|
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: 1226.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 1 MRSFSQLWPTLKRLLAYGSPWRKPLGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVVAGLAAAYVGLQLFAAG 80
Cdd:PRK10790 1 MRSFSQLWPTLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVAGLAAAYVGLQLLAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 81 LHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAM 160
Cdd:PRK10790 81 LHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 161 FSLDWRMALVAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMA 240
Cdd:PRK10790 161 FSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 241 RMQTLRLDGFLLRPLLSLFSSLILCGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERVFE 320
Cdd:PRK10790 241 RMQTLRLDGFLLRPLLSLFSALILCGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 321 LMDGPRQQYGNDDRPLQSGTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL 400
Cdd:PRK10790 321 LMDGPRQQYGNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 401 DGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVG 480
Cdd:PRK10790 401 DGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 481 QKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQ 560
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQ 560
|
570 580 590
....*....|....*....|....*....|..
gi 447178945 561 LLAAQGRYWQMYQLQLAGEELAASVREEESLS 592
Cdd:PRK10790 561 LLAAQGRYWQMYQLQLAGEELAASVREEESLS 592
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-579 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 571.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 8 WPTLKRLLAYGSPWRKPLGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLkvVAGLAAAYVGLQLFAAGLHYAQSL 87
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA--LLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 88 LFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRM 167
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 168 ALVAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRL 247
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 248 DGFLLRPLLSLFSSLILCGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERVFELMD-GPR 326
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDePPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 327 QQYGNDDRPLQ--SGTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRP 404
Cdd:COG1132 324 IPDPPGAVPLPpvRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 405 LSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQ 483
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 484 LLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLA 563
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA 563
|
570
....*....|....*.
gi 447178945 564 AQGRYWQMYQLQLAGE 579
Cdd:COG1132 564 RGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-576 |
7.67e-134 |
|
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: 406.91 E-value: 7.67e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 10 TLKRLLAYGSPWRKPLGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVVagLAAAYVGLQLFAAGLHYAQSLLF 89
Cdd:COG2274 143 GLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWV--LAIGLLLALLFEGLLRLLRSYLL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 90 NRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVtNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMAL 169
Cdd:COG2274 221 LRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLAL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 170 VAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDG 249
Cdd:COG2274 300 VVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 250 FLLRPLLSLFSSLIlcGLLMLFGFSA--SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERVFELMDGPRQ 327
Cdd:COG2274 380 LLSTLSGLLQQLAT--VALLWLGAYLviDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 328 QYGND---DRPLQSGTIEVDNVSFAYRDDN-LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR 403
Cdd:COG2274 458 REEGRsklSLPRLKGDIELENVSFRYPGDSpPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 404 PLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQK 482
Cdd:COG2274 538 DLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDpDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQR 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 483 QLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLL 562
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
570
....*....|....
gi 447178945 563 AAQGRYWQMYQLQL 576
Cdd:COG2274 698 ARKGLYAELVQQQL 711
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-566 |
3.52e-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: 3.52e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 12 KRLLAYGSPWRKPLGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNnLPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNR 91
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGG-APLSALLPLLGLLLAVLLLRALLAWLRERAAFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 92 AAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVA 171
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 172 IMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLdgfl 251
Cdd:COG4988 165 LVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRV---- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 252 lrpllslfsslilcGLLMLFG--FSASGTIEVGVLYAFISYL-GRLN---------------EPLIELTTQ--QAMlqQA 311
Cdd:COG4988 241 --------------AFLSSAVleFFASLSIALVAVYIGFRLLgGSLTlfaalfvlllapeffLPLRDLGSFyhARA--NG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 312 VVAGERVFELMDGPRQQYGNDDRPL---QSGTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLM 388
Cdd:COG4988 305 IAAAEKIFALLDAPEPAAPAGTAPLpaaGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 389 GYYPLTEGEIRLDGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIY 467
Cdd:COG4988 385 GFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLD 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 468 TPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVL 547
Cdd:COG4988 465 TPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVL 544
|
570
....*....|....*....
