISY 290
Cdd:cd18557 237 VLWYGgyLVLSGQLTVGELTSFILY 261
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
341-562 |
9.67e-29 |
|
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: 114.22 E-value: 9.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRL---VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL---R 414
Cdd:cd03258 2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 415 KGVAMV-QQDPVVLADTFYANVTL-------GRDYSQEQVWEVLEKVQLADLARGFSdgintrlgeqgNNLSVGQKQLLA 486
Cdd:cd03258 82 RRIGMIfQHFNLLSSRTVFENVALpleiagvPKAEIEERVLELLELVGLEDKADAYP-----------AQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 487 LARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHT--TLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELL 562
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
28-318 |
1.18e-28 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 115.72 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 28 AVLLLWIAAIAEVSGPLLISYFIDNMVAKS-----YLPLRLVAGLGVAYVGLqlaaAGLhyaQSLLFNRAAVGVVQQLRT 102
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGsreafYRAVLLLLLLSVLSGLF----SGL---RGGCFSYAGTRLVRRLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 103 DVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVM 182
Cdd:cd18572 74 DLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALIT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 183 IIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQF----RQQARFGERMgeasrSHYMARMQTLRLDGFLLRPLLSL 258
Cdd:cd18572 154 KVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFateeREARRYERAL-----DKALKLSVRQALAYAGYVAVNTL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 259 FSALVLCGLLMLFG-LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18572 229 LQNGTQVLVLFYGGhLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
341-551 |
1.42e-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: 112.11 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYReDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKgVAMV 420
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDPvvladTFYANVTlgrdysqeqVWEVLEkvqladlargfsdgintrlgeqgnnLSVGQKQLLALARVLIETPQVLIL 500
Cdd:cd03230 79 PEEP-----SLYENLT---------VRENLK-------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 501 DEATASIDSGTEQAIQQALAAVRDHTTLVVIA-HRLSTIVD-ADTILVLHRGQ 551
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGR 172
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
344-563 |
1.57e-28 |
|
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: 113.30 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYREDRlVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASL-SHNVLRKGVAMVQQ 422
Cdd:cd03224 4 ENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 423 DPVVLAD-TFYANVTLG-RDYSQEQVWEVLEKV-----QLADlargfsdgintRLGEQGNNLSVGQKQLLALARVLIETP 495
Cdd:cd03224 83 GRRIFPElTVEENLLLGaYARRRAKRKARLERVyelfpRLKE-----------RRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 496 QVLILDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLE 563
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-502 |
1.66e-28 |
|
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: 119.90 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 13 RLLAYGSPWrkPLSVAVLLlwiAAIAEVSGPLLIsYFIDNMVAKSYLPLrlvAGLGVAYVGLQLAAAGLHYAQSLLFNRA 92
Cdd:COG4615 5 RLLLRESRW--LLLLALLL---GLLSGLANAGLI-ALINQALNATGAAL---ARLLLLFAGLLVLLLLSRLASQLLLTRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 93 AVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVtVVATVLRSAALIGAMLVAMFSLDWRMALVAI 172
Cdd:COG4615 76 GQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-RLPELLQSVALVLGCLAYLAWLSPPLFLLTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 173 TifpAVLIVMIIYQRYstpiVRRVRAYLA--------------DINDGFNEV-INGMsviqqfRQQARFGERMGEASRS- 236
Cdd:COG4615 155 V---LLGLGVAGYRLL----VRRARRHLRrareaedrlfkhfrALLEGFKELkLNRR------RRRAFFDEDLQPTAERy 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 237 -HYMARMQTLrldgFLLRPLLSLFSALVLCGLLmLFGLSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAG 315
Cdd:COG4615 222 rDLRIRADTI----FALANNWGNLLFFALIGLI-LFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVAL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 316 ERVFEL---MDRPRQAYGHDERPLQSGA---IAFDNVSFAYR----EDRLVLQDITLDVpSRG-FVALVGHTGSGKSTLA 384
Cdd:COG4615 297 RKIEELelaLAAAEPAAADAAAPPAPADfqtLELRGVTYRYPgedgDEGFTLGPIDLTI-RRGeLVFIVGGNGSGKSTLA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 385 SLLMGYYPVTQGEIRLDGRPLASLSHNVLRkgvamvQQDPVVLADtFY---ANVTLGRDYSQEQVWEVLEKVQLADLARg 461
Cdd:COG4615 376 KLLTGLYRPESGEILLDGQPVTADNREAYR------QLFSAVFSD-FHlfdRLLGLDGEADPARARELLERLELDHKVS- 447
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1541475627 462 FSDGINTRLgeqgnNLSVGQKQLLALARVLIETPQVLILDE 502
Cdd:COG4615 448 VEDGRFSTT-----DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
340-554 |
1.90e-28 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 113.21 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYREDRL---VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL--- 413
Cdd:COG1136 4 LLELRNLTKSYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 414 -RKGVAMVQQDPVVLAD-TFYANVTLGRDYS-------QEQVWEVLEKVQLADLARGFSdgintrlgeqgNNLSVGQKQL 484
Cdd:COG1136 84 rRRHIGFVFQFFNLLPElTALENVALPLLLAgvsrkerRERARELLERVGLGDRLDHRP-----------SQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 485 LALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVDADTILVLHRGQAVE 554
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
345-564 |
2.29e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 115.54 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 345 NVSFAYREDRL-VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYP---VTQGEIRLDGRPLASLSHNVLR----KG 416
Cdd:COG0444 8 KVYFPTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRkirgRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 VAMVQQDPV-----------VLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARgfsdgintRLGEQGNNLSVGQKQLL 485
Cdd:COG0444 88 IQMIFQDPMtslnpvmtvgdQIAEPLRIHGGLSKAEARERAIELLERVGLPDPER--------RLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 486 ALARVLIETPQVLILDEATASIDsGTEQAiqQALAAVRD-----HTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHR 559
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALD-VTIQA--QILNLLKDlqrelGLAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVE 236
|
....*
gi 1541475627 560 ELLEA 564
Cdd:COG0444 237 ELFEN 241
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
356-557 |
2.32e-28 |
|
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: 113.30 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS-HNVLRKGVAMVQQDPVVLAD-TFYA 433
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 434 NVTLGRDYSQ-----------------EQVWEVLEKVQLADLARgfsdgintrlgEQGNNLSVGQKQLLALARVLIETPQ 496
Cdd:cd03219 95 NVMVAAQARTgsglllararreerearERAEELLERVGLADLAD-----------RPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 497 VLILDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVERGT 557
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
27-318 |
1.05e-27 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 112.88 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 27 VAVLLLWIAAIAEVSGPLLISYFIDNMVAKSylPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMD 106
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIDEGIANG--DLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 107 AALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAAL-IGAmLVAMFSLDWRMALVAITIFPAVLIVMIIY 185
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMlIGA-IIMAFRINPKLALILLVAIPILALVVFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 186 QRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLrPLLSLFSALVLC 265
Cdd:cd18548 160 MKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLN-PLMMLIMNLAIV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 266 gLLMLFG--LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18548 239 -AILWFGghLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
343-556 |
1.07e-27 |
|
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: 110.69 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 343 FDNVSFAYREDRlVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLShnVLRKGVAMVQQ 422
Cdd:cd03259 3 LKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP--PERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 423 DPVVLAD-TFYANVTLG-------RDYSQEQVWEVLEKVQLADLARgfsdgintRLGEQgnnLSVGQKQLLALARVLIET 494
Cdd:cd03259 80 DYALFPHlTVAENIAFGlklrgvpKAEIRARVRELLELVGLEGLLN--------RYPHE---LSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 495 PQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVERG 556
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
341-567 |
1.64e-27 |
|
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: 111.10 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYReDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLShNVLRKGVAMV 420
Cdd:COG4555 2 IEVENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDPVvladtFYANVTlGRDY-------SQEQVWEVLEKV-QLADLArGFSDGINTRLGEqgnnLSVGQKQLLALARVLI 492
Cdd:COG4555 80 PDERG-----LYDRLT-VRENiryfaelYGLFDEELKKRIeELIELL-GLEEFLDRRVGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 493 ETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIA-HRLSTIVD-ADTILVLHRGQAVERGTHRELLEAKGR 567
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
341-556 |
5.70e-27 |
|
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: 108.65 E-value: 5.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHN---VLRKGV 417
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 418 AMVQQDPVVLAD-TFYANVTL-------GRDYSQEQVWEVLEKVQLADLARGFSdgintrlgeqgNNLSVGQKQLLALAR 489
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFalevtgvPPREIRKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 490 VLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTilvlHRGQAVERG 556
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTR----HRVIALERG 212
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-318 |
6.44e-27 |
|
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: 111.12 E-value: 6.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNMVAK--SYLPLRL-----------VAGLGVAYVGLQLAAAGLHYAQSLLFNR 91
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGeaSFLPLVPaslgpadprgqLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 92 AAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVA 171
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 172 ITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLdGFL 251
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRL-RAA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 252 LRPLLSLFSA------LVLCGLLMLFGLSS-SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18565 240 FFPVIRLVAGagfvatFVVGGYWVLDGPPLfTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
356-553 |
1.18e-26 |
|
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: 105.97 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS-HNVLRKGVAMVQQdpvvladtfyan 434
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 435 vtlgrdysqeqvwevlekvqladlargfsdgintrlgeqgnnLSVGQKQLLALARVLIETPQVLILDEATASIdsgTEQA 514
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL---TPAE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1541475627 515 IQQALAAVRD----HTTLVVIAHRLSTIVD-ADTILVLHRGQAV 553
Cdd:cd03216 118 VERLFKVIRRlraqGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
341-544 |
1.25e-26 |
|
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: 107.56 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAyREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVlRKGVAMV 420
Cdd:COG4133 3 LEAENLSCR-RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 -QQDPVVLADTFYANVTL-----GRDYSQEQVWEVLEKVQLADLArgfsdgiNTRLGeqgnNLSVGQKQLLALARVLIET 494
Cdd:COG4133 81 gHADGLKPELTVRENLRFwaalyGLRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 495 PQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIA-HRLSTIVDADTI 544
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
356-561 |
1.75e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.19 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPsRGFV-ALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS-HNVLRKGVAMVQQDPVVLAD-TFY 432
Cdd:COG1129 19 ALDGVSLELR-PGEVhALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 433 ANVTLGR--------DYSQ--EQVWEVLEKVQLA-DLargfsdgiNTRLGEqgnnLSVGQKQLLALARVLIETPQVLILD 501
Cdd:COG1129 98 ENIFLGReprrggliDWRAmrRRARELLARLGLDiDP--------DTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 502 EATASIdsgTEQAIQQALAAVRD----HTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHREL 561
Cdd:COG1129 166 EPTASL---TEREVERLFRIIRRlkaqGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
337-563 |
2.11e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 110.57 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 337 QSGAIAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNvlRKG 416
Cdd:COG3842 2 AMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 VAMVQQDpvvladtfYA---------NVTLG-------RDYSQEQVWEVLEKVQLADLARgfsdgintRLGEQgnnLSVG 480
Cdd:COG3842 79 VGMVFQD--------YAlfphltvaeNVAFGlrmrgvpKAEIRARVAELLELVGLEGLAD--------RYPHQ---LSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 481 QKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDH--TTLVVIAHRLS---TIvdADTILVLHRGQAVER 555
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElgITFIYVTHDQEealAL--ADRIAVMNDGRIEQV 217
|
....*...
gi 1541475627 556 GTHRELLE 563
Cdd:COG3842 218 GTPEEIYE 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
340-562 |
2.15e-26 |
|
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: 108.25 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFaYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGY-YPVTQGEIRLDGRPLASLSHNVLRK--G 416
Cdd:COG1119 3 LLELRNVTV-RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKriG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 V---AMVQQDPV------VLADTFYANVTLGRDYSQEQ---VWEVLEKVQLADLArgfsdgiNTRLGEqgnnLSVGQKQL 484
Cdd:COG1119 82 LvspALQLRFPRdetvldVVLSGFFDSIGLYREPTDEQrerARELLELLGLAHLA-------DRPFGT----LSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 485 LALARVLIETPQVLILDEATASID-SGTEQAIQ--QALAAvRDHTTLVVIAHRLSTIVDADT-ILVLHRGQAVERGTHRE 560
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDlGARELLLAllDKLAA-EGAPTLVLVTHHVEEIPPGIThVLLLKDGRVVAAGPKEE 229
|
..
gi 1541475627 561 LL 562
Cdd:COG1119 230 VL 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
339-570 |
3.96e-26 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 108.02 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 339 GAIAFDNVSFAYRED-RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPvTQGEIRLDGRPLASLSHNVLRKGV 417
Cdd:cd03289 1 GQMTVKDLTAKYTEGgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 418 AMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQV 497
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 498 LILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEAKGRYWQ 570
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
41-568 |
3.97e-26 |
|
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: 114.27 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 41 SGPLLISY---FIDNMVAKSYLPLrLVAGLgvAYVGLQLAAAGLHYAQSLLFnraAVGVvqQLRTDVMDAALRQPL---- 113
Cdd:TIGR00957 335 IGPQILSLlirFVNDPMAPDWQGY-FYTGL--LFVCACLQTLILHQYFHICF---VSGM--RIKTAVMGAVYRKALvitn 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 114 SEFDIQPVGQVISRVTNDTEVIRDLYVTVvaTVLRSAALigAMLVAMFSLdWrmalvaITIFPAVLI---VMIIYQRYST 190
Cdd:TIGR00957 407 SARKSSTVGEIVNLMSVDAQRFMDLATYI--NMIWSAPL--QVILALYFL-W------LNLGPSVLAgvaVMVLMVPLNA 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 191 PIVRRVRAYLA---DINDG----FNEVINGMSVIQQFRQQARF-----GERMGEAS---RSHYMARMQTLRldgFLLRPL 255
Cdd:TIGR00957 476 VMAMKTKTYQVahmKSKDNriklMNEILNGIKVLKLYAWELAFldkveGIRQEELKvlkKSAYLHAVGTFT---WVCTPF 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 256 LslfsaLVLCGLLMLFGLSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVfelmdrpRQAYGHDE-- 333
Cdd:TIGR00957 553 L-----VALITFAVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL-------RIFLSHEEle 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 334 ------RPLQSG---AIAFDNVSFAY-REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGr 403
Cdd:TIGR00957 621 pdsierRTIKPGegnSITVHNATFTWaRDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG- 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 404 plaslshnvlrkGVAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVQL-ADLARgFSDGINTRLGEQGNNLSVGQK 482
Cdd:TIGR00957 700 ------------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALlPDLEI-LPSGDRTEIGEKGVNLSGGQK 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 483 QLLALARVLIETPQVLILDEATASIDSGTEQAIQQAL---AAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHR 559
Cdd:TIGR00957 767 QRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQ 846
|
....*....
gi 1541475627 560 ELLEAKGRY 568
Cdd:TIGR00957 847 ELLQRDGAF 855
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
310-555 |
6.45e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.21 E-value: 6.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 310 QAVVagERVFEL---MDRPRQAYGHDER--PLQSGAIAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLA 384
Cdd:COG4178 329 RATV--DRLAGFeeaLEAADALPEAASRieTSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 385 SLLMGYYPVTQGEIRldgRPLAslshnvlrKGVAMVQQDPVVLADTFYANVT---LGRDYSQEQVWEVLEKVQLADLArg 461
Cdd:COG4178 407 RAIAGLWPYGSGRIA---RPAG--------ARVLFLPQRPYLPLGTLREALLypaTAEAFSDAELREALEAVGLGHLA-- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 462 fsdginTRLGEQ---GNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTI 538
Cdd:COG4178 474 ------ERLDEEadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLA 547
|
250
....*....|....*..
gi 1541475627 539 VDADTILVLHRGQAVER 555
Cdd:COG4178 548 AFHDRVLELTGDGSWQL 564
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
341-561 |
1.15e-25 |
|
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: 105.66 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLDVPsRG-FVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSH---NVLRKG 416
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVR-RGeILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 VAMVQQDPVVLAD-TFYANVTLG-RDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEqgnnLSVGQKQLLALARVLIET 494
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFPlREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE----LSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 495 PQVLILDEATASIDSGTEQAIQQALAAVRDH--TTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHREL 561
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKElgLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-562 |
1.40e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPSRGFVALVGHTGSGKSTLASL---LMGYYPVTQ--GEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLAD- 429
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEARvsGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 430 TFYANVTLG---------RDYSQEQVWEVLEKVQLADlargfsdGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLIL 500
Cdd:PRK14247 98 SIFENVALGlklnrlvksKKELQERVRWALEKAQLWD-------EVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 501 DEATASIDSGTEQAIQQALAAVRDHTTLVVIAH------RLStivdaDTILVLHRGQAVERGTHRELL 562
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREVF 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
340-563 |
1.02e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.11 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYRE-DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYY---PVTQGEIRLDGRPLASLSHNVLRK 415
Cdd:PRK13640 5 IVEFKHVSFTYPDsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 416 GVAMVQQDPvvlaDTFYANVTLG---------RDYSQEQVWEVLEKVqLADLarGFSDGINTrlgeQGNNLSVGQKQLLA 486
Cdd:PRK13640 85 KVGIVFQNP----DNQFVGATVGddvafglenRAVPRPEMIKIVRDV-LADV--GMLDYIDS----EPANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 487 LARVLIETPQVLILDEATASID-SGTEqaiqQALAAVRD-----HTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRE 560
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDpAGKE----QILKLIRKlkkknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
...
gi 1541475627 561 LLE 563
Cdd:PRK13640 230 IFS 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
341-561 |
1.09e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.33 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRE----DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHN----V 412
Cdd:PRK13634 3 ITFQKVEHRYQYktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 413 LRKGVAMVQQDP-------VVLADTFYANVTLG--RDYSQEQVWEVLEKVQLAD--LARGFSDgintrlgeqgnnLSVGQ 481
Cdd:PRK13634 83 LRKKVGIVFQFPehqlfeeTVEKDICFGPMNFGvsEEDAKQKAREMIELVGLPEelLARSPFE------------LSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 482 KQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAV--RDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTH 558
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
...
gi 1541475627 559 REL 561
Cdd:PRK13634 231 REI 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
341-551 |
1.83e-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: 100.34 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREdRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNV--LRKGVA 418
Cdd:cd03229 1 LELKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 419 MVQQDPVVladtfYANVTlgrdysqeqvweVLEKVQLAdlargfsdgintrlgeqgnnLSVGQKQLLALARVLIETPQVL 498
Cdd:cd03229 80 MVFQDFAL-----FPHLT------------VLENIALG--------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 499 ILDEATASIDSGTEQAIQQALAAVRDH--TTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
341-563 |
1.88e-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: 101.93 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNvlRKGVAMV 420
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDPVVLAD-TFYANVTLG-------RDYSQEQVWEVLEKVQLADLARGFSDgintrlgeqgnNLSVGQKQLLALARVLI 492
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlrlkklpKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 493 ETPQVLILDEATASIDSGTEQAIQQALAAVRDH--TTLVVIAHRLS-TIVDADTILVLHRGQAVERGTHRELLE 563
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElgITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
310-547 |
2.12e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 108.58 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 310 QAVVAGERVFELMDR-PRQAYGHDERPLQS-GAIAFDNVSFAY--REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLAS 385
Cdd:PTZ00265 350 KSLEATNSLYEIINRkPLVENNDDGKKLKDiKKIQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILK 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 386 LLMGYYPVTQGEIRL-DGRPLASLSHNVLRKGVAMVQQDPVVLADTFYANVTLG----------RDYSQE---------- 444
Cdd:PTZ00265 430 LIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealSNYYNEdgndsqenkn 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 445 --------------------------------------QVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLA 486
Cdd:PTZ00265 510 krnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRIS 589
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 487 LARVLIETPQVLILDEATASIDSGTEQAIQQALAAVR--DHTTLVVIAHRLSTIVDADTILVL 547
Cdd:PTZ00265 590 IARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
340-565 |
3.88e-24 |
|
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: 101.21 E-value: 3.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYrEDRLVLQDITLDVPsRG-FVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSH---NVLRK 415
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVP-RGeILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 416 GVAMVQQDPVVLAD-TFYANV--------TLGRDYSQEQVWEVLEKVQLADLARGF-SDgintrlgeqgnnLSVGQKQLL 485
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVafplrehtDLSEAEIRELVLEKLELVGLPGAADKMpSE------------LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 486 ALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELL 562
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELL 230
|
...
gi 1541475627 563 EAK 565
Cdd:COG1127 231 ASD 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
344-565 |
6.06e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.39 E-value: 6.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAyREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQD 423
Cdd:PRK13548 6 RNLSVR-LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 424 PVVladTFYANV-----------TLGRDYSQEQVWEVLEKVQLADLArgfsdginTRLGEQgnnLSVGQKQLLALARVLI 492
Cdd:PRK13548 85 SSL---SFPFTVeevvamgraphGLSRAEDDALVAAALAQVDLAHLA--------GRDYPQ---LSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 493 ------ETPQVLILDEATASIDSGTEQAIQQALA--AVRDHTTLVVIAHRLS-TIVDADTILVLHRGQAVERGTHRELLE 563
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARqlAHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
..
gi 1541475627 564 AK 565
Cdd:PRK13548 231 PE 232
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
28-318 |
1.48e-23 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 101.05 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 28 AVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVAGLGVAYVGLQ---LAAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALALLgvfVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 105 MDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMII 184
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 185 YQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPL-----LSLF 259
Cdd:cd18573 161 YGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTgfsgnLSLL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 260 SALVLCGLLMlfglsSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18573 241 SVLYYGGSLV-----ASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
340-566 |
1.87e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.20 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAM 419
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDP--VVLADTFYANVT-------LGRDYSQEQVWEVLEKVQLADLARgfsdgintrlgEQGNNLSVGQKQLLALARV 490
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVAfgpvnmgLDKDEVERRVEEALKAVRMWDFRD-----------KPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 491 LIETPQVLILDEATASIDSGTEQAIQQALAAV-RDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERG-----THRELLE 563
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGdksllTDEDIVE 232
|
...