gi 447178945 548 HRGQAVEQGTHQQLLAAQG 566
Cdd:COG4988 545 DDGRIVEQGTHEELLAKNG 563
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
10-577 |
1.72e-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: 332.07 E-value: 1.72e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 10 TLKRLLAYGSPWRKPLGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLplKVVAGLAAAYVGLQLFAAGLHYAQSLLF 89
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDR--SVLWWVPLVVIGLAVLRGICSFVSTYLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 90 NRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMAL 169
Cdd:TIGR02203 79 SWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 170 VAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDG 249
Cdd:TIGR02203 159 IVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 250 FLLRPLLSLFSSLILCGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERVFELMDGP-RQQ 328
Cdd:TIGR02203 239 ISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPpEKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 329 YGNDDRPLQSGTIEVDNVSFAYRDDNL-VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS 407
Cdd:TIGR02203 319 TGTRAIERARGDVEFRNVTFRYPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 408 LSHSALRQGVAMVQQDPVVLADTFLANVTLGR--DISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLL 485
Cdd:TIGR02203 399 YTLASLRRQVALVSQDVVLFNDTIANNIAYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 486 ALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQ 565
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARN 558
|
570
....*....|..
gi 447178945 566 GRYWQMYQLQLA 577
Cdd:TIGR02203 559 GLYAQLHNMQFR 570
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
339-566 |
4.69e-100 |
|
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: 303.38 E-value: 4.69e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 339 GTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVA 418
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 419 MVQQDPVVLADTFLANVTLGRDIS-EERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQI 497
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNAtDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 498 LILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQG 566
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
25-318 |
5.07e-99 |
|
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: 303.15 E-value: 5.07e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVI 184
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 185 YQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFlLRPLLSLFSSLIL 264
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFAL-FRPLVELLSSLAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 447178945 265 CGLLMLFGFSA-SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18544 240 ALVLWYGGGQVlSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
10-574 |
3.09e-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: 3.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 10 TLKRLLAYGSPWRKPLGIAVLMMWVAAAAEVSgpLLI--SYFIDNMVaknnlplkvVAGLAAAY----VGLQLFA---AG 80
Cdd:COG4987 2 DLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIG--LLAlsGWLIAAAA---------LAPPILNLfvpiVGVRAFAigrTV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 81 LHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAM 160
Cdd:COG4987 71 FRYLERLVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 161 FSLDWRMALV-AIMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYM 239
Cdd:COG4987 151 AFFSPALALVlALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 240 ARMQTLRLDGFLLRPLLSLFSSLILCGLLMLFGFSASGTIEVGVLYAFI-SYLGrLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:COG4987 231 AQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVlAALA-LFEALAPLPAAAQHLGRVRAAARRL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 319 FELMDGPR--QQYGNDDRPLQSGTIEVDNVSFAYRDDN-LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTE 395
Cdd:COG4987 310 NELLDAPPavTEPAEPAPAPGGPSLELEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 396 GEIRLDGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIYTPLGEQG 474
Cdd:COG4987 390 GSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARpDATDEELWAALERVGLGDWLAALPDGLDTWLGEGG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 475 NNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVE 554
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVE 549
|
570 580
....*....|....*....|
gi 447178945 555 QGTHQQLLAAQGRYWQMYQL 574
Cdd:COG4987 550 QGTHEELLAQNGRYRQLYQR 569
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-587 |
1.25e-95 |
|
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: 304.82 E-value: 1.25e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 2 RSFSQLWPTLKRLLAYGSPWRKP--LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVVA---GLAAAYVGLQL 76
Cdd:COG5265 10 PAAPPRLDLLLRLLLLLLLPPYLrrRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVvpvGLLLAYGLLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 77 FAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLS---EFDTQPVGQVISRVTNDTE-VIRDLYVTVVATVLRsAAL 152
Cdd:COG5265 90 LSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRfhlERQTGGLSRDIERGTKGIEfLLRFLLFNILPTLLE-IAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 153 VGAMLVAMFslDWRMALVaimifpvVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIiNGMSV--------IQQFRQQA 224
Cdd:COG5265 169 VAGILLVKY--DWWFALI-------TLVTVVLYIAFTVVVTEWRTKFRREMNEADSEA-NTRAVdsllnyetVKYFGNEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 225 RFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSslilCGLLMLFGFSA----SGTIEVGVLYAFISYLGRLNEPLIE 300
Cdd:COG5265 239 REARRYDEALARYERAAVKSQTSLALLNFGQALIIA----LGLTAMMLMAAqgvvAGTMTVGDFVLVNAYLIQLYIPLNF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 301 LTTQQAMLQQAVVAGERVFELMDGPRQQYGNDD-RPLQS--GTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTG 377
Cdd:COG5265 315 LGFVYREIRQALADMERMFDLLDQPPEVADAPDaPPLVVggGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 378 SGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLA 456
Cdd:COG5265 395 AGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRpDASEEEVEAAARAAQIH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 457 ELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAV-REHTTLVvIAHRL 535
Cdd:COG5265 475 DFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVaRGRTTLV-IAHRL 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 447178945 536 STIVDADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEELAASVRE 587
Cdd:COG5265 554 STIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEALAA 605
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
9-571 |
5.19e-88 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 287.77 E-value: 5.19e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 9 PTLKRLLAYGSPWRKPLGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPlkvvaGLAAAYVGLQLFAAGLHYAQSLL 88
Cdd:TIGR00958 147 DLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPP-----ALASAIFFMCLLSIASSVSAGLR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 89 ---FNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDW 165
Cdd:TIGR00958 222 ggsFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSP 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 166 RMALVAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFrqqarfGERMGEASRshYMARMQ-T 244
Cdd:TIGR00958 302 RLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSF------AAEEGEASR--FKEALEeT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 245 LRLDGFLLRPLLSLFSSLILCGLLMLFGFSA-------SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGER 317
Cdd:TIGR00958 374 LQLNKRKALAYAGYLWTTSVLGMLIQVLVLYyggqlvlTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 318 VFELMD-GPRQQYGNDDRPLQ-SGTIEVDNVSFAY--RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPL 393
Cdd:TIGR00958 454 VFEYLDrKPNIPLTGTLAPLNlEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 394 TEGEIRLDGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLG-RDISEERVWQALETVQLAELARSMSDGIYTPLGE 472
Cdd:TIGR00958 534 TGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 473 QGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAavREHTTLVVIAHRLSTIVDADTILVLHRGQA 552
Cdd:TIGR00958 614 KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
570
....*....|....*....
gi 447178945 553 VEQGTHQQLLAAQGRYWQM 571
Cdd:TIGR00958 692 VEMGTHKQLMEDQGCYKHL 710
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
341-575 |
1.54e-82 |
|
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: 258.31 E-value: 1.54e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMV 420
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILI 499
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 500 LDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-576 |
1.44e-80 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 264.57 E-value: 1.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 8 WPTLKRLLAYGSPWRKPLGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLplKVVAGLAAAYVGLQLFAAGLHYAQSL 87
Cdd:PRK11176 10 WQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADR--SVLKWMPLVVIGLMILRGITSFISSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 88 LFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRM 167
Cdd:PRK11176 88 CISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 168 ALVAIMIFPVVLVVM-VIYQRYSTpIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASrsHYMaRMQTLR 246
Cdd:PRK11176 168 SLILIVIAPIVSIAIrVVSKRFRN-ISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVS--NRM-RQQGMK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 247 L---DGFLLRPLLSLFSSLILCGLlmlfgFSAS----------GTIEVgvlyAFISYLGrLNEPLIELTTQQAMLQQAVV 313
Cdd:PRK11176 244 MvsaSSISDPIIQLIASLALAFVL-----YAASfpsvmdtltaGTITV----VFSSMIA-LMRPLKSLTNVNAQFQRGMA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 314 AGERVFELMD-GPRQQYGNDDRPLQSGTIEVDNVSFAYRD-DNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYY 391
Cdd:PRK11176 314 ACQTLFAILDlEQEKDEGKRVIERAKGDIEFRNVTFTYPGkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 392 PLTEGEIRLDGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGRD--ISEERVWQALETVQLAELARSMSDGIYTP 469
Cdd:PRK11176 394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeqYSREQIEEAARMAYAMDFINKMDNGLDTV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 470 LGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHR 549
Cdd:PRK11176 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVED 553
|
570 580
....*....|....*....|....*..