gi 1541475627 564 AKG 566
Cdd:PRK13647 233 QAG 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
341-565 |
1.87e-23 |
|
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: 99.56 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL---RKGV 417
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 418 AMV-QQDPVVLADTFYANVTLGR---------------DYSQEQVWEVLEKVQLADLArgfsdgiNTRLGEqgnnLSVGQ 481
Cdd:cd03256 81 GMIfQQFNLIERLSVLENVLSGRlgrrstwrslfglfpKEEKQRALAALERVGLLDKA-------YQRADQ----LSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 482 KQLLALARVLIETPQVLILDEATASIDSGTEQAIQQAL--AAVRDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTH 558
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPP 229
|
....*..
gi 1541475627 559 RELLEAK 565
Cdd:cd03256 230 AELTDEV 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
341-560 |
1.95e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.51 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRE----DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNV--LR 414
Cdd:PRK13637 3 IKIENLTHIYMEgtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 415 KGVAMVQQDP--VVLADTFYANVTLG---RDYSQEqvwEVLEKVQLADLARGFSdgINTRLGEQGNNLSVGQKQLLALAR 489
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGpinLGLSEE---EIENRVKRAMNIVGLD--YEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 490 VLIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRE 560
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
344-533 |
2.25e-23 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 98.10 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASlshNVLRKGVAMVQQD 423
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 424 P--VVLADTFYANVTLGRD---YSQEQVWEVLEKVQLADLARgfsdgintrlgEQGNNLSVGQKQLLALARVLIETPQVL 498
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKeldAGNEQAETVLKDLDLYALKE-----------RHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 1541475627 499 ILDEATASIDSGTEQAIQQA---LAAVRdhTTLVVIAH 533
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELireLAAQG--KAVIVITH 184
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
71-318 |
2.63e-23 |
|
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: 100.63 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 71 YVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRS- 149
Cdd:cd18577 53 FVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSl 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 150 AALIGAMLVAmFSLDWRMALVAITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGER 229
Cdd:cd18577 133 STFIAGFIIA-FIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 230 mgeasrshYMARMQTLRLDGFLLRPLLSLFSALVLCGLLMLFGLS--------SSGTIEVG----VLYAFI---SYLGRL 294
Cdd:cd18577 212 --------YSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAfwygsrlvRDGEISPGdvltVFFAVLigaFSLGQI 283
|
250 260
....*....|....*....|....
gi 1541475627 295 NEPLIELTTqqsmlqqAVVAGERV 318
Cdd:cd18577 284 APNLQAFAK-------ARAAAAKI 300
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
22-318 |
4.67e-23 |
|
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: 99.44 E-value: 4.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 22 RKPLSVAVLLLWIAAIAEVSGPLLISYFIDNmvaksYLPLRLVAGL---GVAYVGLQLAAAGLHYAQSLLFNRAAvgvvQ 98
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDD-----IIPSGDINLLniiSIGLILLYLFQSLLSYIRSYLLLKLS----Q 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 99 QLRTDVMDAALRQ----PLSEFDIQPVGQVISRVtNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITI 174
Cdd:cd18570 72 KLDIRLILGYFKHllklPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 175 FPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMgeasrSHYMARMQTLRLDGFLLRP 254
Cdd:cd18570 151 IPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKI-----EKKFSKLLKKSFKLGKLSN 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 255 LLSLFSALV-LCGLLMLFGLSS----SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18570 226 LQSSIKGLIsLIGSLLILWIGSylviKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
120-561 |
5.19e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 104.29 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 120 PVGQVISRVTNDTEVIRDLyvtvvatvlrsAALIGAMLVAMFSLDWRMAL------VAITIFPAVLIVMIIYQrysTPIV 193
Cdd:PLN03232 396 ASGKVTNMITTDANALQQI-----------AEQLHGLWSAPFRIIVSMVLlyqqlgVASLFGSLILFLLIPLQ---TLIV 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 194 RRVRA------YLADINDGF-NEVINGMSVIQQFRQQARFgermgeasrshyMARMQTLR---LDGFLLRPLLSLFSALV 263
Cdd:PLN03232 462 RKMRKltkeglQWTDKRVGIiNEILASMDTVKCYAWEKSF------------ESRIQGIRneeLSWFRKAQLLSAFNSFI 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 264 LCGLLMLFGLSSSGTIEV--GVL-----YAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDRPRQAYGHDErPL 336
Cdd:PLN03232 530 LNSIPVVVTLVSFGVFVLlgGDLtparaFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNP-PL 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 337 QSG--AIAFDNVSFAY--REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMgyypvtqGEIrldgrPLASLSHNV 412
Cdd:PLN03232 609 QPGapAISIKNGYFSWdsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML-------GEL-----SHAETSSVV 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 413 LRKGVAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLI 492
Cdd:PLN03232 677 IRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVY 756
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 493 ETPQVLILDEATASIDSG-TEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHREL 561
Cdd:PLN03232 757 SNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
336-564 |
6.57e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.20 E-value: 6.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 336 LQSGAIAFD--NVS--FAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLA----- 406
Cdd:PRK14246 1 MEAGKSAEDvfNISrlYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 407 -SLSHNVLRKGVAMVQQDPVVLAD-TFYANVTLG-RDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQ 483
Cdd:PRK14246 81 fQIDAIKLRKEVGMVFQQPNPFPHlSIYDNIAYPlKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 484 LLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELL 562
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
..
gi 1541475627 563 EA 564
Cdd:PRK14246 241 TS 242
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
350-563 |
7.53e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.99 E-value: 7.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 350 YREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLAS-----LLMGYYPVTQGEIRLDGRPLASLSHNVL--RKGVAMVQQ 422
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDVDPIevRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 423 DPVVLAD-TFYANVTLGRDYSQ--EQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLI 499
Cdd:PRK14267 93 YPNPFPHlTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 500 LDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLE 563
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
340-554 |
1.19e-22 |
|
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: 96.73 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAY--REDRL-VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHN----V 412
Cdd:COG4181 8 IIELRGLTKTVgtGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDararL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 413 LRKGVAMVQQDPVVLAdTFYA--NVTL-----GRDYSQEQVWEVLEKVQLADlargfsdgintRLGEQGNNLSVGQKQLL 485
Cdd:COG4181 88 RARHVGFVFQSFQLLP-TLTAleNVMLplelaGRRDARARARALLERVGLGH-----------RLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 486 ALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVDADTILVLHRGQAVE 554
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
341-556 |
1.82e-22 |
|
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: 95.31 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRED-----RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGY--YPVTQGEIRLDGRPlasLSHNVL 413
Cdd:cd03213 4 LSFRNLTVTVKSSpsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRP---LDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 414 RKGVAMVQQDpvvlaDTFYANVTlgrdysqeqVWEVLekvQLADLARGfsdgintrlgeqgnnLSVGQKQLLALARVLIE 493
Cdd:cd03213 81 RKIIGYVPQD-----DILHPTLT---------VRETL---MFAAKLRG---------------LSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 494 TPQVLILDEATASIDSGTEQAIQQALAAVRD-HTTLVVIAHRLSTIV--DADTILVLHRGQAVERG 556
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
341-561 |
3.65e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 96.70 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRED-----RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPlASLSHNV--L 413
Cdd:PRK13633 5 IKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLwdI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 414 RKGVAMVQQDP-------VVLADTFYANVTLGRDYSQ--EQVWEVLEKVQLADLARgfsdgintrlgEQGNNLSVGQKQL 484
Cdd:PRK13633 84 RNKAGMVFQNPdnqivatIVEEDVAFGPENLGIPPEEirERVDESLKKVGMYEYRR-----------HAPHLLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 485 LALARVLIETPQVLILDEATASID-SGTEQAIQQALAAVR-DHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHREL 561
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDpSGRREVVNTIKELNKkYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
341-562 |
4.63e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.21 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRLvlqDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLShnVLRKGVAMV 420
Cdd:COG3840 2 LRLDDLTYRYGDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP--PAERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDPVVLAD-TFYANVTLGRDYS-------QEQVWEVLEKVQLADLArgfsdginTRLGEQgnnLSVGQKQLLALARVLI 492
Cdd:COG3840 77 FQENNLFPHlTVAQNIGLGLRPGlkltaeqRAQVEQALERVGLAGLL--------DRLPGQ---LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 493 -ETPqVLILDEATASIDSGTEQAIQQALAAVRDHT--TLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELL 562
Cdd:COG3840 146 rKRP-ILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
341-557 |
5.01e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 97.46 E-value: 5.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDR---LVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL---R 414
Cdd:COG1135 2 IELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 415 KGVAMV-QQDPVVLADTFYANVTL-------GRDYSQEQVWEVLEKVQLADLARGFSDgintrlgeqgnNLSVGQKQLLA 486
Cdd:COG1135 82 RKIGMIfQHFNLLSSRTVAENVALpleiagvPKAEIRKRVAELLELVGLSDKADAYPS-----------QLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 487 LARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGT 557
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
340-565 |
6.15e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 95.97 E-value: 6.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYRE----DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHN---- 411
Cdd:PRK13649 2 GINLQNVSYTYQAgtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 412 VLRKGVAMVQQDP--VVLADTFYANVTLGRD---YSQEQVwEVLEKVQLADLargfsdGINTRLGEQGN-NLSVGQKQLL 485
Cdd:PRK13649 82 QIRKKVGLVFQFPesQLFEETVLKDVAFGPQnfgVSQEEA-EALAREKLALV------GISESLFEKNPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 486 ALARVLIETPQVLILDEATASIDSGTEQAIQQALAAV-RDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGT------ 557
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKpkdifq 234
|
....*...
gi 1541475627 558 HRELLEAK 565
Cdd:PRK13649 235 DVDFLEEK 242
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
357-559 |
8.04e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.95 E-value: 8.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 357 LQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS-HNVLRKGVAMVQQDPvVLADTF--YA 433
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHF-MLVPNLtvAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 434 NVTLGRDYSQEQV--WEVLEKvQLADLARGFsdGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIdsgT 511
Cdd:COG3845 100 NIVLGLEPTKGGRldRKAARA-RIRELSERY--GLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL---T 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 512 EQAIQQALAAVR----DHTTLVVIAHRLSTIVD-ADTILVLHRGQAVerGTHR 559
Cdd:COG3845 174 PQEADELFEILRrlaaEGKSIIFITHKLREVMAiADRVTVLRRGKVV--GTVD 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
341-561 |
1.39e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.18 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRED--RLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASlsHNV--LRKG 416
Cdd:PRK13650 5 IEVKNLTFKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE--ENVwdIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 VAMVQQDP-------VVLADTFYA--NVTLGRDYSQEQVWEVLEKVQLADlargFSDGINTRLgeqgnnlSVGQKQLLAL 487
Cdd:PRK13650 83 IGMVFQNPdnqfvgaTVEDDVAFGleNKGIPHEEMKERVNEALELVGMQD----FKEREPARL-------SGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 488 ARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIA--HRLSTIVDADTILVLHRGQAVERGTHREL 561
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISitHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
341-562 |
2.12e-21 |
|
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: 93.52 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMV 420
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 -QQDPVVLADTFYANVTL-------GRDYSQEQVWEVLEKVQL--ADLARGFSDgintrlgeqgnNLSVGQKQLLALARV 490
Cdd:cd03295 81 iQQIGLFPHMTVEENIALvpkllkwPKEKIRERADELLALVGLdpAEFADRYPH-----------ELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 491 LIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRL-STIVDADTILVLHRGQAVERGTHRELL 562
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
34-302 |
2.46e-21 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 94.44 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 34 IAAIAEVSGPLLISYFIDNmvaksYLP---LRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALR 110
Cdd:cd18549 13 LIAALDLVFPLIVRYIIDD-----LLPsknLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 111 QPLSEFDIQPVGQVISRVTND----TEVI----RDLYVTVVatvlrsaALIGAMLVaMFSLDWRMALVAITIFPAVLIVM 182
Cdd:cd18549 88 LSFSFFDNNKTGQLMSRITNDlfdiSELAhhgpEDLFISII-------TIIGSFII-LLTINVPLTLIVFALLPLMIIFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 183 IIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGF------LLRPLL 256
Cdd:cd18549 160 IYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYffsgmnFFTNLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1541475627 257 SLFsALVLCGLLMLfglssSGTIEVGVLYAFISYLGRLNEPLIELT 302
Cdd:cd18549 240 NLV-VLVAGGYFII-----KGEITLGDLVAFLLYVNVFIKPIRRLV 279
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
334-559 |
2.56e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.59 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 334 RPLQSGAIAFDNVSFAYREdRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASlshnvL 413
Cdd:PRK11247 6 RLNQGTPLLLNAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 414 RKGVAMVQQDPVVLA-DTFYANVTLG-RDYSQEQVWEVLEKVQLADlargfsdgintRLGEQGNNLSVGQKQLLALARVL 491
Cdd:PRK11247 80 REDTRLMFQDARLLPwKKVIDNVGLGlKGQWRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 492 IETPQVLILDEATASIDSGTEQAIQQALAAV--RDHTTLVVIAHRLSTIVD-ADTILVLHRGQ-----AVE------RGT 557
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSEAVAmADRVLLIEEGKigldlTVDlprprrRGS 228
|
..
gi 1541475627 558 HR 559
Cdd:PRK11247 229 AR 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
340-565 |
2.57e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.51 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYRE----DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHN---- 411
Cdd:PRK13641 2 SIKFENVDYIYSPgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 412 VLRKGVAMVQQDP-------VVLADTFYANVTLG--RDYSQEQVWEVLEKVQLADlargfsDGINTRLGEqgnnLSVGQK 482
Cdd:PRK13641 82 KLRKKVSLVFQFPeaqlfenTVLKDVEFGPKNFGfsEDEAKEKALKWLKKVGLSE------DLISKSPFE----LSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 483 QLLALARVLIETPQVLILDEATASID-SGTEQAIQQALAAVRDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRE 560
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDpEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKE 231
|
....*
gi 1541475627 561 LLEAK 565
Cdd:PRK13641 232 IFSDK 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
341-554 |
4.50e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.21 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRL--------VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS--- 409
Cdd:PRK10419 4 LNVSGLSHHYAHGGLsgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 410 HNVLRKGVAMVQQDPV-----------VLADTFYANVTLGRDYSQEQVWEVLEKVQLAdlargfsDGINTRLGEQgnnLS 478
Cdd:PRK10419 84 RKAFRRDIQMVFQDSIsavnprktvreIIREPLRHLLSLDKAERLARASEMLRAVDLD-------DSVLDKRPPQ---LS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 479 VGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDH--TTLVVIAHRLStIVD--ADTILVLHRGQAVE 554
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfgTACLFITHDLR-LVErfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
344-562 |
4.54e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.62 E-value: 4.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYREDRLV--LQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQ 421
Cdd:PRK13642 8 ENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 422 QDP--VVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARGFSDgINTRlgeQGNNLSVGQKQLLALARVLIETPQVLI 499
Cdd:PRK13642 88 QNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLD-FKTR---EPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 500 LDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELL 562
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
320-561 |
5.73e-21 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 93.38 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 320 ELMDRPRQAYGHDERPLQSGAIAFDNVSFAYREdrlVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIR 399
Cdd:cd03291 19 ELLEKAKQENNDRKHSSDDNNLFFSNLCLVGAP---VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 400 LDGRplaslshnvlrkgVAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSV 479
Cdd:cd03291 96 HSGR-------------ISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 480 GQKQLLALARVLIETPQVLILDEATASIDSGTEQAI-QQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTH 558
Cdd:cd03291 163 GQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTF 242
|
...
gi 1541475627 559 REL 561
Cdd:cd03291 243 SEL 245
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
308-561 |
7.33e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 97.50 E-value: 7.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 308 LQQAVVAGERVfeLMDRPrqayghderPLQSG--AIAFDNVSFAY--REDRLVLQDITLDVPSRGFVALVGHTGSGKSTL 383
Cdd:PLN03130 591 LEELLLAEERV--LLPNP---------PLEPGlpAISIKNGYFSWdsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSL 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 384 ASLLMGYYPVTqgeirldgrplaSLSHNVLRKGVAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVQLA---DLAR 460
Cdd:PLN03130 660 ISAMLGELPPR------------SDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQhdlDLLP 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 461 GfsdGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGT-EQAIQQALAAVRDHTTLVVIAHRLSTIV 539
Cdd:PLN03130 728 G---GDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgRQVFDKCIKDELRGKTRVLVTNQLHFLS 804
|
250 260
....*....|....*....|..
gi 1541475627 540 DADTILVLHRGQAVERGTHREL 561
Cdd:PLN03130 805 QVDRIILVHEGMIKEEGTYEEL 826
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
340-564 |
8.20e-21 |
|
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: 91.63 E-value: 8.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLAslSHNVLRKGVAM 419
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDPVVLAD-TFYANVTLG-----------RDYSQEQVWEVLEKVQLADLARGFSdgintrlgeqgNNLSVGQKQLLAL 487
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAFGlrvkprserppEAEIRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 488 ARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLEA 564
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
339-561 |
1.29e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.60 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 339 GAIAFDNVSFAYREDRlVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLShnVLRKGVA 418
Cdd:COG3839 2 ASLELENVSKSYGGVE-ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP--PKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 419 MVQQDPVV---LadTFYANVTLG---RDYS----QEQVWEVLEKVQLADLARgfsdgintRLGEQgnnLSVGQKQLLALA 488
Cdd:COG3839 79 MVFQSYALyphM--TVYENIAFPlklRKVPkaeiDRRVREAAELLGLEDLLD--------RKPKQ---LSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 489 RVLIETPQVLILDEATASIDSG------TE-QAIQQALAavrdhTTLVVIAHrlstivD-------ADTILVLHRGQAVE 554
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRLG-----TTTIYVTH------DqveamtlADRIAVMNDGRIQQ 214
|
....*..
gi 1541475627 555 RGTHREL 561
Cdd:COG3839 215 VGTPEEL 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
357-564 |
2.89e-20 |
|
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: 94.37 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 357 LQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPvTQGEIRLDGRPLASLSHNV---LRKGVAMVQQDPvvladtfYA 433
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDP-------FG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 434 -------------------NVTLGRDYSQEQVWEVLEKVQLADLARG-----FSdgintrlgeqGnnlsvGQKQLLALAR 489
Cdd:COG4172 374 slsprmtvgqiiaeglrvhGPGLSAAERRARVAEALEEVGLDPAARHrypheFS----------G-----GQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 490 VLIETPQVLILDEATASIDSgTEQAiqQALAAVRD-----HTTLVVIAHRLStIVDA--DTILVLHRGQAVERGTHRELL 562
Cdd:COG4172 439 ALILEPKLLVLDEPTSALDV-SVQA--QILDLLRDlqrehGLAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPTEQVF 514
|
..
gi 1541475627 563 EA 564
Cdd:COG4172 515 DA 516
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
353-556 |
3.41e-20 |
|
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: 89.20 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 353 DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGrPLASLSHNVLRKGVAMVQqdpvvlADTFY 432
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-KSYQKNIEALRRIGALIE------APGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 433 ANVT---------LGRDYSQEQVWEVLEKVQLADLARgfsdgintrlgEQGNNLSVGQKQLLALARVLIETPQVLILDEA 503
Cdd:cd03268 85 PNLTarenlrllaRLLGIRKKRIDEVLDVVGLKDSAK-----------KKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 504 TASIDSGTEQAIQQALAAVRDHTTLVVIA-HRLSTIVD-ADTILVLHRGQAVERG 556
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
341-563 |
5.05e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.56 E-value: 5.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDR----LVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNV---- 412
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 413 LRKGVAMVQQDP-------VVLADTFYANVTLGrdYSQEQVWEV-LEKVQLADLARGFSDgintrlgEQGNNLSVGQKQL 484
Cdd:PRK13643 82 VRKKVGVVFQFPesqlfeeTVLKDVAFGPQNFG--IPKEKAEKIaAEKLEMVGLADEFWE-------KSPFELSGGQMRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 485 LALARVLIETPQVLILDEATASIDSGTEQAIQQALAAV-RDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELL 562
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVF 232
|
.
gi 1541475627 563 E 563
Cdd:PRK13643 233 Q 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
344-563 |
6.67e-20 |
|
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: 88.93 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYREdrLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNvlRKGVAMVQQD 423
Cdd:cd03299 4 ENLSKDWKE--FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 424 PVVLAD-TFYANVTLGRDYSQEQVWEVLEKV-QLADLArgfsdGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILD 501
Cdd:cd03299 80 YALFPHmTVYKNIAYGLKKRKVDKKEIERKVlEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 502 EATASIDSGTEQAIQQALAAVRDH--TTLVVIAHRLSTI-VDADTILVLHRGQAVERGTHRELLE 563
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfgVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
348-550 |
1.06e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 88.16 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 348 FAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEI----RLDGRPLASLSHNVLRKGVAMVQQD 423
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 424 PVVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEA 503
Cdd:cd03290 88 PWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1541475627 504 TASIDSGTEQAIQQA--LAAVR-DHTTLVVIAHRLSTIVDADTILVLHRG 550
Cdd:cd03290 168 FSALDIHLSDHLMQEgiLKFLQdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-564 |
1.20e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.38 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLL-------MGYYpvTQGEIRLDGRPLASLsHNV 412
Cdd:PRK14271 21 AMAAVNLTLGF-AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYR--YSGDVLLGGRSIFNY-RDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 413 L--RKGVAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLAR-GFSDGINTRLGEQGNNLSVGQKQLLALAR 489
Cdd:PRK14271 97 LefRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEvGLWDAVKDRLSDSPFRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 490 VLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLEA 564
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
336-565 |
1.43e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.14 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 336 LQSGAIAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNV--L 413
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLmkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 414 RKGVAMVQQDP-------VVLADTFYA--NVTLGRDYSQEQVWEVLEKVQLADLARgfsdgintrlgEQGNNLSVGQKQL 484
Cdd:PRK13636 81 RESVGMVFQDPdnqlfsaSVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKD-----------KPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 485 LALARVLIETPQVLILDEATASIDS-GTEQAIQQALAAVRD-HTTLVVIAHRLSTI-VDADTILVLHRGQAVERGTHREL 561
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPmGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEV 229
|
....