gi 447178945 550 GQAVEQGTHQQLLAAQGRYWQMYQLQL 576
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVYAQLHKMQF 580
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
11-576 |
6.11e-80 |
|
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: 262.71 E-value: 6.11e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 11 LKRLLAYGSPWRKPLGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPL--KVVAGLAAAYVGLQLFAAGLHYAQSLL 88
Cdd:TIGR02204 6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLlnRYFAFLLVVALVLALGTAARFYLVTWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 89 FNRaavgVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMA 168
Cdd:TIGR02204 86 GER----VVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 169 LVAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQtlRLD 248
Cdd:TIGR02204 162 SLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQ--RIR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 249 GFLLRPLLSLFSSLILCGLLMLFGFS--ASGTIEVGVLYAFISY-------LGRLNEPLIELttqqamlQQAVVAGERVF 319
Cdd:TIGR02204 240 TRALLTAIVIVLVFGAIVGVLWVGAHdvIAGKMSAGTLGQFVFYavmvagsIGTLSEVWGEL-------QRAAGAAERLI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 320 ELMdgprqQYGNDDR-PLQ--------SGTIEVDNVSFAY--RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLM 388
Cdd:TIGR02204 313 ELL-----QAEPDIKaPAHpktlpvplRGEIEFEQVNFAYpaRPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 389 GYYPLTEGEIRLDGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIY 467
Cdd:TIGR02204 388 RFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRpDATDEEVEAAARAAHAHEFISALPEGYD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 468 TPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVL 547
Cdd:TIGR02204 468 TYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVM 547
|
570 580
....*....|....*....|....*....
gi 447178945 548 HRGQAVEQGTHQQLLAAQGRYWQMYQLQL 576
Cdd:TIGR02204 548 DQGRIVAQGTHAELIAKGGLYARLARLQF 576
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
341-572 |
1.95e-79 |
|
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: 250.23 E-value: 1.95e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDD-NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAM 419
Cdd:cd03251 1 VEFKNVTFRYPGDgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQIL 498
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447178945 499 ILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY 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 |
1.77e-78 |
|
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: 247.84 E-value: 1.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAY--RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVA 418
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 419 MVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQI 497
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKpDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 498 LILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
339-557 |
2.02e-76 |
|
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: 242.01 E-value: 2.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 339 GTIEVDNVSFAYRDD-NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGV 417
Cdd:cd03244 1 GDIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVVLADTFLANVtlgrDI----SEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVE 493
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNL----DPfgeySDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447178945 494 TPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGT 557
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
25-547 |
9.69e-73 |
|
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: 242.19 E-value: 9.69e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAevsgplLISYFIDNMVAKNnLPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:TIGR02857 11 LGVLGALLIIAQAW------LLARVVDGLISAG-EPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIrDLYVTVVATVLRSAALVG-AMLVAMFSLDWRMALVAIMIFPVVLVVMV 183
Cdd:TIGR02857 84 LEAVAALGPRWLQGRPSGELATLALEGVEAL-DGYFARYLPQLVLAVIVPlAILAAVFPQDWISGLILLLTAPLIPIFMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 184 IYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLR---LDGFL--LRPLLSL 258
Cdd:TIGR02857 163 LIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRiafLSSAVleLFATLSV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 259 FSSLILCGLLMLFGFSASGTIEVGVLYAFISYLgrlnePLIELTTQQAMLQQAVVAGERVFELMDGPRQQYGN--DDRPL 336
Cdd:TIGR02857 243 ALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYL-----PLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGkaPVTAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 337 QSGTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQG 416
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 417 VAMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETP 495
Cdd:TIGR02857 398 IAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 447178945 496 QILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVL 547
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
109-568 |
4.72e-69 |
|
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: 236.76 E-value: 4.72e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 109 LRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLrSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQRY 188
Cdd:TIGR03796 238 LRLPVRFFAQRHAGDIASRVQLNDQVAEFLSGQLATTAL-DAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 189 STPIVRRVRAYLADINdgfNEIINGMSVIQQFRqqARFGERMGEASRSHYMAR----MQTLRLDGFLLRPLLSLFSSLIL 264
Cdd:TIGR03796 317 RVDANRRLQQDAGKLT---GVAISGLQSIETLK--ASGLESDFFSRWAGYQAKllnaQQELGVLTQILGVLPTLLTSLNS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 265 CGLLMLFGFSA-SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERVFELMDGPRQQYGNDDRPLQ------ 337
Cdd:TIGR03796 392 ALILVVGGLRVmEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRNPVDPLLEEPEGSAatsepp 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 338 ---SGTIEVDNVSFAY-RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAL 413
Cdd:TIGR03796 472 rrlSGYVELRNITFGYsPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQGVAMVQQDPVVLADTFLANVTL-GRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLV 492
Cdd:TIGR03796 552 ANSVAMVDQDIFLFEGTVRDNLTLwDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALV 631
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 493 ETPQILILDEATASIDSGTEQAIQHALAavREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQGRY 568
Cdd:TIGR03796 632 RNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAY 705
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
341-551 |
2.72e-65 |
|
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: 211.09 E-value: 2.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRD-DNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAM 419
Cdd:cd03228 1 IEFKNVSFSYPGrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLADTFLANVtlgrdiseervwqaletvqlaelarsmsdgiytplgeqgnnLSVGQKQLLALARVLVETPQILI 499
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447178945 500 LDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQ 551
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
30-572 |
1.15e-64 |
|
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: 225.00 E-value: 1.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 30 LMMWVAAAAEVSGPLLI--SYFIDNMV-----AKNNLPLKVVA-GLAAAYVGLQLFAaglhYAQSLLFNRAAvgvvQQLR 101
Cdd:TIGR01193 157 LIVNIVIAAIIVTLISIagSYYLQKIIdtyipHKMMGTLGIISiGLIIAYIIQQILS----YIQIFLLNVLG----QRLS 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 102 TDVMDAALRQ----PLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAAL--VGAMLVAMFSLDWRMALVAImif 175
Cdd:TIGR01193 229 IDIILSYIKHlfelPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILviVGLFLVRQNMLLFLLSLLSI--- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 176 PVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRqqarfgermGEASRSHYM-ARMQTLRLDGFLLRP 254
Cdd:TIGR01193 306 PVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLT---------SEAERYSKIdSEFGDYLNKSFKYQK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 255 LLSLFSSLILCGLLML------FG--FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERVFE--LMDG 324
Cdd:TIGR01193 377 ADQGQQAIKAVTKLILnvvilwTGayLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDS 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 325 PRQQYGNDDRPLQS-GTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR 403
Cdd:TIGR01193 457 EFINKKKRTELNNLnGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 404 PLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLG--RDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQ 481
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQ 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 482 KQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVReHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQL 561
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
570
....*....|.
gi 447178945 562 LAAQGRYWQMY 572
Cdd:TIGR01193 696 LDRNGFYASLI 706
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-535 |
1.81e-61 |
|
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: 212.22 E-value: 1.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 11 LKRLLAYGSPWRKPLGIAVLMMWVAAAAEVSGPLLISYFIdnmvAKNNLPLKVVAgLAAAYVGLQLFAAG---LHYAQSL 87
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLI----SRAAEMPPVLY-LSVAAVAVRAFGIGravFRYLERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 88 LFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRM 167
Cdd:TIGR02868 76 VGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 168 ALVAIMIFPVVLVVMVIYQ----RYSTPIVRRVRAYLADindGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQ 243
Cdd:TIGR02868 156 ALILAAGLLLAGFVAPLVSlraaRAAEQALARLRGELAA---QLTDALDGAAELVASGALPAALAQVEEADRELTRAERR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 244 TLRLDGFLLRPLLSLFSSLILCGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERVFELMD 323
Cdd:TIGR02868 233 AAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 324 GPR-----QQYGNDDRPLQSGTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEI 398
Cdd:TIGR02868 313 AAGpvaegSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 399 RLDGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNL 477
Cdd:TIGR02868 393 TLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARL 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 478 SVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRL 535
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
273-573 |
3.97e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 210.09 E-value: 3.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 273 FSASGTIEVGVLYAFISYLGRLN------------------------EPLIELTTQQAMLQQAVVAGERVFELMDGPRQQ 328
Cdd:PRK11174 255 FFASISIALVAVYFGFSYLGELNfghygtgvtlfagffvlilapefyQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAH 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 329 YGNDDRPLQSG---TIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLtEGEIRLDGRPL 405
Cdd:PRK11174 335 PQQGEKELASNdpvTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIEL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 406 SSLSHSALRQGVAMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQL 484
Cdd:PRK11174 414 RELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNpDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQR 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 485 LALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAA 564
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQA 573
|
....*....