gi 1541475627 562 LEAK 565
Cdd:PRK13636 230 FAEK 233
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
25-322 |
1.50e-19 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 89.49 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVagLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYY--LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 105 MDAALRQPLSEFDIQPVGQVISRVTNDTEVI-RDLYVTVVATVLRSAALIGAMLVAMFSLDWrmalVAITIFPaVLIVMI 183
Cdd:cd18580 79 LRSVLRAPMSFFDTTPSGRILNRFSKDIGLIdEELPLALLDFLQSLFSVLGSLIVIAIVSPY----FLIVLPP-LLVVYY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 184 IYQRYSTPIVRRVR----AYLADINDGFNEVINGMSVIQQFRQQARFGERMGE----ASRSHYM----ARMQTLRLDgfl 251
Cdd:cd18580 154 LLQRYYLRTSRQLRrlesESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRlldaSQRAFYLllavQRWLGLRLD--- 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 252 lrpLLSLFSALVLCGLLMLFGLSSSGTIeVGVLyafISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM 322
Cdd:cd18580 231 ---LLGALLALVVALLAVLLRSSISAGL-VGLA---LTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
341-551 |
2.48e-19 |
|
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: 86.81 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNV--LRKGVA 418
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 419 MVQQDPVVLAD-TFYANVTLG--------RDYSQEQVWEVLEKVQLADLARGFSdgintrlgeqgNNLSVGQKQLLALAR 489
Cdd:cd03262 80 MVFQQFNLFPHlTVLENITLApikvkgmsKAEAEERALELLEKVGLADKADAYP-----------AQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 490 VLIETPQVLILDEATASIDS---GTEQAIQQALAavRDHTTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPelvGEVLDVMKDLA--EEGMTMVVVTHEMGFAREvADRVIFMDDGR 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
341-557 |
2.90e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.47 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDR---LVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL---R 414
Cdd:PRK11153 2 IELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 415 KGVAMVQQDPVVLAD-TFYANVTL-------GRDYSQEQVWEVLEKVQLADLARGFSdgintrlgeqgNNLSVGQKQLLA 486
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALplelagtPKAEIKARVTELLELVGLSDKADRYP-----------AQLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 487 LARVLIETPQVLILDEATASIDSGTEQAIQQALAAV--RDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGT 557
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
341-556 |
5.50e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 85.80 E-value: 5.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRlVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL------- 413
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIgylpeer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 414 ---RKgvAMVQQDPVVLADTFyanvTLGRDYSQEQVWEVLEKVQLADLArgfsdgiNTRLGEqgnnLSVGQKQLLALARV 490
Cdd:cd03269 80 glyPK--MKVIDQLVYLAQLK----GLKKEEARRRIDEWLERLELSEYA-------NKRVEE----LSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 491 LIETPQVLILDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVERG 556
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
341-562 |
7.90e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.96 E-value: 7.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSH-NVLRKGVAM 419
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDPvvlaDTFYANVTLGRDYS---QEQVWEVLEKVQLADLARGfSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQ 496
Cdd:PRK13644 82 VFQNP----ETQFVGRTVEEDLAfgpENLCLPPIEIRKRVDRALA-EIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 497 VLILDEATASIDSGTEQAIQQALAAV-RDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELL 562
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
341-564 |
7.99e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 88.28 E-value: 7.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRLvLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASlSHNVLRKGVAMV 420
Cdd:COG1118 3 IEVRNISKRFGSFTL-LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-NLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDpvvladtfYA---------NV-------TLGRDYSQEQVWEVLEKVQLADLARgfsdgintRLGEQgnnLSVGQKQL 484
Cdd:COG1118 81 FQH--------YAlfphmtvaeNIafglrvrPPSKAEIRARVEELLELVQLEGLAD--------RYPSQ---LSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 485 LALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRD---HTTLVVI-----AHRLstivdADTILVLHRGQAVERG 556
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelgGTTVFVThdqeeALEL-----ADRVVVMNQGRIEQVG 216
|
....*...
gi 1541475627 557 THRELLEA 564
Cdd:COG1118 217 TPDEVYDR 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
336-556 |
9.02e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.48 E-value: 9.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 336 LQSGAIAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPlaslSHNVLRK 415
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP----TRQALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 416 G-VAMVQQD-------PVVLADTfyanVTLGR-----------DYSQEQVWEVLEKVQLADLArgfsdgiNTRLGEqgnn 476
Cdd:PRK15056 78 NlVAYVPQSeevdwsfPVLVEDV----VMMGRyghmgwlrrakKRDRQIVTAALARVDMVEFR-------HRQIGE---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 477 LSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTIVDADTILVLHRGQAVER 555
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLAS 222
|
.
gi 1541475627 556 G 556
Cdd:PRK15056 223 G 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
349-566 |
1.06e-18 |
|
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: 84.50 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 349 AYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMG--YYPVTQGEIRLDGRPLASLS-HNVLRKGVAMVQQDPV 425
Cdd:cd03217 8 VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPpEERARLGIFLAFQYPP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 426 vladtfyanvtlgrdysqeqvwEVlEKVQLADLARGFSDGintrlgeqgnnLSVGQKQLLALARVLIETPQVLILDEata 505
Cdd:cd03217 88 ----------------------EI-PGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDE--- 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 506 sIDSGTE----QAIQQALAAVRD-HTTLVVIAH--RLSTIVDADTILVLHRGQAVERGThREL---LEAKG 566
Cdd:cd03217 131 -PDSGLDidalRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELaleIEKKG 199
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
341-556 |
1.13e-18 |
|
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: 84.85 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRLvlqDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLShnVLRKGVAMV 420
Cdd:cd03298 1 VRLDKIRFSYGEQPM---HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP--PADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDPVVLAD-TFYANVTLGRDYSQEQVWEVLEKVQLAdLARGFSDGINTRLGEQgnnLSVGQKQLLALARVLIETPQVLI 499
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGLSPGLKLTAEDRQAIEVA-LARVGLAGLEKRLPGE---LSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 500 LDEATASIDSGTEQAIQQALAAVRDHT--TLVVIAHRLSTIVD-ADTILVLHRGQAVERG 556
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
302-561 |
1.25e-18 |
|
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: 90.35 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 302 TTQQSMLQQAVVAGERVFELMDRPRQAYGHDERPLQSGAIAFDNVSFAYREdrlVLQDITLDVPSRGFVALVGHTGSGKS 381
Cdd:TIGR01271 390 TTEVEMVNVTASWDEGIGELFEKIKQNNKARKQPNGDDGLFFSNFSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKS 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 382 TLASLLMGYYPVTQGEIRLDGRplaslshnvlrkgVAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARG 461
Cdd:TIGR01271 467 SLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIAL 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 462 FSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAI-QQALAAVRDHTTLVVIAHRLSTIVD 540
Cdd:TIGR01271 534 FPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK 613
|
250 260
....*....|....*....|.
gi 1541475627 541 ADTILVLHRGQAVERGTHREL 561
Cdd:TIGR01271 614 ADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
28-290 |
1.84e-18 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 86.00 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 28 AVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPL--RLVAGLGVAYVGLQLAAAGLHYAQSLLFNRaavgVVQQLRTDVM 105
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALlnRAFLLLLAVALVLALASALRFYLVSWLGER----VVADLRKAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 106 DAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAA-LIGAmLVAMFSLDWRMALVAITIFPAVLIVMII 184
Cdd:cd18575 77 AHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLlLIGG-LVMLFITSPKLTLLVLLVIPLVVLPIIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 185 YQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLrpLLSLFSALVL 264
Cdd:cd18575 156 FGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLT--ALVIFLVFGA 233
|
250 260
....*....|....*....|....*...
gi 1541475627 265 CGLLMLFGLSS--SGTIEVGVLYAFISY 290
Cdd:cd18575 234 IVFVLWLGAHDvlAGRMSAGELSQFVFY 261
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
342-564 |
1.86e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 85.61 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 342 AFDNVSFAYREdrlvlqditldvpsRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQ 421
Cdd:PRK15112 28 AVKPLSFTLRE--------------GQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 422 QDPV-----------VLADTFYANVTLGRDYSQEQVWEVLEKVQL-ADLARGFSdgintrlgeqgNNLSVGQKQLLALAR 489
Cdd:PRK15112 94 QDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYP-----------HMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 490 VLIETPQVLILDEATASID-SGTEQAIQQALAAVRDH--TTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLEA 564
Cdd:PRK15112 163 ALILRPKVIIADEALASLDmSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
350-535 |
2.02e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.21 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 350 YREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLL--MG-YYP--VTQGEIRLDGRPLASLSHNV--LRKGVAMVQQ 422
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdLNPevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 423 DPVVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLaRGFS--DGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLIL 500
Cdd:PRK14239 94 QPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSL-KGASiwDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1541475627 501 DEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRL 535
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
345-561 |
4.75e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 84.36 E-value: 4.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 345 NVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL--RKGVAMVQQ 422
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 423 D-------PVVLADTFYA--NVTLGRDYSQEQVWEVLEKVQLADLARgfsdgintrlgEQGNNLSVGQKQLLALARVLIE 493
Cdd:PRK13639 86 NpddqlfaPTVEEDVAFGplNLGLSKEEVEKRVKEALKAVGMEGFEN-----------KPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 494 TPQVLILDEATASIDSGTEQAIQQALAAV-RDHTTLVVIAHRLSTI-VDADTILVLHRGQAVERGTHREL 561
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
352-547 |
6.30e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.90 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 352 EDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEI-RLDGRPLASLshnvlrkgvamVQQdpVVLADT 430
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVrRAGGARVAYV-----------PQR--SEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 431 FYANV----TLGRdYSQEQVW------------EVLEKVQLADLARgfsdginTRLGEqgnnLSVGQKQLLALARVLIET 494
Cdd:NF040873 70 LPLTVrdlvAMGR-WARRGLWrrltrddraavdDALERVGLADLAG-------RQLGE----LSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 495 PQVLILDEATASIDSGTEQAIQQALA-AVRDHTTLVVIAHRLSTIVDADTILVL 547
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAeEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
341-576 |
1.51e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 83.29 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYRE----DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHN----V 412
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 413 LRKGVAMVQQDP--VVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQgnnLSVGQKQLLALARV 490
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQ---MSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 491 LIETPQVLILDEATASIDSGTEQAIQQALAA--VRDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLeAKGR 567
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF-KDKK 238
|
....*....
gi 1541475627 568 YWQMYQLQL 576
Cdd:PRK13646 239 KLADWHIGL 247
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
71-325 |
2.31e-17 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 83.27 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 71 YVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDiQP---VGQVISRVTNDTEVIRDLYVTVVATVL 147
Cdd:cd18578 58 FLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFD-DPensTGALTSRLSTDASDVRGLVGDRLGLIL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 148 RS-AALIGAMLVAmFSLDWRMALVAITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARF 226
Cdd:cd18578 137 QAiVTLVAGLIIA-FVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 227 GERMGEASRSHYMARMQTLRLDGFLLRplLSLFSALVLCGLLMLFG--LSSSGTIEVG----VLYAFI---SYLGRlnep 297
Cdd:cd18578 216 LEKYEEALEEPLKKGLRRALISGLGFG--LSQSLTFFAYALAFWYGgrLVANGEYTFEqffiVFMALIfgaQSAGQ---- 289
|
250 260
....*....|....*....|....*...
gi 1541475627 298 lieLTTQQSMLQQAVVAGERVFELMDRP 325
Cdd:cd18578 290 ---AFSFAPDIAKAKAAAARIFRLLDRK 314
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
338-553 |
2.78e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.98 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 338 SGAIAFDNVSFAYREDRLVlqditldvpsrgfvALVGHTGSGKSTLASLLMGYYPVT--QGEIRLDGRPLAslSHNVL-- 413
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIV--------------SLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQ--ASNIRdt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 414 -RKGVAMVQQDPVVLAD-TFYANVTLGR--------DYSQ--EQVWEVLEKVQLadlargfsdGIN--TRLGeqgnNLSV 479
Cdd:PRK13549 80 eRAGIAIIHQELALVKElSVLENIFLGNeitpggimDYDAmyLRAQKLLAQLKL---------DINpaTPVG----NLGL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 480 GQKQLLALARVLIETPQVLILDEATASIdsgTEQAIQQALAAVRD----HTTLVVIAHRLSTIVD-ADTILVLHRGQAV 553
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASL---TESETAVLLDIIRDlkahGIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
341-554 |
3.07e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.91 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTL----ASLLMgyyPvTQGEIRLDGRPLASLSHNVLRKG 416
Cdd:PRK10247 8 LQLQNVGYLA-GDAKILNNISFSLRAGEFKLITGPSGCGKSTLlkivASLIS---P-TSGTLLFEGEDISTLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 VAMVQQDPVVLADTFYANVTLGRDYSQEQvweVLEKVQLADLAR-GFSDGIntrLGEQGNNLSVGQKQLLALARVLIETP 495
Cdd:PRK10247 83 VSYCAQTPTLFGDTVYDNLIFPWQIRNQQ---PDPAIFLDDLERfALPDTI---LTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 496 QVLILDEATASIDSGTEQAIQQALAA-VRDHTTLVV-IAHRLSTIVDADTILVL--HRGQAVE 554
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVITLqpHAGEMQE 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
353-561 |
4.14e-17 |
|
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: 80.63 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 353 DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVlRKGVAMVQQDpvvlaDTFY 432
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA-RQSLGYCPQF-----DALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 433 ANVT-------------LGRDYSQEQVWEVLEKVQLADLArgfsdgiNTRLGeqgnNLSVGQKQLLALARVLIETPQVLI 499
Cdd:cd03263 88 DELTvrehlrfyarlkgLPKSEIKEEVELLLRVLGLTDKA-------NKRAR----TLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 500 LDEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRLSTI-VDADTILVLHRGQAVERGTHREL 561
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
344-556 |
7.43e-17 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 79.61 E-value: 7.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNvlRKGVAMVQQD 423
Cdd:cd03301 4 ENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 424 PVVLAD-TFYANVTLG-------RDYSQEQVWEVLEKVQLADLargfsdgintrLGEQGNNLSVGQKQLLALARVLIETP 495
Cdd:cd03301 81 YALYPHmTVYDNIAFGlklrkvpKDEIDERVREVAELLQIEHL-----------LDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 496 QVLILDEATASIDSGTEQA-------IQQALAAvrdhTTLVVIAHRLSTIVDADTILVLHRGQAVERG 556
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQmraelkrLQQRLGT----TTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
351-553 |
7.64e-17 |
|
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: 80.01 E-value: 7.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 351 REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMG---YYPVTQGEIRLDGRPLaslSHNVLRKGVAMVQQDPVVL 427
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPR---KPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 428 AD-------TFYANVTLGRDYSQEQVWEVLEKVQLADLArgfsdgiNTRLGEQG-NNLSVGQKQLLALARVLIETPQVLI 499
Cdd:cd03234 94 PGltvretlTYTAILRLPRKSSDAIRKKRVEDVLLRDLA-------LTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 500 LDEATASIDSGTEQAIQQALA--AVRDHTTLVVIAHRLSTIVDA-DTILVLHRGQAV 553
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSqlARRNRIVILTIHQPRSDLFRLfDRILLLSSGEIV 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
357-563 |
8.75e-17 |
|
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: 80.77 E-value: 8.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 357 LQDITLDVpSRG--FVaLVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL----RKGVAMVQQDPVVLAD- 429
Cdd:cd03294 40 VNDVSLDV-REGeiFV-IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 430 TFYANVTLG-------RDYSQEQVWEVLEKVQLADLARGFSDgintrlgeqgnNLSVGQKQLLALARVLIETPQVLILDE 502
Cdd:cd03294 118 TVLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 503 ATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLE 563
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAelQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
340-509 |
1.33e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.67 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYREDRlVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLsHNVLRKgVAM 419
Cdd:PRK10851 2 SIEIANIKKSFGRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL-HARDRK-VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDPVVLAD-TFYANVTLG-----------RDYSQEQVWEVLEKVQLADLArgfsdginTRLGEQgnnLSVGQKQLLAL 487
Cdd:PRK10851 79 VFQHYALFRHmTVFDNIAFGltvlprrerpnAAAIKAKVTQLLEMVQLAHLA--------DRYPAQ---LSGGQKQRVAL 147
|
170 180
....*....|....*....|..
gi 1541475627 488 ARVLIETPQVLILDEATASIDS 509
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDA 169
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
341-564 |
1.33e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYR---EDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPV-----TQGEIRLDGRPLASLSHNV 412
Cdd:PRK15134 6 LAIENLSVAFRqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 413 LRK----GVAMVQQDPVV-------LADTFYANVTLGRDYSQE----QVWEVLEKVQLADLARgfsdgintRLGEQGNNL 477
Cdd:PRK15134 86 LRGvrgnKIAMIFQEPMVslnplhtLEKQLYEVLSLHRGMRREaargEILNCLDRVGIRQAAK--------RLTDYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 478 SVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLStIVD--ADTILVLHRGQAV 553
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLS-IVRklADRVAVMQNGRCV 236
|
250
....*....|.
gi 1541475627 554 ERGTHRELLEA 564
Cdd:PRK15134 237 EQNRAATLFSA 247
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-562 |
1.34e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.08 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYREDRlVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVtQGEIRLDGRPL--------ASLSHN 411
Cdd:PRK14258 7 AIKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRVEffnqniyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 412 VLRKGVAMVQQDPVVLADTFYANVTLG-RDYSQEQVWEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARV 490
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 491 LIETPQVLILDEATASIDSGTEQAIQQAL--AAVRDHTTLVVIAHRLSTIVD-ADTILVLHR-----GQAVERGTHRELL 562
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGLTKKIF 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
357-556 |
1.36e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.91 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 357 LQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRK-GVAMVQQDPVVLAD-TFYAN 434
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 435 VTLGR------------DYS--QEQVWEVLEKVqladlargfsdGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLIL 500
Cdd:PRK09700 101 LYIGRhltkkvcgvniiDWRemRVRAAMMLLRV-----------GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 501 DEATASIdsgTEQAIQQALAAVR----DHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERG 556
Cdd:PRK09700 170 DEPTSSL---TNKEVDYLFLIMNqlrkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
356-551 |
1.50e-16 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 77.86 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS-HNVLRKGVAMVQQDP----VVLADT 430
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 431 FYANVTLGRDysqeqvwevlekvqladlargfsdgintrlgeqgnnLSVGQKQLLALARVLIETPQVLILDEATASIDSG 510
Cdd:cd03215 95 VAENIALSSL------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1541475627 511 TEQAIQQALAAVRDH-TTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:cd03215 139 AKAEIYRLIRELADAgKAVLLISSELDELLGlCDRILVMYEGR 181
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
341-534 |
1.98e-16 |
|
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: 77.19 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIrldGRPLaslshnvlRKGVAMV 420
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPE--------GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDPvvladtFYANVTLgrdysQEQV---WevlekvqladlargfsdgintrlgeqGNNLSVGQKQLLALARVLIETPQV 497
Cdd:cd03223 70 PQRP------YLPLGTL-----REQLiypW--------------------------DDVLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 1541475627 498 LILDEATASIDSGTEQAIQQALaavRDH-TTLVVIAHR 534
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLL---KELgITVISVGHR 147
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
339-561 |
2.13e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 79.26 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 339 GAIAFDNVSFAYREDRLVlqditldvpsrgfvALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASL-SHNVLRKGV 417
Cdd:PRK11300 17 GLLAVNNVNLEVREQEIV--------------SLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 418 AMVQQ------DPVVLADTFYA-------NVTLG-------RDYSQE-----QVWevLEKVQLADLArgfsdgintrlGE 472
Cdd:PRK11300 83 VRTFQhvrlfrEMTVIENLLVAqhqqlktGLFSGllktpafRRAESEaldraATW--LERVGLLEHA-----------NR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 473 QGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDH--TTLVVIAHRLSTIVD-ADTILVLHR 549
Cdd:PRK11300 150 QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhnVTVLLIEHDMKLVMGiSDRIYVVNQ 229
|
250
....*....|..
gi 1541475627 550 GQAVERGTHREL 561
Cdd:PRK11300 230 GTPLANGTPEEI 241
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
329-556 |
3.12e-16 |
|
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: 77.96 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 329 YGHDERPLQSGAIAFDNVSfayREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPlASL 408
Cdd:cd03220 13 YKGGSSSLKKLGILGRKGE---VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-SSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 409 shnvLRKGVAMvqqDPvvlADTFYANVTL-GRDY--SQEQVWEVLEKVQladlarGFSDgintrLGEQGN----NLSVGQ 481
Cdd:cd03220 89 ----LGLGGGF---NP---ELTGRENIYLnGRLLglSRKEIDEKIDEII------EFSE-----LGDFIDlpvkTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 482 KQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAA-VRDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERG 556
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRElLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
373-561 |
3.49e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 80.14 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 373 VGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL---RKGVAMVQQDPV-----------VLAD---TFYANv 435
Cdd:PRK15079 53 VGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDPLaslnprmtigeIIAEplrTYHPK- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 436 tLGRDYSQEQVWEVLEKVQLadlargFSDGINTRLGEqgnnLSVGQKQLLALARVLIETPQVLILDEATASIDSGTE--- 512
Cdd:PRK15079 132 -LSRQEVKDRVKAMMLKVGL------LPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaqv 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 513 ----QAIQQALAavrdhTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHREL 561
Cdd:PRK15079 201 vnllQQLQREMG-----LSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
28-318 |
4.40e-16 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 79.22 E-value: 4.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 28 AVLLLWIAAIAEVSGPLLISYFIDNMV---------AKSYLpLRLVAGLGVAYVGLQLAAAglhyAQSLLFNRAAVGVVQ 98
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTnhsgsggeeALRAL-NQAVLILLGVVLIGSIATF----LRSWLFTLAGERVVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 99 QLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAV 178
Cdd:cd18780 76 RLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 179 LIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEA-SRSHYMARMQTLRLDGFLlrPLLS 257
Cdd:cd18780 156 SIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKiNESYLLGKKLARASGGFN--GFMG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 258 LFSALVLcGLLMLFG--LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18780 234 AAAQLAI-VLVLWYGgrLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
342-557 |
4.46e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 79.62 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 342 AFDNVSFAYREDRlvlqdiTLdvpsrgfvALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNV---LRKGVA 418
Cdd:PRK11308 30 ALDGVSFTLERGK------TL--------AVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 419 MVQQDPV-----------VLADTFYANVTLGRDYSQEQVWEVLEKVqladlargfsdGINTrlgEQGNN----LSVGQKQ 483
Cdd:PRK11308 96 IVFQNPYgslnprkkvgqILEEPLLINTSLSAAERREKALAMMAKV-----------GLRP---EHYDRyphmFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 484 LLALARVLIETPQVLILDEATASIDSgteqAIQ-QALAAVRD-----HTTLVVIAHRLStIVD--ADTILVLHRGQAVER 555
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDV----SVQaQVLNLMMDlqqelGLSYVFISHDLS-VVEhiADEVMVMYLGRCVEK 236
|
..