gi 447178945 565 QGRYWQMYQ 573
Cdd:PRK11174 574 GGLFATLLA 582
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-571 |
1.50e-59 |
|
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: 215.19 E-value: 1.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVVAGLAAAYVGLQLFAAglhYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:TIGR00957 968 FLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGILQGFAV---FGYSMAVSIGGIQASRVLHQDL 1044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSA-ALVGAMLVAMFSldwrMALVAIMIFPVVLVVMV 183
Cdd:TIGR00957 1045 LHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLfNVIGALIVILLA----TPIAAVIIPPLGLLYFF 1120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 184 IyQRYSTPIVRRVR----AYLADINDGFNEIINGMSVIQQFRQQARF----GERMGEASRSHYMA----RMQTLRLDgfl 251
Cdd:TIGR00957 1121 V-QRFYVASSRQLKrlesVSRSPVYSHFNETLLGVSVIRAFEEQERFihqsDLKVDENQKAYYPSivanRWLAVRLE--- 1196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 252 lrpllslfsSLILCGLLM--LFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERVFEL----MDGP 325
Cdd:TIGR00957 1197 ---------CVGNCIVLFaaLFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYseteKEAP 1267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 326 RQQYGNddRPL----QSGTIEVDNVSFAYRDD-NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL 400
Cdd:TIGR00957 1268 WQIQET--APPsgwpPRGRVEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 401 DGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVG 480
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVG 1425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 481 QKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQ 560
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSN 1505
|
570
....*....|.
gi 447178945 561 LLAAQGRYWQM 571
Cdd:TIGR00957 1506 LLQQRGIFYSM 1516
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
341-575 |
4.90e-59 |
|
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: 196.94 E-value: 4.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYR-DDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAM 419
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLADTFLANVTLGRD-ISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQIL 498
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 499 ILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
339-556 |
2.92e-58 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 194.35 E-value: 2.92e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 339 GTIEVDNVSFAYRDD-NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGV 417
Cdd:cd03245 1 GRIEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQ 496
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGApLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 497 ILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQG 556
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
339-551 |
6.24e-57 |
|
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: 191.14 E-value: 6.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 339 GTIEVDNVSFAY--RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQG 416
Cdd:cd03248 10 GIVKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 417 VAMVQQDPVVLADTFLANVTLG-RDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETP 495
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 496 QILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQ 551
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
29-575 |
1.08e-56 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 200.32 E-value: 1.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 29 VLMMWVAAAAEVSGPLLISYFIDNMVAKNnlplkVVAGLAAAYVGLQLFAA----GLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:PRK10789 1 VALLIIIAMLQLIPPKVVGIIVDGVTEQH-----MTTGQILMWIGTMVLIAvvvyLLRYVWRVLLFGASYQLAVELREDF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFS-LDWRMALVAIMIFPVVLVVMv 183
Cdd:PRK10789 76 YRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTqISWQLTLLALLPMPVMAIMI- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 184 iyQRYSTPIVRRVR---AYLADINDGFNEIINGMSVIQQF----RQQARFGERMGEASRSH-YMARMQTlRLDGFLLRPL 255
Cdd:PRK10789 155 --KRYGDQLHERFKlaqAAFSSLNDRTQESLTSIRMIKAFgledRQSALFAADAEDTGKKNmRVARIDA-RFDPTIYIAI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 256 LSLFSSLILCGLLMLFgfsaSGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERVFELMD-GPRQQYGNDDR 334
Cdd:PRK10789 232 GMANLLAIGGGSWMVV----NGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAeAPVVKDGSEPV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 335 PLQSGTIEVDNVSFAY-RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAL 413
Cdd:PRK10789 308 PEGRGELDVNIRQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQGVAMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLV 492
Cdd:PRK10789 388 RSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALL 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 493 ETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY 572
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMY 547
|
...