gi 1541475627 556 GT 557
Cdd:PRK11308 237 GT 238
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
43-318 |
4.70e-16 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 79.00 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 43 PLLISYFIDNMVAKSYLPL-----RLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFD 117
Cdd:cd18554 19 PLILKYIVDDVIQGSSLTLdekvyKLFTIIGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 118 IQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFP-AVLIVMIIYQRYSTPIVRRV 196
Cdd:cd18554 99 NNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPfYILAVKYFFGRLRKLTKERS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 197 RAyLADINDGFNEVINGMSVIQQF----RQQARFGERMGE-ASRSHYMARMQTLRldgfllrplLSLFSALVLCGLLMLF 271
Cdd:cd18554 179 QA-LAEVQGFLHERIQGMSVIKSFalekHEQKQFDKRNGHfLTRALKHTRWNAKT---------FSAVNTITDLAPLLVI 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 272 GLSS----SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18554 249 GFAAylviEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
345-561 |
4.80e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.69 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 345 NVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDP 424
Cdd:PRK13652 8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 425 -------VVLADTFYANVTLGRDYS--QEQVWEVLEKVQLADLargfsdgintrLGEQGNNLSVGQKQLLALARVLIETP 495
Cdd:PRK13652 88 ddqifspTVEQDIAFGPINLGLDEEtvAHRVSSALHMLGLEEL-----------RDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 496 QVLILDEATASIDSgteQAIQQALAAVRDHT-----TLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHREL 561
Cdd:PRK13652 157 QVLVLDEPTAGLDP---QGVKELIDFLNDLPetygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
351-552 |
6.42e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 76.76 E-value: 6.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 351 REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADT 430
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 431 FYANVT-LGRDYSQEQVWEVLEKVQLadlaRGFSDGIntrlgeqGNNLSVGQKQLLALARVLIETPQVLILDEATASIDS 509
Cdd:cd03231 90 VLENLRfWHADHSDEQVEEALARVGL----NGFEDRP-------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1541475627 510 GTEQAIQQALAAVRDHTTLVVIAHRLSTIVDADTILVLHRGQA 552
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLGFK 201
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
341-562 |
1.14e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.35 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNV--LRKGVA 418
Cdd:PRK13638 2 LATSDLWFRY-QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLlaLRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 419 MVQQDPVvlADTFYANVTLGRDYSQEQVwevleKVQLADLARGFSDGInTRLGEQG------NNLSVGQKQLLALARVLI 492
Cdd:PRK13638 81 TVFQDPE--QQIFYTDIDSDIAFSLRNL-----GVPEAEITRRVDEAL-TLVDAQHfrhqpiQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 493 ETPQVLILDEATASID-SGTEQ--AIQQALAAVRDHttLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELL 562
Cdd:PRK13638 153 LQARYLLLDEPTAGLDpAGRTQmiAIIRRIVAQGNH--VIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
332-564 |
1.22e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 332 DERPLQSGAIAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHN 411
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRV-PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 412 VLRKGVAMV-QQDPVVLADTFYANVTLGR-----------DYSQEQVWEVLEKVQLADLARGFSDgintrlgeqgnNLSV 479
Cdd:PRK10575 82 AFARKVAYLpQQLPAAEGMTVRELVAIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVD-----------SLSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 480 GQKQLLALARVLIETPQVLILDEATASIDSGTE---QAIQQALAAVRDHTTLVVIaHRLSTIVD-ADTILVLHRGQAVER 555
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQvdvLALVHRLSQERGLTVIAVL-HDINMAARyCDYLVALRGGEMIAQ 229
|
....*....
gi 1541475627 556 GTHRELLEA 564
Cdd:PRK10575 230 GTPAELMRG 238
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
359-556 |
1.58e-15 |
|
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: 75.79 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 359 DITLDVPSrGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL----RKGVA-MVQQDPVVLADTFYA 433
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlppqQRKIGlVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 434 NVTLG-----RDYSQEQVWEVLEKVQLADLARGFSDGintrlgeqgnnLSVGQKQLLALARVLIETPQVLILDEATASID 508
Cdd:cd03297 95 NLAFGlkrkrNREDRISVDELLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 509 SGTEQAIQQALAAVRDHTTLVVI--AHRLSTIVD-ADTILVLHRGQAVERG 556
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIfvTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
341-551 |
1.75e-15 |
|
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: 73.64 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDgrplaslshnvlrkgvamv 420
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 qqdpvvladtfyANVTLGRdYSQeqvwevlekvqladlargfsdgintrlgeqgnnLSVGQKQLLALARVLIETPQVLIL 500
Cdd:cd03221 61 ------------STVKIGY-FEQ---------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 501 DEATASIDSGTEQAIQQALAAVRDhtTLVVIAH-R--LSTIvdADTILVLHRGQ 551
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEYPG--TVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
28-318 |
1.96e-15 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 76.97 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 28 AVLLLWIAAIAEVSGPLLISYFIDNMV-AKSYLPLRLvaglGVAYVGLQLAAAGLHYA-QSLLFNRAAVGVVQQLRTDVM 105
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIViEKSQDKFSR----AIIIMGLLAIASSVAAGiRGGLFTLAMARLNIRIRNLLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 106 DAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMIIY 185
Cdd:cd18784 77 RSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 186 QRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQArfgermGEASRshYMARMQ-TLRLDgfLLRPLL-------S 257
Cdd:cd18784 157 GDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANED------GEANR--YSEKLKdTYKLK--IKEALAyggyvwsN 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 258 LFSALVLCGLLMLFG--LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18784 227 ELTELALTVSTLYYGghLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
345-564 |
2.52e-15 |
|
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: 78.96 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 345 NVSFA-YREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYP----VTQGEIRLDGRPLASLSHNVLRK---- 415
Cdd:COG4172 13 SVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 416 GVAMVQQDPVV-----------LADTFYANVTLGRDYSQEQVWEVLEKVQLADLARgfsdgintRLGEQGNNLSVGQKQL 484
Cdd:COG4172 93 RIAMIFQEPMTslnplhtigkqIAEVLRLHRGLSGAAARARALELLERVGIPDPER--------RLDAYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 485 LALARVLIETPQVLILDEATASIDSgTEQAiqQALAAVRD-----HTTLVVIAHRLStIVD--ADTILVLHRGQAVERGT 557
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDV-TVQA--QILDLLKDlqrelGMALLLITHDLG-VVRrfADRVAVMRQGEIVEQGP 240
|
....*..
gi 1541475627 558 HRELLEA 564
Cdd:COG4172 241 TAELFAA 247
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
351-526 |
2.75e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 74.70 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 351 REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDPVVLADT 430
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 431 FYANVTLGRD---YSQEQVWEVLEKVQLadlaRGFSDGIntrlgeqGNNLSVGQKQLLALARVLIETPQVLILDEATASI 507
Cdd:TIGR01189 90 ALENLHFWAAihgGAQRTIEDALAAVGL----TGFEDLP-------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170
....*....|....*....
gi 1541475627 508 DSgteQAIQQALAAVRDHT 526
Cdd:TIGR01189 159 DK---AGVALLAGLLRAHL 174
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
341-515 |
2.89e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHN---VLRKGV 417
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 418 AMVQQDPVVLAD-TFYANVTL--------GRDYsQEQVWEVLEKVQLADLARGFSDgintrlgeqgnNLSVGQKQLLALA 488
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIpliiagasGDDI-RRRVSAALDKVGLLDKAKNFPI-----------QLSGGEQQRVGIA 149
|
170 180
....*....|....*....|....*..
gi 1541475627 489 RVLIETPQVLILDEATASIDSGTEQAI 515
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGI 176
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
323-562 |
2.99e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.77 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 323 DRPRQAYGHDERPLQSGAIaFDNVSFAyredrLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDG 402
Cdd:PRK10070 16 EHPQRAFKYIEQGLSKEQI-LEKTGLS-----LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 403 RPLASLS----HNVLRKGVAMVQQDPVVLAD-TFYANVTLGRDYS-------QEQVWEVLEKVQLADLARGFSDgintrl 470
Cdd:PRK10070 90 VDIAKISdaelREVRRKKIAMVFQSFALMPHmTVLDNTAFGMELAginaeerREKALDALRQVGLENYAHSYPD------ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 471 geqgnNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAV--RDHTTLVVIAHRLSTIVD-ADTILVL 547
Cdd:PRK10070 164 -----ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRiGDRIAIM 238
|
250
....*....|....*
gi 1541475627 548 HRGQAVERGTHRELL 562
Cdd:PRK10070 239 QNGEVVQVGTPDEIL 253
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
370-563 |
3.10e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 370 VALVGHTGSGKSTLASLLMGYYP---VTQGEIRLDGRPLASlshNVLRKGVAMVQQD----PVVLAD---TFYANVTLGR 439
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDA---KEMRAISAYVQQDdlfiPTLTVRehlMFQAHLRMPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 440 DYSQEQ----VWEVLEKVQLADLArgfsdgiNTRLGEQGN--NLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQ 513
Cdd:TIGR00955 131 RVTKKEkrerVDEVLQALGLRKCA-------NTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 514 AIQQALA--AVRDHTTLVVIAHRLSTIVDA-DTILVLHRGQAVERGTHRELLE 563
Cdd:TIGR00955 204 SVVQVLKglAQKGKTIICTIHQPSSELFELfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
43-318 |
4.79e-15 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 76.09 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 43 PLLISYFIDNMVAKSYLPLRLVagLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVG 122
Cdd:cd18782 22 PLLFQVIIDKVLVQQDLATLYV--IGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 123 QVISRVtNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMIIYQRYSTPIVRRVRAYLAD 202
Cdd:cd18782 100 ELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 203 INDGFNEVINGMSVIQQFRQQARFGERMGEAsRSHYMARMQTLRLDGFLLRPLLSLFSALVlcGLLMLF---GLSSSGTI 279
Cdd:cd18782 179 TQSYLVESLTGIQTVKAQNAELKARWRWQNR-YARSLGEGFKLTVLGTTSGSLSQFLNKLS--SLLVLWvgaYLVLRGEL 255
|
250 260 270
....*....|....*....|....*....|....*....
gi 1541475627 280 EVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18782 256 TLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
341-554 |
4.79e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRldgrplasLSHNVLrkgVAMV 420
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK--------LGETVK---IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDpvvlADTFYANVTLgrdysQEQVWEVLEKVQLAD----LAR-GFS-DGINTRLGeqgnNLSVGQKQLLALARVLIET 494
Cdd:COG0488 384 DQH----QEELDPDKTV-----LDELRDGAPGGTEQEvrgyLGRfLFSgDDAFKPVG----VLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 495 PQVLILDEATASIDSGTEQAIQQALAavrDHT-TLVVIAH-R--LSTIvdADTILVLHRGQAVE 554
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEALD---DFPgTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
320-563 |
7.26e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.41 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 320 ELMDRPRQAYGHDERPLqsgaIAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIR 399
Cdd:PRK11607 3 DAIPRPQAKTRKALTPL----LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 400 LDGRPLASLShNVLRKGVAMVQQDPVVLADTFYANVTLG-------RDYSQEQVWEVLEKVQLADLARgfsdgintrlgE 472
Cdd:PRK11607 78 LDGVDLSHVP-PYQRPINMMFQSYALFPHMTVEQNIAFGlkqdklpKAEIASRVNEMLGLVHMQEFAK-----------R 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 473 QGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAV--RDHTTLVVIAH-RLSTIVDADTILVLHR 549
Cdd:PRK11607 146 KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDIleRVGVTCVMVTHdQEEAMTMAGRIAIMNR 225
|
250
....*....|....
gi 1541475627 550 GQAVERGTHRELLE 563
Cdd:PRK11607 226 GKFVQIGEPEEIYE 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
356-553 |
7.56e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.37 E-value: 7.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVpSRG-FVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS-HNVLRKGVAMV----QQDPVVLAD 429
Cdd:COG1129 267 VVRDVSFSV-RAGeILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVpedrKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 430 TFYANVTLGrdySQEQV--WEVLEKVQLADLARGFSD--GINTRLGEQG-NNLSVGQKQLLALARVLIETPQVLILDEAT 504
Cdd:COG1129 346 SIRENITLA---SLDRLsrGGLLDRRRERALAEEYIKrlRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 505 ASIDSGTEQAIQQALAA-VRDHTTLVVIAHRLSTIVD-ADTILVLHRGQAV 553
Cdd:COG1129 423 RGIDVGAKAEIYRLIRElAAEGKAVIVISSELPELLGlSDRILVMREGRIV 473
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
356-533 |
7.78e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.05 E-value: 7.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHN---VLR-KGVAMVQQDpVVLADTF 431
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQS-FMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 432 YAnvtlgrdysqeqvwevLEKVQLADLARGFSD--------------GINTRLGEQGNNLSVGQKQLLALARVLIETPQV 497
Cdd:PRK10584 104 NA----------------LENVELPALLRGESSrqsrngakalleqlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDV 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1541475627 498 LILDEATASIDSGTEQAIQQALAAV-RDH-TTLVVIAH 533
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLnREHgTTLILVTH 205
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
344-565 |
9.93e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.28 E-value: 9.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYREDRlVLQDITLDVPSRGFVALVGHTGSGKSTL----ASLLMgyyPVTqGEIRLDGRPLASLSHNVLRKGVAM 419
Cdd:PRK11231 6 ENLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLlkcfARLLT---PQS-GTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDPVVLAD-TFYANVTLGR-----------DYSQEQVWEVLEKVQLADLArgfsdgiNTRLGEqgnnLSVGQKQLLAL 487
Cdd:PRK11231 81 LPQHHLTPEGiTVRELVAYGRspwlslwgrlsAEDNARVNQAMEQTRINHLA-------DRRLTD----LSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 488 ARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLEAK 565
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
352-550 |
1.36e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.51 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 352 EDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIrldgrpLASLShnvlrkgVAMVQQDPVVLADTF 431
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------WAERS-------IAYVPQQAWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 432 YANVTLGRDYSQEQVWEVLEKVQL-ADLARgFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSG 510
Cdd:PTZ00243 738 RGNILFFDEEDAARLADAVRVSQLeADLAQ-LGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1541475627 511 TEQAIQQA--LAAVRDHTTlVVIAHRLSTIVDADTILVLHRG 550
Cdd:PTZ00243 817 VGERVVEEcfLGALAGKTR-VLATHQVHVVPRADYVVALGDG 857
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
101-536 |
1.56e-14 |
|
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: 76.71 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 101 RTDVMDAALRQPLSEFDIQPVGQVISRVTN-DTEVIRDLYVTVVATVLRSAALIGAML-VAMFSLDWRMALVAI---TIF 175
Cdd:TIGR00954 167 RVRLTRYLYSKYLSGFTFYKVSNLDSRIQNpDQLLTQDVEKFCDSVVELYSNLTKPILdVILYSFKLLTALGSVgpaGLF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 176 PAVLIVMIIYQRYSTPIVRRV---RAYLADINDGFNEVINGMSVIQQFRQQARfgermgEASRSHYMARmqtlRLDGFLL 252
Cdd:TIGR00954 247 AYLFATGVVLTKLRPPIGKLTveeQALEGEYRYVHSRLIMNSEEIAFYQGNKV------EKETVMSSFY----RLVEHLN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 253 RPLLSLFSALVLCGLLMLFGLSSSGTIEVGVLYAFISYLG----RLNEPLIELTTQQSMLQQAVVAGER----------- 317
Cdd:TIGR00954 317 LIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAflemSEEELMQEFYNNGRLLLKAADALGRlmlagrdmtrl 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 318 ------VFELMD------RPRQAYGHDERPLQSGA--------------------IAFDNVSFAYREDRLVLQDITLDVP 365
Cdd:TIGR00954 397 agftarVDTLLQvlddvkSGNFKRPRVEEIESGREggrnsnlvpgrgiveyqdngIKFENIPLVTPNGDVLIESLSFEVP 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 366 SRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDG---------RPLASLShnVLRkgvamvqqDPVVLADTfyANVT 436
Cdd:TIGR00954 477 SGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAkgklfyvpqRPYMTLG--TLR--------DQIIYPDS--SEDM 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 437 LGRDYSQEQVWEVLEKVQLADLAR---GFSdgintRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQ 513
Cdd:TIGR00954 545 KRRGLSDKDLEQILDNVQLTHILEregGWS-----AVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
490 500
....*....|....*....|...
gi 1541475627 514 AIQQALAAVRdhTTLVVIAHRLS 536
Cdd:TIGR00954 620 YMYRLCREFG--ITLFSVSHRKS 640
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
344-536 |
1.56e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 73.31 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYREDRL---VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNV---LR-KG 416
Cdd:PRK11629 9 DNLCKRYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 VAMVQQDPVVLAD-TFYANVTL-------GRDYSQEQVWEVLEKVqladlargfsdGINTRLGEQGNNLSVGQKQLLALA 488
Cdd:PRK11629 89 LGFIYQFHHLLPDfTALENVAMplligkkKPAEINSRALEMLAAV-----------GLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1541475627 489 RVLIETPQVLILDEATASIDSGTEQAIQQALAA--VRDHTTLVVIAHRLS 536
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
356-561 |
1.67e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.14 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLShnVLRKGVAMVQQDPVVLAD-TFYAN 434
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS--IQQRDICMVFQSYALFPHmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 435 VTLG-------RDYSQEQVWEVLEKVQLAdlarGFSDgintRLGEQgnnLSVGQKQLLALARVLIETPQVLILDEATASI 507
Cdd:PRK11432 99 VGYGlkmlgvpKEERKQRVKEALELVDLA----GFED----RYVDQ---ISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 508 DSGTEQA-------IQQALaavrDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHREL 561
Cdd:PRK11432 168 DANLRRSmrekireLQQQF----NITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
371-564 |
1.95e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.56 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 371 ALVGHTGSGKSTLASLLMGYYP----VTQGEIRLDGRPLASLS----HNVLRKGVAMVQQDPVVLADtfyANVTLGRDYS 442
Cdd:COG4170 37 GLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSprerRKIIGREIAMIFQEPSSCLD---PSAKIGDQLI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 443 Q-------------------EQVWEVLEKVQLAD---LARGF----SDGIntrlgeqgnnlsvGQKQLLALArvLIETPQ 496
Cdd:COG4170 114 EaipswtfkgkwwqrfkwrkKRAIELLHRVGIKDhkdIMNSYphelTEGE-------------CQKVMIAMA--IANQPR 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 497 VLILDEATASIDSGTEQAIQQALAAVR--DHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLEA 564
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLNqlQGTSILLISHDLESISQwADTITVLYCGQTVESGPTEQILKS 249
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
25-272 |
1.98e-14 |
|
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: 73.98 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAevsgplLISYFIDNMVAKSyLPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18584 4 LGLLAALLIIAQAW------LLARIIAGVFLEG-AGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 105 MDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMII 184
Cdd:cd18584 77 LARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 185 YQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLdGFLLRPLLSLFSAL-- 262
Cdd:cd18584 157 IGKAAQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRV-AFLSSAVLEFFATLsi 235
|
250
....*....|....
gi 1541475627 263 ----VLCGLLMLFG 272
Cdd:cd18584 236 alvaVYIGFRLLGG 249
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
338-564 |
2.08e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.19 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 338 SGAIAFDNVSFAYR---------------------EDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQG 396
Cdd:COG1134 2 SSMIEVENVSKSYRlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 397 EIRLDGRpLASLshnvLRKGVAMVQQdpvvLadTFYANVTL-GR--DYSQEQVWEVLEKVQ-LADLA-------RGFSDG 465
Cdd:COG1134 82 RVEVNGR-VSAL----LELGAGFHPE----L--TGRENIYLnGRllGLSRKEIDEKFDEIVeFAELGdfidqpvKTYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 466 INTRLGeqgnnlsvgqkqlLALArVLIEtPQVLILDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTIVD-ADT 543
Cdd:COG1134 151 MRARLA-------------FAVA-TAVD-PDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRlCDR 215
|
250 260
....*....|....*....|.
gi 1541475627 544 ILVLHRGQAVERGTHRELLEA 564
Cdd:COG1134 216 AIWLEKGRLVMDGDPEEVIAA 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
347-554 |
2.18e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.68 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 347 SFAYREDRL---VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDgrplaslshnvlrkgvamvqqd 423
Cdd:COG2401 33 AFGVELRVVeryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 424 pvVLADTFYANVTL----GRDYSQEQVWEVLEKVQLAD---LARGFSdgintrlgeqgnNLSVGQKQLLALARVLIETPQ 496
Cdd:COG2401 91 --VPDNQFGREASLidaiGRKGDFKDAVELLNAVGLSDavlWLRRFK------------ELSTGQKFRFRLALLLAERPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 497 VLILDEATASIDSGTEQAIQQALA-AVRDH-TTLVVIAHRlSTIVDA---DTILVLHRGQAVE 554
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVARNLQkLARRAgITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
333-561 |
2.63e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.12 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 333 ERPLQSGAI-AFDNVSFAYREDR----LVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLD------ 401
Cdd:PRK13631 13 PNPLSDDIIlRVKNLYCVFDEKQenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 402 --GRPLASLSHNV--------LRKGVAMVQQDP-------VVLADTFYANVTLG--RDYSQEQVWEVLEKVQLADlargf 462
Cdd:PRK13631 93 kkNNHELITNPYSkkiknfkeLRRRVSMVFQFPeyqlfkdTIEKDIMFGPVALGvkKSEAKKLAKFYLNKMGLDD----- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 463 sdginTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASID-SGTEQAIQQALAAVRDHTTLVVIAHRLSTIVD- 540
Cdd:PRK13631 168 -----SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpKGEHEMMQLILDAKANNKTVFVITHTMEHVLEv 242
|
250 260
....*....|....*....|.