gi 447178945 573 QLQ 575
Cdd:PRK10789 548 RYQ 550
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
122-573 |
1.17e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 200.44 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 122 GQVISRVTNDTEVIRDLYVTVVATVLrsAALVGAMLVAMFS--LDWRMALV--AIMIFPVVLVVMVIYqRYSTPIVRRVR 197
Cdd:PRK11160 117 GDLLNRLVADVDTLDHLYLRLISPLV--AALVVILVLTIGLsfFDLTLALTlgGILLLLLLLLPLLFY-RLGKKPGQDLT 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 198 AYLADINDGFNEIINGMSVIQQFRQQARFGERMgEASRSHYMARMQTL-RLDGFLLrpllslfsslilcGLLMLfgfsAS 276
Cdd:PRK11160 194 HLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQL-EQTEQQWLAAQRRQaNLTGLSQ-------------ALMIL----AN 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 277 GTIEVGVLYAFISYLGRLNEP--LIELTTQQAM---------------LQQAVVAGERVFELMDG-PRQQY-GNDDRPLQ 337
Cdd:PRK11160 256 GLTVVLMLWLAAGGVGGNAQPgaLIALFVFAALaafealmpvagafqhLGQVIASARRINEITEQkPEVTFpTTSTAAAD 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 338 SGTIEVDNVSFAYRDDNL-VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQG 416
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 417 VAMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSmSDGIYTPLGEQGNNLSVGQKQLLALARVLVETP 495
Cdd:PRK11160 416 ISVVSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDA 494
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 496 QILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-589 |
1.83e-55 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 197.49 E-value: 1.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEvsgPLLISYFIDNMVAKNNlplkvVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:PRK13657 24 LAVANVLLAAATFAE---PILFGRIIDAISGKGD-----IFPLLAAWAGFGLFNIIAGVLVARHADRLAHRRRLAVLTEY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVI--------RDLYVTVVATVLrsaalvgaMLVAMFSLDWRMALVAImifp 176
Cdd:PRK13657 96 FERIIQLPLAWHSQRGSGRALHTLLRGTDALfglwlefmREHLATLVALVV--------LLPLALFMNWRLSLVLV---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 177 vvlVVMVIYQRYSTPIVRR-------VRAYLADINDGFNEIINGMSVIQQF-RQQArfgermgEASRSHYMAR----MQT 244
Cdd:PRK13657 164 ---VLGIVYTLITTLVMRKtkdgqaaVEEHYHDLFAHVSDAIGNVSVVQSYnRIEA-------ETQALRDIADnllaAQM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 245 LRLD--GFLLRPLLSLFSSLILCGLLMLFGFSASGTIEVGVLYAFISY----LGRLNEP---LIELTTQQAMLQQavvag 315
Cdd:PRK13657 234 PVLSwwALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFatllIGRLDQVvafINQVFMAAPKLEE----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 316 erVFELMDG-PRQQYGNDDRPLQ--SGTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYP 392
Cdd:PRK13657 309 --FFEVEDAvPDVRDPPGAIDLGrvKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 393 LTEGEIRLDGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIYTPLG 471
Cdd:PRK13657 387 PQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRpDATDEEMRAAAERAQAHDFIERKPDGYDTVVG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 472 EQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQ 551
Cdd:PRK13657 467 ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGR 546
|
570 580 590
....*....|....*....|....*....|....*....
gi 447178945 552 AVEQGTHQQLLAAQGRYWQMYQLQ-LAGEELAASVREEE 589
Cdd:PRK13657 547 VVESGSFDELVARGGRFAALLRAQgMLQEDERRKQPAAE 585
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
341-563 |
4.23e-55 |
|
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: 186.38 E-value: 4.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMV 420
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDP-------VVLAD-TF-LANVTLGRDISEERVWQALETVQLAELA-RSMSDgiytplgeqgnnLSVGQKQLLALARV 490
Cdd:COG1122 81 FQNPddqlfapTVEEDvAFgPENLGLPREEIRERVEEALELVGLEHLAdRPPHE------------LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447178945 491 LVETPQILILDEATASIDSGTEQAIQHALAAV-REHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLA 563
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
25-318 |
7.80e-54 |
|
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: 185.06 E-value: 7.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLkvVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSL--LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVI 184
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 185 YQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFllrpLLSLFSSLIL 264
Cdd:cd07346 159 FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSAL----FSPLIGLLTA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 265 CGLLMLFGFSAS----GTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd07346 235 LGTALVLLYGGYlvlqGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
25-318 |
1.07e-49 |
|
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: 173.83 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPlkVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLG--VLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVI 184
Cdd:cd18546 79 FAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 185 YQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSLIL 264
Cdd:cd18546 159 FRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447178945 265 CGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18546 239 AVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