gi 1541475627 541 ADTILVLHRGQAVERGTHREL 561
Cdd:PRK13631 243 ADEVIVMDKGKILKTGTPYEI 263
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
338-581 |
2.88e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.50 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 338 SGAIAFDNVSFAYRE----DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGE-IRLDGRPLASLSH-- 410
Cdd:PRK13645 4 SKDIILDNVSYTYAKktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtIVGDYAIPANLKKik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 411 --NVLRKGVAMVQQDP-------VVLADTFYANVTLGRDySQEQVWEVLEKVQLADLARGFSDgintrlgEQGNNLSVGQ 481
Cdd:PRK13645 84 evKRLRKEIGLVFQFPeyqlfqeTIEKDIAFGPVNLGEN-KQEAYKKVPELLKLVQLPEDYVK-------RSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 482 KQLLALARVLIETPQVLILDEATASID-SGTEQAIQQALAAVRDHTT-LVVIAHRLSTIVD-ADTILVLHRGQAVERG-- 556
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDpKGEEDFINLFERLNKEYKKrIIMVTHNMDQVLRiADEVIVMHEGKVISIGsp 235
|
250 260 270
....*....|....*....|....*....|....
gi 1541475627 557 ----THRELL-----EAKGRYWQMYQLQLAGEEL 581
Cdd:PRK13645 236 feifSNQELLtkieiDPPKLYQLMYKLKNKGIDL 269
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
43-318 |
2.95e-14 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 73.70 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 43 PLLISYFIDNMVAKSYLPLRLVAGLGVayVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVG 122
Cdd:cd18555 22 PILTQYVIDNVIVPGNLNLLNVLGIGI--LILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 123 QVISRVtNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIfpAVLIVMIIYqrYSTPIVRRVR----A 198
Cdd:cd18555 100 DLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLL--GLLIVLLLL--LTRKKIKKLNqeeiV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 199 YLADINDGFNEVINGMSVI--------------QQFRQQARFGERmgeasRSHYMARMQTLRLDGFLLRPLLSLFsalvL 264
Cdd:cd18555 175 AQTKVQSYLTETLYGIETIkslgsekniykkweNLFKKQLKAFKK-----KERLSNILNSISSSIQFIAPLLILW----I 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 265 CGLLMLfglssSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18555 246 GAYLVI-----NGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
340-563 |
3.33e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.10 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYReDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHnVLRKGVAM 419
Cdd:PRK13536 41 AIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR-LARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQ-DPVVLADTFYAN-VTLGRDY--SQEQVWEVLEkvQLADLARgFSDGINTRLGEqgnnLSVGQKQLLALARVLIETP 495
Cdd:PRK13536 119 VPQfDNLDLEFTVRENlLVFGRYFgmSTREIEAVIP--SLLEFAR-LESKADARVSD----LSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 496 QVLILDEATASIDSGTEQAIQQALAAV--RDHTTLVVI-----AHRLstivdADTILVLHRGQAVERGTHRELLE 563
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLlaRGKTILLTThfmeeAERL-----CDRLCVLEAGRKIAEGRPHALID 261
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
357-571 |
4.23e-14 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 72.11 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 357 LQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLrkgvaMVQQDPVVLA-DTFYANV 435
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 436 TLG-----RDYSQEQVWEVLEK-VQLAdlarGFSDGINTRLGEqgnnLSVGQKQLLALARVLIETPQVLILDEATASIDS 509
Cdd:TIGR01184 76 ALAvdrvlPDLSKSERRAIVEEhIALV----GLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 510 GTEQAIQQALAAV--RDHTTLVVIAHRL-STIVDADTILVLHRGQA----------VERGTHRELLEAKGRYWQM 571
Cdd:TIGR01184 148 LTRGNLQEELMQIweEHRVTVLMVTHDVdEALLLSDRVVMLTNGPAanigqilevpFPRPRDRLEVVEDPSYYDL 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
341-563 |
5.92e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.83 E-value: 5.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNvlRKGVAMV 420
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDPVVLAD-TFYANVTLG-------RDYSQEQVWEVLEKVQLADLARgfsdgintRLGEQgnnLSVGQKQLLALARVLI 492
Cdd:PRK09452 92 FQSYALFPHmTVFENVAFGlrmqktpAAEITPRVMEALRMVQLEEFAQ--------RKPHQ---LSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 493 ETPQVLILDEATASIDSGTEQAIQQALAAVRDHT--TLVVIAH-RLSTIVDADTILVLHRGQAVERGTHRELLE 563
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
347-550 |
6.50e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.59 E-value: 6.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 347 SFAYREDRLV--LQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDG-RPLASLSHNVLRKGVAMVQQD 423
Cdd:cd03267 25 SLFKRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKRRKKFLRRIGVVFGQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 424 PVV----LADTFYANVTLGR-DYSQ--EQVWEVLEKVQLADLargfsdgintrLGEQGNNLSVGQKQLLALARVLIETPQ 496
Cdd:cd03267 105 QLWwdlpVIDSFYLLAAIYDlPPARfkKRLDELSELLDLEEL-----------LDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 497 VLILDEATASIDSGTEQAIQQAL-AAVRDH-TTLVVIAHRLSTIVD-ADTILVLHRG 550
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLkEYNRERgTTVLLTSHYMKDIEAlARRVLVIDKG 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
357-553 |
7.45e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.09 E-value: 7.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 357 LQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYP--VTQGEIRLDGRPL-ASLSHNVLRKGVAMVQQDPVVLAD-TFY 432
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLkASNIRDTERAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 433 ANVTLGRDYSQE-----------QVWEVLEKVQLADL--ARGFSDgintrlgeqgnnLSVGQKQLLALARVLIETPQVLI 499
Cdd:TIGR02633 97 ENIFLGNEITLPggrmaynamylRAKNLLRELQLDADnvTRPVGD------------YGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 500 LDEATASIdsgTEQAIQQALAAVRD----HTTLVVIAHRLSTI-VDADTILVLHRGQAV 553
Cdd:TIGR02633 165 LDEPSSSL---TEKETEILLDIIRDlkahGVACVYISHKLNEVkAVCDTICVIRDGQHV 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
346-564 |
8.98e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.34 E-value: 8.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 346 VSFAyreDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQDpv 425
Cdd:PRK09536 11 VEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 426 vladtfyanVTLGRDYSQEQVWEVLEKVQLADLARGFSDGinTRLGEQGNN--------------LSVGQKQLLALARVL 491
Cdd:PRK09536 86 ---------TSLSFEFDVRQVVEMGRTPHRSRFDTWTETD--RAAVERAMErtgvaqfadrpvtsLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 492 IETPQVLILDEATASIDsgTEQAIqQALAAVR----DHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLEA 564
Cdd:PRK09536 155 AQATPVLLLDEPTASLD--INHQV-RTLELVRrlvdDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTA 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
356-555 |
1.23e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.27 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLShnvLRKGVaMVQQDPVVLADTFYANV 435
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG---AERGV-VFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 436 TLG-------RDYSQEQVWEVLEKVQLAdlargfsdGINTRLGEQgnnLSVGQKQLLALARVLIETPQVLILDEATASID 508
Cdd:PRK11248 92 AFGlqlagveKMQRLEIAHQMLKKVGLE--------GAEKRYIWQ---LSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 509 SGTEQAIQQALAAVRDHT--TLVVIAHRLSTIVDADTILVL---HRGQAVER 555
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETgkQVLLITHDIEEAVFMATELVLlspGPGRVVER 212
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
350-535 |
1.48e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.97 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 350 YREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLA-------SLLMGYYpvTQGEIRLDGRPL--ASLSHNVLRKGVAMV 420
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR--VEGKVTFHGKNLyaPDVDPVEVRRRIGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDPVVLADTFYANVTLGRDYSQEQVwEVLEKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLIL 500
Cdd:PRK14243 97 FQKPNPFPKSIYDNIAYGARINGYKG-DMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1541475627 501 DEATASIDSGTEQAIQQALAAVRDHTTLVVIAHRL 535
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
349-532 |
1.63e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.52 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 349 AYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRP-----LASLSH-----NVLrKGVA 418
Cdd:PRK13539 10 CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDiddpdVAEACHylghrNAM-KPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 419 MVQQDpvvLAdtFYANVTLGRDYSqeqVWEVLEKVQLADLArgfsdgintrlGEQGNNLSVGQKQLLALARVLIETPQVL 498
Cdd:PRK13539 89 TVAEN---LE--FWAAFLGGEELD---IAAALEAVGLAPLA-----------HLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....
gi 1541475627 499 ILDEATASIDSGTEQAIQQALAAVRDHTTLVVIA 532
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
344-563 |
1.68e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 70.26 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYREdRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS-HNVLRKGVAMVQQ 422
Cdd:cd03218 4 ENLSKRYGK-RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 423 DPVVLAD-TFYANV-------TLGRDYSQEQVWEVLEKVQLADLARgfsdgintrlgEQGNNLSVGQKQLLALARVLIET 494
Cdd:cd03218 83 EASIFRKlTVEENIlavleirGLSKKEREEKLEELLEEFHITHLRK-----------SKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 495 PQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIA-HRLSTIVD-ADTILVLHRGQAVERGTHRELLE 563
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
341-563 |
4.03e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 69.35 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNV--LRKGVA 418
Cdd:PRK09493 2 IEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 419 MV-QQDPVVLADTFYANVTLG--------RDYSQEQVWEVLEKVQLADlargfsdgintRLGEQGNNLSVGQKQLLALAR 489
Cdd:PRK09493 81 MVfQQFYLFPHLTALENVMFGplrvrgasKEEAEKQARELLAKVGLAE-----------RAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 490 VLIETPQVLILDEATASIDSGTEQ---AIQQALAavRDHTTLVVIAHRLSTIVDADTILV-LHRGQAVERGTHRELLE 563
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHevlKVMQDLA--EEGMTMVIVTHEIGFAEKVASRLIfIDKGRIAEDGDPQVLIK 225
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
351-508 |
4.11e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 351 REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLAslshnvlrkgvamvQQDPVVLADT 430
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR--------------RQRDEYHQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 431 FY------------------ANVTLGRDYSQEQVWEVLEKVQLAdlarGFSDgINTRlgeqgnNLSVGQKQLLALARVLI 492
Cdd:PRK13538 77 LYlghqpgikteltalenlrFYQRLHGPGDDEALWEALAQVGLA----GFED-VPVR------QLSAGQQRRVALARLWL 145
|
170
....*....|....*.
gi 1541475627 493 ETPQVLILDEATASID 508
Cdd:PRK13538 146 TRAPLWILDEPFTAID 161
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
340-558 |
4.31e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.27 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYREDRlVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLaSLSHNV------- 412
Cdd:PRK11124 2 SIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHF-DFSKTPsdkaire 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 413 LRKGVAMVQQD----P--VVLADTFYANVT---LGRDYSQEQVWEVLEKVQLADLARGFSdgintrlgeqgNNLSVGQKQ 483
Cdd:PRK11124 80 LRRNVGMVFQQynlwPhlTVQQNLIEAPCRvlgLSKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 484 LLALARVLIETPQVLILDEATASIDSG-TEQ--AIQQALAAVrdHTTLVVIAHRlstiVD-----ADTILVLHRGQAVER 555
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEiTAQivSIIRELAET--GITQVIVTHE----VEvarktASRVVYMENGHIVEQ 222
|
...
gi 1541475627 556 GTH 558
Cdd:PRK11124 223 GDA 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
353-561 |
6.87e-13 |
|
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: 68.17 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 353 DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVlRKGVAMVQQDPVVLAD-TF 431
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV-RRRIGIVFQDLSVDDElTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 432 YANVTL-GRDYS------QEQVWEVLEKVQLAD----LARGFSDGINTRlgeqgnnlsvgqkqlLALARVLIETPQVLIL 500
Cdd:cd03265 91 WENLYIhARLYGvpgaerRERIDELLDFVGLLEaadrLVKTYSGGMRRR---------------LEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 501 DEATASIDSGTEQAIQQALAAVRDH--TTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHREL 561
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEfgMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
357-553 |
6.93e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.91 E-value: 6.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 357 LQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLA-SLSHNVLRKGVAMVQQD-PVVLADTFYAN 434
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 435 VTLGRdYSQEQVWeVLEKVQLADLARGFSD-GINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIdsgTEQ 513
Cdd:PRK10982 94 MWLGR-YPTKGMF-VDQDKMYRDTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1541475627 514 AIQQALAAVRD----HTTLVVIAHRLSTIVD-ADTILVLHRGQAV 553
Cdd:PRK10982 169 EVNHLFTIIRKlkerGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
344-562 |
7.14e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.77 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYREdRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS-HNVLRKGVAMVQQ 422
Cdd:PRK10895 7 KNLAKAYKG-RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 423 DPVVLA-----DTFYANVTLGRDYSQEQ----VWEVLEKVQLADLARGFsdgintrlgeqGNNLSVGQKQLLALARVLIE 493
Cdd:PRK10895 86 EASIFRrlsvyDNLMAVLQIRDDLSAEQredrANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 494 TPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVVIA-HRLSTIVDA-DTILVLHRGQAVERGTHRELL 562
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVcERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
67-322 |
7.55e-13 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 69.42 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 67 LGVaYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVI-RDLYVTVVAT 145
Cdd:cd18604 46 LGI-YALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIdSELADSLSSL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 146 VLRSAALIGAMLVAMFSLdWRMALVAITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQAR 225
Cdd:cd18604 125 LESTLSLLVILIAIVVVS-PAFLLPAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEER 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 226 FGERMGE-------ASRSHYMA-RMQTLRLDgfllrpLLSLFSALVLCGLLMLFGLSSSGTIevgvlyAF-ISYLGRLNE 296
Cdd:cd18604 204 FIEEMLRridrysrAFRYLWNLnRWLSVRID------LLGALFSFATAALLVYGPGIDAGLA------GFsLSFALGFSS 271
|
250 260
....*....|....*....|....*.
gi 1541475627 297 PLIELTTQQSMLQQAVVAGERVFELM 322
Cdd:cd18604 272 AILWLVRSYNELELDMNSVERIQEYL 297
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
341-585 |
1.56e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYreDRLVLQdITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNvlRKGVAMV 420
Cdd:PRK10771 2 LKLTDITWLY--HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDPVVLAD-TFYANVTLGRD-------YSQEQVWEVLEKVQLADLArgfsdginTRLGEQgnnLSVGQKQLLALARVLI 492
Cdd:PRK10771 77 FQENNLFSHlTVAQNIGLGLNpglklnaAQREKLHAIARQMGIEDLL--------ARLPGQ---LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 493 ETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLStivDADTIlvlhrgqavergTHRELLEAKGR-YW 569
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQerQLTLLMVSHSLE---DAARI------------APRSLVVADGRiAW 210
|
250
....*....|....*..
gi 1541475627 570 Q-MYQLQLAGEELAASV 585
Cdd:PRK10771 211 DgPTDELLSGKASASAL 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
325-551 |
1.95e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 325 PRQAYGHDERPLQ----SGAiAFDNVSFAYREDRLVlqditldvpsrGFVALVGhtgSGKSTLASLLMGYYPVTQGEIRL 400
Cdd:PRK10762 247 PRLDKAPGEVRLKvdnlSGP-GVNDVSFTLRKGEIL-----------GVSGLMG---AGRTELMKVLYGALPRTSGYVTL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 401 DGRPLASLS-HNVLRKGVAMVQQDP----VVLADTFYANVTLG--RDYSQE--QVWEVLEKVQLADLARGFSdgINTRLG 471
Cdd:PRK10762 312 DGHEVVTRSpQDGLANGIVYISEDRkrdgLVLGMSVKENMSLTalRYFSRAggSLKHADEQQAVSDFIRLFN--IKTPSM 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 472 EQG-NNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRdhttlvviAHRLSTIV----------D 540
Cdd:PRK10762 390 EQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFK--------AEGLSIILvssempevlgM 461
|
250
....*....|.
gi 1541475627 541 ADTILVLHRGQ 551
Cdd:PRK10762 462 SDRILVMHEGR 472
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
341-556 |
2.05e-12 |
|
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: 66.62 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDR---LVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRK-G 416
Cdd:cd03266 2 ITADALTKRFRDVKktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 VamvqqdpVVLADTFYANVTlgrdysqeqVWEVLE-------------KVQLADLARGFsdGINTRLGEQGNNLSVGQKQ 483
Cdd:cd03266 82 F-------VSDSTGLYDRLT---------ARENLEyfaglyglkgdelTARLEELADRL--GMEELLDRRVGGFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 484 LLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVERG 556
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
25-320 |
2.14e-12 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 67.89 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 25 LSVAVLLLWIAAIAEVSGPLLISYFIDNMVAKS-------YLPLRLVAGLGVAYVGLQLAAAGLhYAQSLLFNRAAVGVv 97
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLSqgfyigiYAGLGVLQAIFLFLFGLLLAYLGI-RASKRLHNKALKRV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 98 qqlrtdvmdaaLRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMF-SLDWrMALVAITIFP 176
Cdd:cd18606 79 -----------LRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIiYLPW-FAIALPPLLV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 177 AVLIVMIIYQRYSTPIVR-----RVRAYLAdindgFNEVINGMSVIQQFRQQARFGERMGEA----SRSHYM----ARMQ 243
Cdd:cd18606 147 LYYFIANYYRASSRELKRlesilRSFVYAN-----FSESLSGLSTIRAYGAQDRFIKKNEKLidnmNRAYFLtianQRWL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 244 TLRLDgfLLRPLLSLFSAlvLCGLLMLFGLSSSgtiEVGVLyafISYLGRLNEPLIELTTQQSMLQQAVVAGERVFE 320
Cdd:cd18606 222 AIRLD--LLGSLLVLIVA--LLCVTRRFSISPS---STGLV---LSYVLQITQVLSWLVRQFAEVENNMNSVERLLH 288
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
343-504 |
2.59e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.32 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 343 FDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRplaslshnvLRkgVAMVQQ 422
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 423 DPVvladtFYANVTLgRDY---SQEQVWEVLEKVQLADLARGFSDGINTRLGE---------------------QG---- 474
Cdd:COG0488 69 EPP-----LDDDLTV-LDTvldGDAELRALEAELEELEAKLAEPDEDLERLAElqeefealggweaearaeeilSGlgfp 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 1541475627 475 --------NNLSVGQKQLLALARVLIETPQVLILDEAT 504
Cdd:COG0488 143 eedldrpvSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
344-551 |
2.87e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYREDRLVlqditldvpsrGFVALVGhtgSGKSTLASLLMGYYP-VTQGEIRLDGRPLA-SLSHNVLRKGVAMVQ 421
Cdd:PRK13549 279 DDVSFSLRRGEIL-----------GIAGLVG---AGRTELVQCLFGAYPgRWEGEIFIDGKPVKiRNPQQAIAQGIAMVP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 422 QDP----VVLADTFYANVTLGrDYSQEQVWEVLEKVQLADLARGFSD--GINTRLGEQG-NNLSVGQKQLLALARVLIET 494
Cdd:PRK13549 345 EDRkrdgIVPVMGVGKNITLA-ALDRFTGGSRIDDAAELKTILESIQrlKVKTASPELAiARLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 495 PQVLILDEATASIDSGTEQAIQQALAA-VRDHTTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVLGlSDRVLVMHEGK 482
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
341-561 |
3.65e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.85 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRLVLQDITLDVpSRG-FVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAM 419
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTI-KRGeLLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDpVVLADTFYANVtlGRDYSQEQVWEVLEKVQLADLARgFSDGINTRLgeqgnNLSVGQKQLLALARVLIETPQVLI 499
Cdd:PRK10522 402 VFTD-FHLFDQLLGPE--GKPANPALVEKWLERLKMAHKLE-LEDGRISNL-----KLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 500 LDEATASIDSGTEQAI-QQALAAVRDH-TTLVVIAHRLSTIVDADTILVLHRGQAVE-RGTHREL 561
Cdd:PRK10522 473 LDEWAADQDPHFRREFyQVLLPLLQEMgKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDA 537
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
356-577 |
3.70e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.96 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPvTQGEIRLDGRPLASLSHNVL---RKGVAMVQQDP-------- 424
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsslnprl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 425 ---VVLADTFYAN-VTLGRDYSQEQVWEVLEKVQLADLARGfsdgintrlgEQGNNLSVGQKQLLALARVLIETPQVLIL 500
Cdd:PRK15134 380 nvlQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLDPETRH----------RYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 501 DEATASIDSGTEQAIQQALAAVRDHTTL--VVIAHRLStIVDA--DTILVLHRGQAVERGTHRELLEAKGRYWQMYQLQL 576
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLH-VVRAlcHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLAL 528
|
.
gi 1541475627 577 A 577
Cdd:PRK15134 529 S 529
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
370-562 |
5.17e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 370 VALVGHTGSGKSTLASLLMGYYPvTQGEIRLDGRPLASLSHNVL--RKGVAMVQQDPVVLADTF-------YANVTLgrD 440
Cdd:PRK03695 25 LHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELarHRAYLSQQQTPPFAMPVFqyltlhqPDKTRT--E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 441 YSQEQVWEVLEKVQLADLargfsdgintrLGEQGNNLSVGQKQLLALARVLIET-------PQVLILDEATASIDSGTEQ 513
Cdd:PRK03695 102 AVASALNEVAEALGLDDK-----------LGRSVNQLSGGEWQRVRLAAVVLQVwpdinpaGQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 514 AIQQALAAV-RDHTTLVVIAHRLS-TIVDADTILVLHRGQAVERGTHRELL 562
Cdd:PRK03695 171 ALDRLLSELcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
356-562 |
5.22e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 66.31 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPSRGFVALVGHTGSGKST-LASLLMGYYP----VTQGEIRLDG-RPLASLSHNV--LRKGVAMVQQDPVVL 427
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTlLRCINLLEQPeagtIRVGDITIDTaRSLSQQKGLIrqLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 428 AD-TFYANVTLG--------RDYSQEQVWEVLEKVQLAdlarGFSDGINTRLgeqgnnlSVGQKQLLALARVLIETPQVL 498
Cdd:PRK11264 98 PHrTVLENIIEGpvivkgepKEEATARARELLAKVGLA----GKETSYPRRL-------SGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 499 ILDEATASIDSgteQAIQQALAAVR----DHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELL 562
Cdd:PRK11264 167 LFDEPTSALDP---ELVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
371-561 |
5.56e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 371 ALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRK-GVAMVQQDPVVLAD-TFYANVTLGRDYSQEQvwe 448
Cdd:PRK15439 41 ALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLFPNlSVKENILFGLPKRQAS--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 449 vLEKVQ--LADLargfsdGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSG-TEQAIQQALAAVRDH 525
Cdd:PRK15439 118 -MQKMKqlLAAL------GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAeTERLFSRIRELLAQG 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 1541475627 526 TTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHREL 561
Cdd:PRK15439 191 VGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
332-553 |
7.95e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.74 E-value: 7.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 332 DERPLQSGAIAF--DNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS 409
Cdd:COG3845 247 EKAPAEPGEVVLevENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 410 -HNVLRKGVAMVQQDP----VVLADTFYANVTLGRdYSQEQV--WEVLEKVQLADLARG----FS---DGINTRLGeqgn 475
Cdd:COG3845 327 pRERRRLGVAYIPEDRlgrgLVPDMSVAENLILGR-YRRPPFsrGGFLDRKAIRAFAEElieeFDvrtPGPDTPAR---- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 476 NLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTIVD-ADTILVLHRGQAV 553
Cdd:COG3845 402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
371-557 |
7.98e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.50 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 371 ALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASlSHNVLRKGVAMVQQDPVVLADTFYANVTLGRDYSQEQVWevl 450
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW--- 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 451 EKVQLADLARGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVV 530
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIM 1115
|
170 180
....*....|....*....|....*...
gi 1541475627 531 IAHRLSTI-VDADTILVLHRGQAVERGT 557
Cdd:TIGR01257 1116 STHHMDEAdLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
356-553 |
9.95e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.83 E-value: 9.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL----RKGVAMVQQDPVVLAD-T 430
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 431 FYANVT-------LGRDYSQEQVWEVLEKVQLADlargfsdgintRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEA 503
Cdd:PRK10535 103 AAQNVEvpavyagLERKQRLLRAQELLQRLGLED-----------RVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 504 TASIDSGTEQAIQQALAAVRD--HTTLVViAHRLSTIVDADTILVLHRGQAV 553
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQLRDrgHTVIIV-THDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
26-290 |
1.99e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 65.18 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 26 SVAVLLLWIAAIAEV---SGPLLISYFIDNMVAKSYLPLRLVagLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRT 102
Cdd:cd18567 2 RALLQILLLSLALELfalASPLYLQLVIDEVIVSGDRDLLTV--LAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 103 DVMDAALRQPLSEFDIQPVGQVISRVtNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVM 182
Cdd:cd18567 80 NLFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 183 IIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDgfllrPLLSLFSAL 262
Cdd:cd18567 159 LALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQ-----ILFSAANGL 233
|
250 260 270
....*....|....*....|....*....|...
gi 1541475627 263 V--LCGLLMLF---GLSSSGTIEVGVLYAFISY 290
Cdd:cd18567 234 LfgLENILVIYlgaLLVLDGEFTVGMLFAFLAY 266
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
350-563 |
2.47e-11 |
|
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: 66.36 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 350 YREDRLVLQ---DITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEI--------------RLDGRPLASLSHNV 412
Cdd:TIGR03269 290 ISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpGPDGRGRAKRYIGI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 413 LRKGVAMVQQDPVVLADTFYANVTLGRDYSQEQVWEVLEKVqladlarGFSD----GINTRLGEQgnnLSVGQKQLLALA 488
Cdd:TIGR03269 370 LHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMV-------GFDEekaeEILDKYPDE---LSEGERHRVALA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 489 RVLIETPQVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLE 563
Cdd:TIGR03269 440 QVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
372-561 |
2.88e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.13 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 372 LVGHTGSGKSTLASLLMGYYP---VTQGEIRLDGRPLASLSHNVLRK----GVAMVQQDPVV-------LADTFYANVTL 437
Cdd:PRK09473 47 IVGESGSGKSQTAFALMGLLAangRIGGSATFNGREILNLPEKELNKlraeQISMIFQDPMTslnpymrVGEQLMEVLML 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 438 GRDYSQEQVWEvlEKVQLADL-----ARgfsdginTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTE 512
Cdd:PRK09473 127 HKGMSKAEAFE--ESVRMLDAvkmpeAR-------KRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQ 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 513 QAIQQALAAVRD--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHREL 561
Cdd:PRK09473 198 AQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
341-564 |
3.05e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRL---VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKG- 416
Cdd:PRK10261 13 LAVENLNIAFMQEQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 -------------VAMVQQDPVV-----------LADTFYANVTLGRDYSQEQVWEVLEKVQLADlargfSDGINTRLGE 472
Cdd:PRK10261 93 qsaaqmrhvrgadMAMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEAKRMLDQVRIPE-----AQTILSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 473 QgnnLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDHTTLVV--IAHRLSTIVD-ADTILVLHR 549
Cdd:PRK10261 168 Q---LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVAEiADRVLVMYQ 244
|
250
....*....|....*
gi 1541475627 550 GQAVERGTHRELLEA 564
Cdd:PRK10261 245 GEAVETGSVEQIFHA 259
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
30-318 |
3.34e-11 |
|
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: 64.50 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 30 LLLWIAAIAEV------SGPLLISYFIDNMVAKSYLPLRLVAGLGVAYVGL-QLAaagLHYAQSLLFNRAAVGVVQQLRT 102
Cdd:cd18568 3 LLAEILLASLLlqllglALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIfQIL---LSAVRQYLLDYFANRIDLSLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 103 DVMDAALRQPLSEFDIQPVGQVISRVtNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVM 182
Cdd:cd18568 80 DFYKHLLSLPLSFFASRKVGDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 183 IiyqrYSTPIVRR----VRAYLADINDGFNEVINGMSVI------QQFRQQarfgermGEAsrshYMARMQTLRLDGFLL 252
Cdd:cd18568 159 L----LSSPKLKRnsreIFQANAEQQSFLVEALTGIATIkalaaeRPIRWR-------WEN----KFAKALNTRFRGQKL 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 253 RPLLSLFSALV--LCGLLMLFGLSS---SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18568 224 SIVLQLISSLInhLGTIAVLWYGAYlviSGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
357-554 |
3.38e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.58 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 357 LQDITLDVpSRGFV-ALVGHTGSGKSTLASLLMGYYP--VTQGEIRLDGRPLA----SLSHnvlRKGVAMVQQDpvvLA- 428
Cdd:NF040905 17 LDDVNLSV-REGEIhALCGENGAGKSTLMKVLSGVYPhgSYEGEILFDGEVCRfkdiRDSE---ALGIVIIHQE---LAl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 429 ---DTFYANVTLGRDYSQEQV--W--------EVLEKVqladlarGFSDGINTRLGeqgnNLSVGQKQLLALARVLIETP 495
Cdd:NF040905 90 ipyLSIAENIFLGNERAKRGVidWnetnrrarELLAKV-------GLDESPDTLVT----DIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 496 QVLILDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVE 554
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
344-551 |
3.55e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.62 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYREDRLVlqditldvpsrGFVALVGhtgSGKSTLASLLMGYYP-VTQGEIRLDGRPLASLS-HNVLRKGVAMVQ 421
Cdd:TIGR02633 277 DDVSFSLRRGEIL-----------GVAGLVG---AGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAGIAMVP 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 422 QDP----VVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLARGFSdgintRLGEQGNN-------LSVGQKQLLALARV 490
Cdd:TIGR02633 343 EDRkrhgIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQ-----RLKVKTASpflpigrLSGGNQQKAVLAKM 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 491 LIETPQVLILDEATASIDSGTEQAIQQALAA-VRDHTTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGK 480
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
370-564 |
5.06e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.38 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 370 VALVGHTGSGKSTLASLLMGY--YP--VTQGEIRLDGRPLASLSHNVLRK----GVAMVQQDPVVLADTFYanvTLG--- 438
Cdd:PRK11022 36 VGIVGESGSGKSVSSLAIMGLidYPgrVMAEKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPMTSLNPCY---TVGfqi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 439 -----------RDYSQEQVWEVLEKVQLADLArgfsdginTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASI 507
Cdd:PRK11022 113 meaikvhqggnKKTRRQRAIDLLNQVGIPDPA--------SRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTAL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 508 DSGTEQAIQQALAAV--RDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLEA 564
Cdd:PRK11022 185 DVTIQAQIIELLLELqqKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIFRA 244
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
74-318 |
5.16e-11 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 63.64 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 74 LQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALI 153
Cdd:cd18589 45 LTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 154 GAMLVAMFSLDWRMALVAITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQArfgermGEA 233
Cdd:cd18589 125 LFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEE------GEA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 234 SRshYMARMQ-TLRLD-----GFLLRPLLSLFSALVL-CGLLMLFG-LSSSGTIEVGVLYAFISYLGRLNEPLIELTTQQ 305
Cdd:cd18589 199 QR--YRQRLQkTYRLNkkeaaAYAVSMWTSSFSGLALkVGILYYGGqLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYY 276
|
250
....*....|...
gi 1541475627 306 SMLQQAVVAGERV 318
Cdd:cd18589 277 PSVMKAVGSSEKI 289
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
337-561 |
5.44e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 337 QSGAIAFDNVSFAYREDRlVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS-HNVLRK 415
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAStTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 416 GVAMVQQD-PVVLADTFYANVTLGR--------DYSqEQVWEVLEkvQLADLARGFSDgiNTRLGEqgnnLSVGQKQLLA 486
Cdd:PRK11288 80 GVAIIYQElHLVPEMTVAENLYLGQlphkggivNRR-LLNYEARE--QLEHLGVDIDP--DTPLKY----LSIGQRQMVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 487 LARVLIETPQVLILDEATASIDSgteQAIQQALAAVR----DHTTLVVIAHRLSTIVD-ADTILVLHRGQAVErgTHREL 561
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSLSA---REIEQLFRVIRelraEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TFDDM 225
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
352-569 |
6.07e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.89 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 352 EDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGY--YPVTQGEIRLDGRPLASLS-HNVLRKGVAMVQQDPVVL- 427
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVEIp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 428 --ADTFYANVTLG--RDYSQEQVWE-------VLEKVQLADLargfSDGINTRLGEQGnnLSVGQKQLLALARVLIETPQ 496
Cdd:PRK09580 92 gvSNQFFLQTALNavRSYRGQEPLDrfdfqdlMEEKIALLKM----PEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 497 VLILDEATASIDSGTEQAIQQALAAVRD-HTTLVVIAH--RLSTIVDADTILVLHRGQAVERGTHR--ELLEAKGRYW 569
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTlvKQLEEQGYGW 243
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
345-561 |
7.56e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.90 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 345 NVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNvlRKGVAMVQQDP 424
Cdd:PRK11000 8 NVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 425 VVLAD-TFYANVTLG----------RDYSQEQVWEVLekvQLADLargfsdgintrLGEQGNNLSVGQKQLLALARVLIE 493
Cdd:PRK11000 85 ALYPHlSVAENMSFGlklagakkeeINQRVNQVAEVL---QLAHL-----------LDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 494 TPQVLILDEATASIDSGTEqaIQQALAAVRDH----TTLVVIAH-RLSTIVDADTILVLHRGQAVERGTHREL 561
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALR--VQMRIEISRLHkrlgRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
356-533 |
1.07e-10 |
|
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: 62.07 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRL--DGRP--LASLS-HNVL---RKGVAMVQQ----D 423
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWvdLAQASpREILalrRRTIGYVSQflrvI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 424 PVVLADTFYANVTL----GRDYSQEQVWEVLEKVQ----LADLArgfsdgintrlgeqGNNLSVGQKQLLALARVLIETP 495
Cdd:COG4778 106 PRVSALDVVAEPLLergvDREEARARARELLARLNlperLWDLP--------------PATFSGGEQQRVNIARGFIADP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1541475627 496 QVLILDEATASIDSGTEQA----IQQALAAvrdHTTLVVIAH 533
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVvvelIEEAKAR---GTAIIGIFH 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-579 |
1.18e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 62.82 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 353 DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPlasLSHNVLRK--------GVamvqqdp 424
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---LDPEDRRRigylpeerGL------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 425 vvladtfYANVT-------------LGRDYSQEQVWEVLEKVQLADLArgfsdgiNTRLGEqgnnLSVGQKQLLALARVL 491
Cdd:COG4152 83 -------YPKMKvgeqlvylarlkgLSKAEAKRRADEWLERLGLGDRA-------NKKVEE----LSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 492 IETPQVLILDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTiVD--ADTILVLHRGQAVERGTHRELLEAKGRy 568
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMEL-VEelCDRIVIINKGRKVLSGSVDEIRRQFGR- 222
|
250
....*....|.
gi 1541475627 569 wQMYQLQLAGE 579
Cdd:COG4152 223 -NTLRLEADGD 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
335-565 |
1.75e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.52 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 335 PLQSGAIAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVlR 414
Cdd:PRK13537 2 PMSVAPIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 415 KGVAMVQQ----DPVVladTFYANVTLGRDYSQEQVWEVLEKVQ-LADLARgFSDGINTRLGEqgnnLSVGQKQLLALAR 489
Cdd:PRK13537 80 QRVGVVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPpLLEFAK-LENKADAKVGE----LSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 490 VLIETPQVLILDEATASIDSGTEQAIQQALAAV--RDHTTLVVI-----AHRLstivdADTILVLHRGQAVERGTHRELL 562
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlaRGKTILLTThfmeeAERL-----CDRLCVIEEGRKIAEGAPHALI 226
|
...
gi 1541475627 563 EAK 565
Cdd:PRK13537 227 ESE 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
341-563 |
2.09e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 63.28 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGY--YPVTQGEI----------------RLDG 402
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 403 RPLA------------------SLSHNVLRKGVAMVQQ------DPVVLADTFYANVTLGR--DYSQEQVWEVLEKVQLA 456
Cdd:TIGR03269 80 EPCPvcggtlepeevdfwnlsdKLRRRIRKRIAIMLQRtfalygDDTVLDNVLEALEEIGYegKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 457 DlargfsdgintRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQAL-AAVRDH-TTLVVIAHR 534
Cdd:TIGR03269 160 H-----------RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASgISMVLTSHW 228
|
250 260 270
....*....|....*....|....*....|
gi 1541475627 535 LSTIVD-ADTILVLHRGQAVERGTHRELLE 563
Cdd:TIGR03269 229 PEVIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
341-562 |
2.26e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.05 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREDRlVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASL-SHNVLRKGVAM 419
Cdd:PRK11614 6 LSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDPVVLAD-TFYANVTLGRDY-SQEQVWEVLEKVQladlarGFSDGINTRLGEQGNNLSVGQKQLLALARVLIETPQV 497
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGGFFaERDQFQERIKWVY------ELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1541475627 498 LILDEATASIDSGTEQAIQQALAAVRDH--TTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELL 562
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQgmTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
344-564 |
2.36e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.54 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYREdRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKGVAMVQQD 423
Cdd:PRK10253 11 EQLTLGYGK-YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 424 PVVLAD-TFYANVTLGRdYSQEQVWEVLEKVQLADLARGF-SDGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILD 501
Cdd:PRK10253 90 ATTPGDiTVQELVARGR-YPHQPLFTRWRKEDEEAVTKAMqATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 502 EATASIDSGTEQAIQQALAAVRDHT--TLVVIAHRLSTIVDADTILV-LHRGQAVERGTHRELLEA 564
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRYASHLIaLREGKIVAQGAPKEIVTA 234
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
27-318 |
5.63e-10 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 60.58 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 27 VAVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVAGLGVAYVGLQLAAA-GLHYAQSLLFNraaVGVvqQLRTDVM 105
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSlLLHQYFFLSFR---LGM--RVRSALS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 106 DA----ALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVlrSAALIgaMLVAMFSLDWRM---ALVAItifpAV 178
Cdd:cd18579 76 SLiyrkALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLW--SAPLQ--IIVALYLLYRLLgwaALAGL----GV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 179 LIVMIIYQRYSTPIVRRVRAYLADINDG----FNEVINGMSVIQQFRQQARFGERMGEAsRS---HYMARMQTLR-LDGF 250
Cdd:cd18579 148 LLLLIPLQAFLAKLISKLRKKLMKATDErvklTNEILSGIKVIKLYAWEKPFLKRIEEL-RKkelKALRKFGYLRaLNSF 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 251 LLR--PLLSLFSALVLCGLLMlfglsssGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18579 227 LFFstPVLVSLATFATYVLLG-------NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
341-550 |
6.19e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 58.79 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSF---AYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLL-----MGyypVTQGEIRLDGRPLASlshnV 412
Cdd:cd03232 4 LTWKNLNYtvpVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAG---VITGEILINGRPLDK----N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 413 LRKGVAMVQQdpvvlADTFYANVTlgrdysqeqvweVLEKVQLADLARGfsdgintrlgeqgnnLSVGQKQLLALARVLI 492
Cdd:cd03232 77 FQRSTGYVEQ-----QDVHSPNLT------------VREALRFSALLRG---------------LSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1541475627 493 ETPQVLILDEATASIDSGTEQAIQQALAAVRDH--TTLVVIAHRLSTIVDA-DTILVLHRG 550
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSgqAILCTIHQPSASIFEKfDRLLLLKRG 185
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
345-561 |
1.06e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.39 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 345 NVSFAyREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL---RKGVAMVQ 421
Cdd:PRK11831 12 GVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 422 QDPVVLAD-TFYANVTLG-RDYSQ-------EQVWEVLEKVQLadlaRGFSDGINtrlgeqgNNLSVGQKQLLALARVLI 492
Cdd:PRK11831 91 QSGALFTDmNVFDNVAYPlREHTQlpapllhSTVMMKLEAVGL----RGAAKLMP-------SELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 493 ETPQVLILDEATASIDSGTeQAIQQALAAVRDHT---TLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHREL 561
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPIT-MGVLVKLISELNSAlgvTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
65-322 |
2.03e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 59.08 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 65 AGLGVAYVGLQLAAAGLHYAQSLlfnRAAVGVVQQLrtdvMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVA 144
Cdd:cd18605 49 GFLAGLNSLFTLLRAFLFAYGGL---RAARRLHNKL----LSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 145 TVLRSAA-LIGAMLVAMFSLDWrmalvaitIFPAVLIVMIIY---QRYSTPIVRRVRAyLADINDG-----FNEVINGMS 215
Cdd:cd18605 122 ILLAQLFgLLGYLVVICYQLPW--------LLLLLLPLAFIYyriQRYYRATSRELKR-LNSVNLSplythFSETLKGLV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 216 VIQQFRQQARFG----ERMGEASRSHY--MARMQ--TLRLdgfLLRPLLSLFSALVLCGLLMLFGLS-SSGTIEVGVLYA 286
Cdd:cd18605 193 TIRAFRKQERFLkeylEKLENNQRAQLasQAASQwlSIRL---QLLGVLIVTFVALTAVVQHFFGLSiDAGLIGLALSYA 269
|
250 260 270
....*....|....*....|....*....|....*...
gi 1541475627 287 --FISYLGRLNEPLIEltTQQSMlqqavVAGERVFELM 322
Cdd:cd18605 270 lpITGLLSGLLNSFTE--TEKEM-----VSVERVRQYF 300
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
371-551 |
2.05e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 371 ALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGR------PLASLShnvlrKGVAMVQQDPVVLAD-TFYANVTLGRDYSQ 443
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevtfngPKSSQE-----AGIGIIHQELNLIPQlTIAENIFLGREFVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 444 EQ---VWEVLEKVQLADLAR-GFSDGINTRLGEqgnnLSVGQKQLLALARVLIETPQVLILDEATasiDSGTEQAIQQAL 519
Cdd:PRK10762 109 RFgriDWKKMYAEADKLLARlNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPT---DALTDTETESLF 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 1541475627 520 AAVRD----HTTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:PRK10762 182 RVIRElksqGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
329-565 |
2.65e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 329 YGHDERPLQSGAIAFDNVSfayreDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASL 408
Cdd:PRK11288 246 YGYRPRPLGEVRLRLDGLK-----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIR 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 409 S-HNVLRKGVAMVQQD-------PVV-LADTFyaNVTLGRDYSQ-----EQVWEvlekvqlADLARGF--SDGINTRLGE 472
Cdd:PRK11288 321 SpRDAIRAGIMLCPEDrkaegiiPVHsVADNI--NISARRHHLRagcliNNRWE-------AENADRFirSLNIKTPSRE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 473 QG-NNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQ---ALAAvrDHTTLVVIAHRLSTIVD-ADTILVL 547
Cdd:PRK11288 392 QLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNviyELAA--QGVAVLFVSSDLPEVLGvADRIVVM 469
|
250
....*....|....*...
gi 1541475627 548 HRGQAVERGTHRELLEAK 565
Cdd:PRK11288 470 REGRIAGELAREQATERQ 487
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
356-562 |
2.74e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.06 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPSRGFVALVGHTGSGKSTLASLL-------MGYYPVTQGEIRL----DGRPLASLSHNV--LRKGVAMVQQ 422
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGQTINLvrdkDGQLKVADKNQLrlLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 423 D------PVVLADTFYANVT---LGRDYSQEQVWEVLEKVQLADLARGfsdgintrlgEQGNNLSVGQKQLLALARVLIE 493
Cdd:PRK10619 100 HfnlwshMTVLENVMEAPIQvlgLSKQEARERAVKYLAKVGIDERAQG----------KYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 494 TPQVLILDEATASIDS---GTEQAIQQALAavRDHTTLVVIAHRLSTIVDADT-ILVLHRGQAVERGTHRELL 562
Cdd:PRK10619 170 EPEVLLFDEPTSALDPelvGEVLRIMQQLA--EEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLF 240
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
341-537 |
2.79e-09 |
|
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: 59.95 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDgrplaslshnvlrkgvamv 420
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG------------------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 qqDPVVLAdtfYanVTLGRDY--SQEQVWEV----LEKVQLADL---ARGFSDGINTRLGEQGN---NLSVGQKQLLALA 488
Cdd:TIGR03719 383 --ETVKLA---Y--VDQSRDAldPNKTVWEEisggLDIIKLGKReipSRAYVGRFNFKGSDQQKkvgQLSGGERNRVHLA 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 489 RVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDhtTLVVIAH------RLST 537
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG--CAVVISHdrwfldRIAT 508
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
372-564 |
3.42e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.66 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 372 LVGHTGSGKSTLASLLMGY----YPVTQGEIRLDGRPLASLS----HNVLRKGVAMVQQDPVVLADtfyANVTLGRDYSQ 443
Cdd:PRK15093 38 LVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSprerRKLVGHNVSMIFQEPQSCLD---PSERVGRQLMQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 444 E--------QVW-----------EVLEKVQLAD---LARGFSdgintrlgeqgNNLSVGQKQLLALARVLIETPQVLILD 501
Cdd:PRK15093 115 NipgwtykgRWWqrfgwrkrraiELLHRVGIKDhkdAMRSFP-----------YELTEGECQKVMIAIALANQPRLLIAD 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 502 EATASIDSGTEQAIQQALAAV--RDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLEA 564
Cdd:PRK15093 184 EPTNAMEPTTQAQIFRLLTRLnqNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVTT 249
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
352-550 |
4.62e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 352 EDRLVLQDITldvpsrGFV------ALVGHTGSGKSTLASLL-----MGYypVTQGEIRLDGRPLASlshnVLRKGVAMV 420
Cdd:TIGR00956 774 EKRVILNNVD------GWVkpgtltALMGASGAGKTTLLNVLaervtTGV--ITGGDRLVNGRPLDS----SFQRSIGYV 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQDPVVLADT-------FYANVTLGRDYSQEQ----VWEVLEKVQLADLArgfsDGIntrLGEQGNNLSVGQKQLLALAR 489
Cdd:TIGR00956 842 QQQDLHLPTStvreslrFSAYLRQPKSVSKSEkmeyVEEVIKLLEMESYA----DAV---VGVPGEGLNVEQRKRLTIGV 914
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 490 VLIETPQVLI-LDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAHRLSTIVDA--DTILVLHRG 550
Cdd:TIGR00956 915 ELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHgQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
63-318 |
4.88e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 57.98 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 63 LVAGLGVAYVGLQLaaagLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVtNDTEVIRDLYVTV 142
Cdd:cd18566 44 LVIGVVIAILLESL----LRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 143 VATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMIIYQrystPIVRRVRAYLADIND---GF-NEVINGMSVIQ 218
Cdd:cd18566 119 ALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLG----PILRRALKERSRADErrqNFlIETLTGIHTIK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 219 QF----RQQARFGERMGEASRSHYMARMQTLRLDGFllrplLSLFSALVlcGLLMLFGLSS---SGTIEVGVLYAFISYL 291
Cdd:cd18566 195 AMamepQMLRRYERLQANAAYAGFKVAKINAVAQTL-----GQLFSQVS--MVAVVAFGALlviNGDLTVGALIACTMLS 267
|
250 260
....*....|....*....|....*..
gi 1541475627 292 GRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18566 268 GRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
359-551 |
5.72e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 359 DITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS-HNVLRKGVAMV----QQDPVVLADTFYA 433
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLpedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 434 NVTlGRDYSQEQVWevLEKVQLADLARGFSDGINTRL--GEQG-NNLSVGQKQLLALARVLIETPQVLILDEATASIDSG 510
Cdd:PRK15439 361 NVC-ALTHNRRGFW--IKPARENAVLERYRRALNIKFnhAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1541475627 511 TEQAIQQALAAV-RDHTTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:PRK15439 438 ARNDIYQLIRSIaAQNVAVLFISSDLEEIEQmADRVLVMHQGE 480
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
28-318 |
6.77e-09 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 57.35 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 28 AVLLLWIAAIAEVSGPLLISYFIDnMVAKSYLP---LRLVAGLGVAYVGLQLAAaGLhyaQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVID-ILGGEYQHnafTSAIGLMCLFSLGSSLSA-GL---RGGLFMCTLSRLNLRLRHQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 105 MDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMII 184
Cdd:cd18590 76 FSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 185 YQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHY--MARMQTLRLDGFLLRPLLSLFS-- 260
Cdd:cd18590 156 YNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYnlKDRRDTVRAVYLLVRRVLQLGVqv 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 261 ALVLCGLLMLfglsSSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18590 236 LMLYCGRQLI----QSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
71-230 |
8.56e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 57.23 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 71 YVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSA 150
Cdd:cd18602 56 YAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 151 -ALIGAMLVAMFSLDWrMALVAITIFPAVLIVMIIYQRYSTPIVRrvrayLADINDG-----FNEVINGMSVIQQFRQQA 224
Cdd:cd18602 136 lLCLSAIIVNAIVTPY-FLIALIPIIIVYYFLQKFYRASSRELQR-----LDNITKSpvfshFSETLGGLTTIRAFRQQA 209
|
....*.
gi 1541475627 225 RFGERM 230
Cdd:cd18602 210 RFTQQM 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
309-563 |
1.20e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 309 QQAVVAGERVFELMDRPRQAyghderPLQSGAiaFDNVSfayREDRLVlQDITLDVPSRGFVALVGHTGSGKSTLASLLM 388
Cdd:PRK10261 304 QDTVVDGEPILQVRNLVTRF------PLRSGL--LNRVT---REVHAV-EKVSFDLWPGETLSLVGESGSGKSTTGRALL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 389 GYYPVTQGEIRLDGRPLASLSH---NVLRKGVAMVQQDPVVLAD-----------TFYANVTLGRDYSQEQVWEVLEKVQ 454
Cdd:PRK10261 372 RLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPYASLDprqtvgdsimePLRVHGLLPGKAAAARVAWLLERVG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 455 LadlargfsdgintrLGEQG----NNLSVGQKQLLALARVLIETPQVLILDEATASID-SGTEQAIQQALAAVRD----- 524
Cdd:PRK10261 452 L--------------LPEHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDvSIRGQIINLLLDLQRDfgiay 517
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1541475627 525 ----HTTLVV--IAHRLStivdadtilVLHRGQAVERGTHRELLE 563
Cdd:PRK10261 518 lfisHDMAVVerISHRVA---------VMYLGQIVEIGPRRAVFE 553
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
353-556 |
1.25e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.09 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 353 DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGR-----PLASLSHN----VLRKGVAMVQQD 423
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAerrrLLRTEWGFVHQH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 424 PvvlADTFYANVTLG------------RDYSQ--EQVWEVLEKVQLA-----DLARGFSDGIntrlgeqgnnlsvgqKQL 484
Cdd:PRK11701 98 P---RDGLRMQVSAGgnigerlmavgaRHYGDirATAGDWLERVEIDaaridDLPTTFSGGM---------------QQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 485 LALARVLIETPQVLILDEATASIDSgteqAIQQAL-----AAVRD-HTTLVVIAHRLSTI-VDADTILVLHRGQAVERG 556
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDV----SVQARLldllrGLVRElGLAVVIVTHDLAVArLLAHRLLVMKQGRVVESG 234
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
28-247 |
2.49e-08 |
|
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: 55.75 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 28 AVLLLWIAAIAEVSGPLLISYFIDNMVAKsyLPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDA 107
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAG--GPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 108 ALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMIIYQR 187
Cdd:cd18561 79 LLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 188 YSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRL 247
Cdd:cd18561 159 LAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAV 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
345-525 |
2.71e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 345 NVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPlaslshnvLRKGVAMVQQDP 424
Cdd:PRK13540 6 ELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS--------IKKDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 425 VVLADT--FYANVTLgRDYSQEQVWEVLEKVQLADLARGFSDG--INTRLGEqgnnLSVGQKQLLALARVLIETPQVLIL 500
Cdd:PRK13540 77 CFVGHRsgINPYLTL-RENCLYDIHFSPGAVGITELCRLFSLEhlIDYPCGL----LSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180
....*....|....*....|....*
gi 1541475627 501 DEATASIDsgtEQAIQQALAAVRDH 525
Cdd:PRK13540 152 DEPLVALD---ELSLLTIITKIQEH 173
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
357-535 |
8.71e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.86 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 357 LQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYY---PVTQGEIRLDGRPL---ASLSHNVlRKGVA----MVQQDPVV 426
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVqreGRLARDI-RKSRAntgyIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 427 LADTFYANVTLG------------RDYSQEQVWEVLEKVQLADLARGFSDGINTrlgeqgnnLSVGQKQLLALARVLIET 494
Cdd:PRK09984 99 NRLSVLENVLIGalgstpfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVST--------LSGGQQQRVAIARALMQQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1541475627 495 PQVLILDEATASIDSGTEQAIQQALAAVR--DHTTLVVIAHRL 535
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINqnDGITVVVTLHQV 213
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
351-562 |
1.11e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 351 REDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYP--------VTQGEIRLDGRPLASLSHNVL-RKGVAMVQ 421
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPRLaRLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 422 QDPVVLADTFYANVTLGRDYSQEQVWEVLEK---VQLADLARGfsdGINTRLGEQGNNLSVGQKQLLALARVL------- 491
Cdd:PRK13547 91 AAQPAFAFSAREIVLLGRYPHARRAGALTHRdgeIAWQALALA---GATALVGRDVTTLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 492 --IETPQVLILDEATASIDSGTEqaiQQALAAVRD-----HTTLVVIAHRLSTIV-DADTILVLHRGQAVERGTHRELL 562
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDLAHQ---HRLLDTVRRlardwNLGVLAIVHDPNLAArHADRIAMLADGAIVAHGAPADVL 243
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
340-502 |
1.19e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.08 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLaslshNVLR---KG 416
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-----NELEpadRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 VAMVQQDpvvladtfYA----------------NVTLGRDYSQEQVWEVLEKVQLADLargfsdgintrLGEQGNNLSVG 480
Cdd:PRK11650 78 IAMVFQN--------YAlyphmsvrenmayglkIRGMPKAEIEERVAEAARILELEPL-----------LDRKPRELSGG 138
|
170 180
....*....|....*....|..
gi 1541475627 481 QKQLLALARVLIETPQVLILDE 502
Cdd:PRK11650 139 QRQRVAMGRAIVREPAVFLFDE 160
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
28-313 |
1.59e-07 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 53.38 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 28 AVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDA 107
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 108 ALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAA-LIGAMLVAMFSLDWRMALVAITIFPAVLIVMIIYQ 186
Cdd:cd18560 81 LHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLeLIVVSVVFAFHFGAWLALIVFLSVLLYGVFTIKVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 187 RYSTPIVRRV----RAYLADINDGFnevINGMSViQQFRQQARFGERMGEASRSHYMARMQTLRLDGFL-----LRPLLS 257
Cdd:cd18560 161 EWRTKFRRAAnkkdNEAHDIAVDSL---LNFETV-KYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLnvgqqLIIQLG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1541475627 258 LFSALVLCGLLMLFGLSSsgtieVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVV 313
Cdd:cd18560 237 LTLGLLLAGYRVVDGGLS-----VGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLT 287
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
362-562 |
2.20e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 362 LDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVLRKgvamvqqdpvVLADTFYANVT----- 436
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK----------LVSDEWQRNNTdmlsp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 437 ----LGRDYSQEQVWEVLEKVQLADLARGFsdGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTE 512
Cdd:PRK10938 94 geddTGRTTAEIIQDEVKDPARCEQLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 513 QAIQQALAAVRDH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELL 562
Cdd:PRK10938 172 QQLAELLASLHQSgITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
352-560 |
2.77e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.73 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 352 EDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVT--QGEIRLDGRPLASlshNVLRKgVAMVQQDpvvlaD 429
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK---QILKR-TGFVTQD-----D 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 430 TFYANVTlgrdysqeqVWEVLEKVQLADLARGFSDGINTRLGEQ---------------GNN----LSVGQKQLLALARV 490
Cdd:PLN03211 150 ILYPHLT---------VRETLVFCSLLRLPKSLTKQEKILVAESviselgltkcentiiGNSfirgISGGERKRVSIAHE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 491 LIETPQVLILDEATASIDsgteqaiqqALAAVRDHTTLVVIAHRLSTIVDA------------DTILVLHRGQAVERGTH 558
Cdd:PLN03211 221 MLINPSLLILDEPTSGLD---------ATAAYRLVLTLGSLAQKGKTIVTSmhqpssrvyqmfDSVLVLSEGRCLFFGKG 291
|
..
gi 1541475627 559 RE 560
Cdd:PLN03211 292 SD 293
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
341-508 |
2.80e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.04 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYREdRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRplaslshnvLRKGvaMV 420
Cdd:PRK09544 5 VSLENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LRIG--YV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 421 QQ----DPvVLADTFYANVTLGRDYSQEQVWEVLEKVQLADLargfsdgintrLGEQGNNLSVGQKQLLALARVLIETPQ 496
Cdd:PRK09544 73 PQklylDT-TLPLTVNRFLRLRPGTKKEDILPALKRVQAGHL-----------IDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170
....*....|..
gi 1541475627 497 VLILDEATASID 508
Cdd:PRK09544 141 LLVLDEPTQGVD 152
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
366-549 |
2.84e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.06 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 366 SRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIrldgrplaslshnvlrkgvamvqqdpvvladtFYANVTLGRDYSQEQ 445
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLDQ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 446 VWEVLekvqladlargfsdgintrLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQAL------ 519
Cdd:smart00382 49 LLLII-------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlll 109
|
170 180 190
....*....|....*....|....*....|.
gi 1541475627 520 -AAVRDHTTLVVIAHRLSTIVDADTILVLHR 549
Cdd:smart00382 110 lLKSEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
70-229 |
3.42e-07 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 52.28 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 70 AYVGLQLAAAGL--HYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVL 147
Cdd:cd18558 62 AYYYLIIGAIVLitAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 148 RSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMIIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFG 227
Cdd:cd18558 142 QNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEE 221
|
..
gi 1541475627 228 ER 229
Cdd:cd18558 222 TR 223
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
341-533 |
3.55e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLD-VP-SRgfVALVGHTGSGKSTLASLLMGYYPVTQGEIRL-DGRPLASLSHN---VLR 414
Cdd:PRK10636 313 LKMEKVSAGY-GDRIILDSIKLNlVPgSR--IGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHqleFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 415 KGVAMVQQdpvvladtfyanvtLGRDYSQEqvwevLEKvQLADLARGFsdGIN-TRLGEQGNNLSVGQKQLLALARVLIE 493
Cdd:PRK10636 390 ADESPLQH--------------LARLAPQE-----LEQ-KLRDYLGGF--GFQgDKVTEETRRFSGGEKARLVLALIVWQ 447
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1541475627 494 TPQVLILDEATASIDSGTEQAIQQALaaVRDHTTLVVIAH 533
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLDMRQALTEAL--IDFEGALVVVSH 485
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
313-573 |
4.35e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.86 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 313 VAGERVFELmdrpRQAYGHDERPLQsgaiafdNVSFAYREDRLVlqditldvpsrGFVALVGhtgSGKSTLASLLMGYYP 392
Cdd:PRK09700 260 LAHETVFEV----RNVTSRDRKKVR-------DISFSVCRGEIL-----------GFAGLVG---SGRTELMNCLFGVDK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 393 VTQGEIRLDGRPLASLS-HNVLRKGVAMVQQDPvvlADT-FYANVTLGRDYSQEQ---------VWEVL---EKVQLADL 458
Cdd:PRK09700 315 RAGGEIRLNGKDISPRSpLDAVKKGMAYITESR---RDNgFFPNFSIAQNMAISRslkdggykgAMGLFhevDEQRTAEN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 459 ARGF----SDGINTRLGEqgnnLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALAAVRDH-TTLVVIAH 533
Cdd:PRK09700 392 QRELlalkCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSS 467
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1541475627 534 RLSTIVDA-DTILVLHRGQAVERGTHR-ELLEAKGRYWQMYQ 573
Cdd:PRK09700 468 ELPEIITVcDRIAVFCEGRLTQILTNRdDMSEEEIMAWALPQ 509
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
353-583 |
4.95e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.24 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 353 DRLVLQDITLDVpSRGFV-ALVGHTGSGKSTLASLLMGYYP----VTQGEIRLDGRPLASLShnvLR-KGVAMVQQDP-- 424
Cdd:PRK10418 15 AQPLVHGVSLTL-QRGRVlALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVAPCA---LRgRKIATIMQNPrs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 425 ---VVLADTFYANVTL---GRDYSQEQVWEVLEKVQLADLARgfsdgintRLGEQGNNLSVG--QKQLLALArVLIETPq 496
Cdd:PRK10418 91 afnPLHTMHTHARETClalGKPADDATLTAALEAVGLENAAR--------VLKLYPFEMSGGmlQRMMIALA-LLCEAP- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 497 VLILDEATASIDSGTEQAIQQALAA-VRDHTT-LVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLEAKG----RYW 569
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESiVQKRALgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAPKhavtRSL 240
|
250
....*....|....
gi 1541475627 570 QMYQLQLAGEELAA 583
Cdd:PRK10418 241 VSAHLALYGMELAS 254
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
67-230 |
5.02e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 51.71 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 67 LGVaYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATV 146
Cdd:cd18603 44 LGV-YGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 147 LRSAA-LIGAMLVAMFSLDWrmalvAITIFPAVLIVMIIYQRYSTPIVRRVR----AYLADINDGFNEVINGMSVIQQFR 221
Cdd:cd18603 123 LNCLFqVISTLVVISISTPI-----FLVVIIPLAILYFFIQRFYVATSRQLKrlesVSRSPIYSHFSETLQGASTIRAYG 197
|
....*....
gi 1541475627 222 QQARFGERM 230
Cdd:cd18603 198 VQERFIRES 206
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
67-314 |
5.68e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 51.36 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 67 LGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVtNDTEVIRDlYVT--VVA 144
Cdd:cd18783 44 LTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQ-FLTgqLFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 145 TVLRSAALIGAMLVaMFSLDWRMALV----AITIFPAVLIVMIIYQRYSTpivrrvRAYLADINDGFN--EVINGMSVIQ 218
Cdd:cd18783 122 TLLDATSLLVFLPV-LFFYSPTLALVvlafSALIALIILAFLPPFRRRLQ------ALYRAEGERQAFlvETVHGIRTVK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 219 QF----RQQARFGERMGEASRSHY-MARMQTL--RLDGFLLRpllSLFSALVLCGLLMLFglssSGTIEVGVLYAFISYL 291
Cdd:cd18783 195 SLalepRQRREWDERVARAIRARFaVGRLSNWpqTLTGPLEK---LMTVGVIWVGAYLVF----AGSLTVGALIAFNMLA 267
|
250 260
....*....|....*....|...
gi 1541475627 292 GRLNEPLIELTTQQSMLQQAVVA 314
Cdd:cd18783 268 GRVAGPLVQLAGLVQEYQEARLS 290
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
353-510 |
7.01e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 353 DRLVLQDITLDVpSRG-FVALVGHTGSGKSTLASLLMG--YYPVTQGEIRLDGRPlASLShNV---LRKGVAMVQQDP-- 424
Cdd:NF040905 272 ERKVVDDVSLNV-RRGeIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKE-VDVS-TVsdaIDAGLAYVTEDRkg 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 425 --VVLADTFYANVTLGrdySQEQVWE--VLEKVQLADLARGFSDGINTR---LGEQGNNLSVGQKQLLALARVLIETPQV 497
Cdd:NF040905 349 ygLNLIDDIKRNITLA---NLGKVSRrgVIDENEEIKVAEEYRKKMNIKtpsVFQKVGNLSGGNQQKVVLSKWLFTDPDV 425
|
170
....*....|...
gi 1541475627 498 LILDEATASIDSG 510
Cdd:NF040905 426 LILDEPTRGIDVG 438
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
67-318 |
1.13e-06 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 50.58 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 67 LGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVtNDTEVIRDLYVTVVATV 146
Cdd:cd18588 44 LAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARV-RELESIRQFLTGSALTL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 147 LRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMIIyqrySTPIVRR---VRAYLADINDGF-NEVINGMSVI----- 217
Cdd:cd18588 123 VLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLL----VTPILRRrleEKFQRGAENQSFlVETVTGIETVkslav 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 218 -QQFRQqaRFGERMGEASRSHYmaRMQTLRLDGFLLRPLLS-LFSALVLC-GLLMLFglssSGTIEVGVLYAFISYLGRL 294
Cdd:cd18588 199 ePQFQR--RWEELLARYVKASF--KTANLSNLASQIVQLIQkLTTLAILWfGAYLVM----DGELTIGQLIAFNMLAGQV 270
|
250 260
....*....|....*....|....
gi 1541475627 295 NEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18588 271 SQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
359-551 |
1.22e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.64 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 359 DITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVL----RKGVAMVQQDpvvlADTF--Y 432
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClppeKRRIGYVFQD----ARLFphY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 433 ---ANVTLG-RDYSQEQVWEVlekVQLAdlargfsdGINTRLGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASID 508
Cdd:PRK11144 92 kvrGNLRYGmAKSMVAQFDKI---VALL--------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1541475627 509 SGTEQAIQ---QALAAvRDHTTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:PRK11144 161 LPRKRELLpylERLAR-EINIPILYVSHSLDEILRlADRVVVLEQGK 206
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
351-579 |
1.26e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.47 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 351 REDRLV--LQDITLDVPsRG-FVALVGHTGSGKSTLASLLMG-YYPvTQGEIRLDGR-PLASLSHNVLRKGVAMVQ---- 421
Cdd:COG4586 30 REYREVeaVDDISFTIE-PGeIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEVRVLGYvPFKRRKEFARRIGVVFGQrsql 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 422 -QD-PVVlaDTFYANVTL----GRDYSQ--EQVWEVLEkvqLADLargfsdgINT--RlgeqgnNLSVGQKQLLALARVL 491
Cdd:COG4586 108 wWDlPAI--DSFRLLKAIyripDAEYKKrlDELVELLD---LGEL-------LDTpvR------QLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 492 IETPQVLILDEATASIDSGTEQAIQQALAAV--RDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELLEAKGRY 568
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
250
....*....|.
gi 1541475627 569 WQMyQLQLAGE 579
Cdd:COG4586 250 KTI-VLELAEP 259
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
335-553 |
1.34e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.77 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 335 PLQSGAIAFDNVSF-----------AYREDRL-VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYP--VTQGEIRL 400
Cdd:PLN03140 862 PFTPLAMSFDDVNYfvdmpaemkeqGVTEDRLqLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRI 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 401 DGRP-----LASLS----HNVLRKGVAMVQQDPVvladtFYANVTLGRDYSQEQ----VWEVLEKVQLADLargfSDGIN 467
Cdd:PLN03140 942 SGFPkkqetFARISgyceQNDIHSPQVTVRESLI-----YSAFLRLPKEVSKEEkmmfVDEVMELVELDNL----KDAIV 1012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 468 TRLGEQGnnLSVGQKQLLALARVLIETPQVLILDEATASIDSgteQAIQQALAAVRDHT----TLVVIAHRLST-IVDA- 541
Cdd:PLN03140 1013 GLPGVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA---RAAAIVMRTVRNTVdtgrTVVCTIHQPSIdIFEAf 1087
|
250
....*....|..
gi 1541475627 542 DTILVLHRGQAV 553
Cdd:PLN03140 1088 DELLLMKRGGQV 1099
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
357-545 |
1.50e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 357 LQDITLDVPSRGFVALVGHTGSGKSTLasLLMGYYpvTQGEIRL-DGRPLASlshnvlrkgvamvqQDPVVLADTFYANV 435
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLiSFLPKFS--------------RNKLIFIDQLQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 436 TLGRDYsqeqvwevlekvqladlargfsdginTRLGEQGNNLSVGQKQLLALARVLIETPQ--VLILDEATASIDsgtEQ 513
Cdd:cd03238 73 DVGLGY--------------------------LTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH---QQ 123
|
170 180 190
....*....|....*....|....*....|....*.
gi 1541475627 514 AIQQALAAVRD----HTTLVVIAHRLSTIVDADTIL 545
Cdd:cd03238 124 DINQLLEVIKGlidlGNTVILIEHNLDVLSSADWII 159
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
340-508 |
1.75e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 340 AIAFDNVSFAYReDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHnvlRKGVA- 418
Cdd:NF033858 1 VARLEGVSHRYG-KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARH---RRAVCp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 419 ----MVQqdpvvladtfyanvTLGRD-YSQEQVWEVLE-------------KVQLADLARgfSDGINTRLGEQGNNLSVG 480
Cdd:NF033858 77 riayMPQ--------------GLGKNlYPTLSVFENLDffgrlfgqdaaerRRRIDELLR--ATGLAPFADRPAGKLSGG 140
|
170 180
....*....|....*....|....*...
gi 1541475627 481 QKQLLALARVLIETPQVLILDEATASID 508
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
341-519 |
1.75e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 341 IAFDNVSFAYrEDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLdgrplaslshnvlrkG---- 416
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI---------------Getvk 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 417 VAMVQQDPVVLAD--TFYANVTLGRDYSQeqvwevLEKVQLAdlARGFSDGINTRLGEQG---NNLSVGQKQLLALARVL 491
Cdd:PRK11819 389 LAYVDQSRDALDPnkTVWEEISGGLDIIK------VGNREIP--SRAYVGRFNFKGGDQQkkvGVLSGGERNRLHLAKTL 460
|
170 180
....*....|....*....|....*...
gi 1541475627 492 IETPQVLILDEATASIDSGTEQAIQQAL 519
Cdd:PRK11819 461 KQGGNVLLLDEPTNDLDVETLRALEEAL 488
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
370-580 |
2.31e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 370 VALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGrplaslshNVLrkgVAMVQQDPV-VLADTFYANVT------------ 436
Cdd:PRK11147 32 VCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ--------DLI---VARLQQDPPrNVEGTVYDFVAegieeqaeylkr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 437 -------LGRDYSqEQVWEVLEKVQ-LADLARG--FSDGINTRLGEQG-------NNLSVGQKQLLALARVLIETPQVLI 499
Cdd:PRK11147 101 yhdishlVETDPS-EKNLNELAKLQeQLDHHNLwqLENRINEVLAQLGldpdaalSSLSGGWLRKAALGRALVSNPDVLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 500 LDEATASIDSGTEQAIQQALAAVRDhtTLVVIAH------RLST-IVDADtilvlhRGQAVE-RGTHRELLEAKGRYWQM 571
Cdd:PRK11147 180 LDEPTNHLDIETIEWLEGFLKTFQG--SIIFISHdrsfirNMATrIVDLD------RGKLVSyPGNYDQYLLEKEEALRV 251
|
250
....*....|....*.
gi 1541475627 572 YQLQ-------LAGEE 580
Cdd:PRK11147 252 EELQnaefdrkLAQEE 267
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
344-587 |
3.96e-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: 49.55 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYREDRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIR---------LDGRPLASLSHNVlR 414
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARpqpgikvgyLPQEPQLDPTKTV-R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 415 KGVAMVQQDPVVLADTF---YANVTL-GRDYS-----QEQVWEVLEKVQLADLARGFSDGINT-RL--GEQG-NNLSVGQ 481
Cdd:TIGR03719 87 ENVEEGVAEIKDALDRFneiSAKYAEpDADFDklaaeQAELQEIIDAADAWDLDSQLEIAMDAlRCppWDADvTKLSGGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 482 KQLLALARVLIETPQVLILDEATASIDSGTEQAIQQALaavRDHT-TLVVIAH-R--LSTIvdADTILVLHRGQAVE-RG 556
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL---QEYPgTVVAVTHdRyfLDNV--AGWILELDRGRGIPwEG 241
|
250 260 270
....*....|....*....|....*....|.
gi 1541475627 557 THRELLEAKgrywqmyQLQLAGEELAASVRE 587
Cdd:TIGR03719 242 NYSSWLEQK-------QKRLEQEEKEESARQ 265
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
28-196 |
6.48e-06 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 48.26 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 28 AVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDA 107
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRVFRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 108 ALRQPLSEFDIQPVG---QVISRVTNDTE-VIRDLYVTVVATVLRsAALIGAMLVAMFslDWRMALVAITIFPAVLIVMI 183
Cdd:cd18582 81 LHSLSLRFHLSRKTGalsRAIERGTRGIEfLLRFLLFNILPTILE-LLLVCGILWYLY--GWSYALITLVTVALYVAFTI 157
|
170
....*....|...
gi 1541475627 184 IYQRYSTPIVRRV 196
Cdd:cd18582 158 KVTEWRTKFRREM 170
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
28-237 |
1.28e-05 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 47.15 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 28 AVLLLWIAAIAEVSGPLLISYFIdNMVAKSYLP-----LRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRT 102
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLV-NVISRSLKEtngdfIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 103 DVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVM 182
Cdd:cd18574 80 DLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1541475627 183 IIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQF----RQQARFGERMGEASRSH 237
Cdd:cd18574 160 TLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFamedRELELYEEEVEKAAKLN 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
342-566 |
1.94e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 342 AFDNVSFAYRedrlvlqditldvpsR----GFValvGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLSHNVlRKGV 417
Cdd:NF033858 281 AVDHVSFRIR---------------RgeifGFL---GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIAT-RRRV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 418 A-M-----------VQQDPVVLADTFYanvtLGRDYSQEQVWEVLEKVQLADLARGFSDgintrlgeqgnNLSVGQKQLL 485
Cdd:NF033858 342 GyMsqafslygeltVRQNLELHARLFH----LPAAEIAARVAEMLERFDLADVADALPD-----------SLPLGIRQRL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 486 ALARVLIETPQVLILDEATASIDSGTEQAIQQALA--AVRDHTTLVVIAHRLSTIVDADTILVLHRGQAVERGTHRELLE 563
Cdd:NF033858 407 SLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIelSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVA 486
|
...
gi 1541475627 564 AKG 566
Cdd:NF033858 487 ARG 489
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
357-568 |
2.36e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 357 LQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDGRPLASLS-HNVLRKGVAMVQQDPvvLADTFYANV 435
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEER--RSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 436 TLGRDYSQEQVWEVLEKVQLADLARGFSD-------------GINTRLGeqgnNLSVGQKQLLALARVLIETPQVLILDE 502
Cdd:PRK10982 342 DIGFNSLISNIRNYKNKVGLLDNSRMKSDtqwvidsmrvktpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1541475627 503 ATASIDSGTEQAIQQALA--AVRDHTTLVVIAHRLSTIVDADTILVLHRGQAV-----ERGTHRELLEAKGRY 568
Cdd:PRK10982 418 PTRGIDVGAKFEIYQLIAelAKKDKGIIIISSEMPELLGITDRILVMSNGLVAgivdtKTTTQNEILRLASLH 490
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
353-569 |
4.23e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.40 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 353 DRLVLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGY--YPVTQGEIRLDGRPLASL-----SHnvlrKGVAMVQQDPV 425
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLepeerAH----LGIFLAFQYPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 426 VLADTfyANVTLGR-DYSQEQVWEVL-------------EKVQLADLARGFsdgINTRLGEqgnNLSVGQK---QLLALA 488
Cdd:CHL00131 95 EIPGV--SNADFLRlAYNSKRKFQGLpeldplefleiinEKLKLVGMDPSF---LSRNVNE---GFSGGEKkrnEILQMA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 489 rvLIEtPQVLILDEatasIDSGTE----QAIQQALAAVRDHTT-LVVIAH--RLSTIVDADTILVLHRGQAVERGThREL 561
Cdd:CHL00131 167 --LLD-SELAILDE----TDSGLDidalKIIAEGINKLMTSENsIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD-AEL 238
|
250
....*....|.
gi 1541475627 562 ---LEAKGRYW 569
Cdd:CHL00131 239 akeLEKKGYDW 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
356-563 |
6.30e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.08 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 356 VLQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEI----------RLDGRPLASLSHNV------------- 412
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEKVLEKLViqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 413 -LRKGVAMVQQ-------DPVVLADTFYANVTLGRDySQEQVWEVLEKVQLADLARGFsdgintrLGEQGNNLSVGQKQL 484
Cdd:PRK13651 102 eIRRRVGVVFQfaeyqlfEQTIEKDIIFGPVSMGVS-KEEAKKRAAKYIELVGLDESY-------LQRSPFELSGGQKRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 485 LALARVLIETPQVLILDEATASID-SGTEQAIQQALAAVRDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHRELL 562
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDpQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEwTKRTIFFKDGKIIKDGDTYDIL 253
|
.
gi 1541475627 563 E 563
Cdd:PRK13651 254 S 254
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
374-508 |
6.30e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.45 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 374 GHTGSGKSTLASLLMGYYPVTQGEIRLDGRP---------LASLSHnvlrkgVAMVQQDPVVLADTFYANVTLGRdYSQE 444
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTatrgdrsrfMAYLGH------LPGLKADLSTLENLHFLCGLHGR-RAKQ 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 445 QVWEVLEKVQLADLARGFSdgintrlgeqgNNLSVGQKQLLALARVLIETPQVLILDEATASID 508
Cdd:PRK13543 117 MPGSALAIVGLAGYEDTLV-----------RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
71-270 |
1.21e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 44.23 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 71 YVGLQLAAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDLYVTVVATVLRSA 150
Cdd:cd18601 65 YAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 151 ALI-GAMLVAMFSLDWrmalVAITIFPaVLIVMIIYQRYSTPIVRRVRAyLADINDG-----FNEVINGMSVIQQFRQQA 224
Cdd:cd18601 145 LQVvGVVLLAVVVNPW----VLIPVIP-LVILFLFLRRYYLKTSREVKR-IEGTTRSpvfshLSSTLQGLWTIRAYSAQE 218
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1541475627 225 RFGERMGEASRSH---YMARMQTLRLDGFLLRPLLSLFSALVLCGLLML 270
Cdd:cd18601 219 RFQEEFDAHQDLHseaWFLFLATSRWLAVRLDALCALFVTVVAFGSLFL 267
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
286-502 |
2.74e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 286 AFISYLGRLNE-PLIELTTQQSMLQQAVVA----GERVFELM----DRPRQaygHDERPLQSGAIAFDNVSFAYrEDRLV 356
Cdd:PRK10938 200 DFVQFAGVLADcTLAETGEREEILQQALVAqlahSEQLEGVQlpepDEPSA---RHALPANEPRIVLNNGVVSY-NDRPI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 357 LQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPvtQG---EIRLDGRPLAS-----------------------LSH 410
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP--QGysnDLTLFGRRRGSgetiwdikkhigyvssslhldyrVST 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 411 NVLRkgvamvqqdpvVLADTFYANVTLGRDYSQEQvwevlekVQLAD--LARgfsDGINTRLGEQG-NNLSVGQKQLLAL 487
Cdd:PRK10938 354 SVRN-----------VILSGFFDSIGIYQAVSDRQ-------QKLAQqwLDI---LGIDKRTADAPfHSLSWGQQRLALI 412
|
250
....*....|....*
gi 1541475627 488 ARVLIETPQVLILDE 502
Cdd:PRK10938 413 VRALVKHPTLLILDE 427
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
122-288 |
3.52e-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: 42.85 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 122 GQVISRVTNDTEVIRDLYVTVVATVLrsAALIGAMLVAMF--SLDWRMALVAITIFPAVLIVM-IIYQRYSTPIVRRVRA 198
Cdd:cd18585 92 GDLLNRIVADIDTLDNLYLRVLSPPV--VALLVILATILFlaFFSPALALILLAGLLLAGVVIpLLFYRLGKKIGQQLVQ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 199 YLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYM--ARMQTLRLDGFLLRPLLSLFSalVLCGLLMLFGLSSS 276
Cdd:cd18585 170 LRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKeqRRLARLSGLSQALMILLSGLT--VWLVLWLGAPLVQN 247
|
170
....*....|..
gi 1541475627 277 GTIEvGVLYAFI 288
Cdd:cd18585 248 GALD-GALLAML 258
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
344-553 |
3.78e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 41.86 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 344 DNVSFAYREDRLVLqditldvpsrgfvaLVGHTGSGKSTL----ASLLMGYYPVTqGEIRLDGRPLASLsHNVLRKGVAM 419
Cdd:cd03233 24 KDFSGVVKPGEMVL--------------VLGRPGSGCSTLlkalANRTEGNVSVE-GDIHYNGIPYKEF-AEKYPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 420 VQQDpvvlaDTFYANVTlgrdysqeqVWEVLEkvqladlargFSdginTRLgeQGNN----LSVGQKQLLALARVLIETP 495
Cdd:cd03233 88 VSEE-----DVHFPTLT---------VRETLD----------FA----LRC--KGNEfvrgISGGERKRVSIAEALVSRA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1541475627 496 QVLILDEATASIDSGTEQAIQQALAAVRD--HTTLVVIAHRLS-TIVDA-DTILVLHRGQAV 553
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTMADvlKTTTFVSLYQASdEIYDLfDKVLVLYEGRQI 199
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
43-318 |
6.76e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 42.15 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 43 PLLISYFIDNMVAKSYLPLRLVAGLGVAYVGLQLAAAGLHYAQSLLFNRAAVGVvqQLRTDVMDAALRQPLSEFDIQPVG 122
Cdd:cd18779 22 PLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDT--QLTLGFLEHLLRLPYRFFQQRSTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 123 QVISRVTNDTeVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAITIFPAVLIVMIIYQRYSTPIVRRVRAYLAD 202
Cdd:cd18779 100 DLLMRLSSNA-TIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLATRRRVRELMARELAAQAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 203 INDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFL--LRPLLSLFSALVlcglLMLFGLSS--SGT 278
Cdd:cd18779 179 AQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVdaLLATLRLAAPLV----LLWVGAWQvlDGQ 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1541475627 279 IEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
Cdd:cd18779 255 LSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
30-268 |
8.98e-04 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 41.46 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 30 LLLWIAAIAEVSGPL----LISYFIDNMVAKSYLPLRLVAGLGVAYVGLQLaaagLHyaQSLLFNRAAVGVvqQLR---- 101
Cdd:cd18594 4 ILLFLEESLKIVQPLllgrLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVL----LH--HPYFFGLHRYGM--QLRials 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 102 TDVMDAALRQPLSEFDIQPVGQVISRVTNDTEVIRDlyVTVVATVLRSAALigaMLVAMFSLDWRMALVAITIFPAVLIV 181
Cdd:cd18594 76 SLIYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDE--VLVYLHFLWIAPL---QVIVLTGLLWREIGPSSLAGLGVLLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 182 MIIYQRY-STPIVRRVRAYLADINDGF---NEVINGMSVIQQFRQQARFGE-----RMGEASRSHYMARMQTLRLDGFLL 252
Cdd:cd18594 151 LLPLQAYlGKLFAKYRRKTAGLTDERVkimNEIISGMRVIKMYTWEESFAKlieniRKKELKLIRKAAYIRAFNMAFFFF 230
|
250
....*....|....*.
gi 1541475627 253 RPLLSLFSALVLCGLL 268
Cdd:cd18594 231 SPTLVSFATFVPYVLT 246
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
152-318 |
1.92e-03 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 40.59 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 152 LIGAMLVAMFSLDWRMALVaitifpaVLIVMIIYQRYSTPIVRRVRAYLADINDGF-------NEVINGMSVIQQFRQQA 224
Cdd:cd18583 124 LVIAIVYLYYLFDPYMGLI-------VAVVMVLYVWSTIKLTSWRTKLRRDMIDADreersilTESLLNWETVKYFNREP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 225 RFGERMGEASRSHyMARMQTLRLDGFLLRPLLSLfsaLVLCGLLMLFGLS----SSGTIEVGVLYAFISYLGRLNEPLIE 300
Cdd:cd18583 197 YEKERYREAVKNY-QKAERKYLFSLNLLNAVQSL---ILTLGLLAGCFLAayqvSQGQATVGDFVTLLTYWAQLSGPLNF 272
|
170
....*....|....*...
gi 1541475627 301 LTTQQSMLQQAVVAGERV 318
Cdd:cd18583 273 FATLYRSIQSDLIDAERL 290
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
357-384 |
2.05e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 2.05e-03
10 20
....*....|....*....|....*...
gi 1541475627 357 LQDITLDVPSRGFVALVGHTGSGKSTLA 384
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSLA 39
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
437-571 |
2.17e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 437 LGRDYSQEQVWEVLEKVQLADLArgfsdgintrlGEQGNNLSVGQKQLLALARVLIETPQVLILDEATASIDSGTEQAI- 515
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAA-----------GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVw 184
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1541475627 516 QQALAAVRDHTTLVVIAHRLSTIVD-ADTILVLHRGQAVERGTHREL-LEAKGRYWQM 571
Cdd:NF000106 185 DEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELkTKVGGRTLQI 242
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
357-402 |
2.58e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 2.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1541475627 357 LQDITLDVPSRGFVALVGHTGSGKSTLASLLMGYYPVTQGEIRLDG 402
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
27-246 |
2.67e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 40.13 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 27 VAVLLLWIAAIAEVSGPLLISYFIDNMVAKSYLPLRLVAGLGVAYVglqLAAAGLHYAQSLLFNRA-----AVGVvqQLR 101
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDAYLGGPPPSIGYGIGYA---IGLFLLQLLSSLLLNHFfyrsmLTGA--QVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 102 TDVMDAALRQPL-------SEFdiqPVGQVISRVTNDTEVIrDLYVTVVATVLrsAALIgAMLVAMFSLDWRM---ALVA 171
Cdd:cd18597 76 AALTKAIYRKSLrlsgksrHEF---PNGKITNLMSTDLSRI-DFALGFFHFLW--TAPI-QIIIAIALLIVNLgpsALVG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 172 ItifpAVLIVMIIYQRYSTPIVRRVRAYLADINDG----FNEVINGMSVIQQFRQQARFGERMGEASRS--HYMARMQTL 245
Cdd:cd18597 149 I----GVLILSIPLQGFLMKKLFKLRKKANKITDKrvklTQEILQGIRVIKFYAWEDAFLERITEIRKKelKYVRKLQIL 224
|
.
gi 1541475627 246 R 246
Cdd:cd18597 225 R 225
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
331-533 |
3.94e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 38.90 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 331 HDERPLQSGAIAFDNVSFAYREDrlVLQDItldVPSRGFVALVGHTGSGKSTLASLLMgyYPVTQGEiRLDGRPLASLSH 410
Cdd:pfam13481 2 AEPLELLDVLADGLAAPPPPRRW--LIKGL---LPAGGLGLLAGAPGTGKTTLALDLA--AAVATGK-PWLGGPRVPEQG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1541475627 411 NVLrkgvaMVQ--QDPVVLADTFYAnvtLGRDYSQEQVWEVLekvqladlargfSDGINTRLGEQGNNLSVGQKQLLALA 488
Cdd:pfam13481 74 KVL-----YVSaeGPADELRRRLRA---AGADLDLPARLLFL------------SLVESLPLFFLDRGGPLLDADVDALE 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1541475627 489 RVL--IETPQVLILDEATASI-----DSGTEQAIQQALAAVRDHT--TLVVIAH 533
Cdd:pfam13481 134 AALeeVEDPDLVVIDPLARALggdenSNSDVGRLVKALDRLARRTgaTVLLVHH 187
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
338-399 |
7.92e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.16 E-value: 7.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1541475627 338 SGAIAFD--NVSFAYrEDRLVLQDITLDVpSRG-FVALVGHTGSGKSTLASLLMGYYPVTQGEIR 399
Cdd:PRK11147 315 SGKIVFEmeNVNYQI-DGKQLVKDFSAQV-QRGdKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
|
|
| |