40-566 |
2.05e-49 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 185.18 E-value: 2.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 40 VSGPLLISYFIDNMVAKNNLP--LKVVAGLaaayvgLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFD 117
Cdd:PLN03232 929 VSSSTWLSIWTDQSTPKSYSPgfYIVVYAL------LGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFH 1002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 118 TQPVGQVISRVTNDT-EVIRD------LYVTVVATVLRSAALVGamLVAMFSLdWrmalvAIMIFPVVLVVMVIYQRYST 190
Cdd:PLN03232 1003 TNPTGRVINRFSKDIgDIDRNvanlmnMFMNQLWQLLSTFALIG--TVSTISL-W-----AIMPLLILFYAAYLYYQSTS 1074
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 191 PIVRRVRAYL-ADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSLILcgLLM 269
Cdd:PLN03232 1075 REVRRLDSVTrSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIW--LTA 1152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 270 LFGFSASGTIEVGVLYA-----FISYLGRLNEPLIELTTQQAMLQQAVVAGERVFELMDGPRQQYG--NDDRPLQS---- 338
Cdd:PLN03232 1153 TFAVLRNGNAENQAGFAstmglLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAiiENNRPVSGwpsr 1232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 339 GTIEVDNVSFAYRDD-NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGV 417
Cdd:PLN03232 1233 GSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVL 1312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQI 497
Cdd:PLN03232 1313 SIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKI 1392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 498 LILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQG 566
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
25-318 |
1.92e-48 |
|
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: 170.73 E-value: 1.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLkvVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSG--LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVI 184
Cdd:cd18545 80 FSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 185 YQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSLIl 264
Cdd:cd18545 160 LRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGT- 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 265 cGLLMLFG--FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18545 239 -ALVYWYGgkLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
337-557 |
9.77e-48 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 165.66 E-value: 9.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 337 QSGTIEVDNVSFAYRDD-NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQ 415
Cdd:cd03369 3 EHGEIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 416 GVAMVQQDPVVLADTFLANVTLGRDISEERVWQALEtvqlaelarsmsdgiytpLGEQGNNLSVGQKQLLALARVLVETP 495
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447178945 496 QILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGT 557
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
342-551 |
3.54e-47 |
|
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: 164.56 E-value: 3.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 342 EVDNVSFAYRDDN-LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMV 420
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPvvlaDTFLANVTLGRDIS-------------EERVWQALETVQLAELA-RSmsdgIYTplgeqgnnLSVGQKQLLA 486
Cdd:cd03225 81 FQNP----DDQFFGPTVEEEVAfglenlglpeeeiEERVEEALELVGLEGLRdRS----PFT--------LSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 487 LARVLVETPQILILDEATASIDSGTEQAIQHALAAV-REHTTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
98-566 |
3.02e-45 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 172.62 E-value: 3.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 98 QQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDT-------EVIRDLYVTVVATVLRSAALVGamLVAMFSLdWrmalv 170
Cdd:PLN03130 986 KRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLgdidrnvAVFVNMFLGQIFQLLSTFVLIG--IVSTISL-W----- 1057
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 171 AIMIFPVVLVVMVIYQRYSTPIVRRVRAYL-ADINDGFNEIINGMSVIQQFRQQARFGERMGEA------------SRSH 237
Cdd:PLN03130 1058 AIMPLLVLFYGAYLYYQSTAREVKRLDSITrSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSmdnnirftlvnmSSNR 1137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 238 YMA-RMQTLrldgfllrpllslfsslilcGLLMLF---GFSASGTIEVGVLYAFISYLGRLNEPLIELTT-QQAMLQQAV 312
Cdd:PLN03130 1138 WLAiRLETL--------------------GGLMIWltaSFAVMQNGRAENQAAFASTMGLLLSYALNITSlLTAVLRLAS 1197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 313 VAG------ERVFELMDGPRQQ--YGNDDRPL----QSGTIEVDNVSFAYRDD-NLVLKNINLSVPSRNFVALVGHTGSG 379
Cdd:PLN03130 1198 LAEnslnavERVGTYIDLPSEAplVIENNRPPpgwpSSGSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAG 1277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 380 KSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGRDISEERVWQALETVQLAELA 459
Cdd:PLN03130 1278 KSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVI 1357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 460 RSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIV 539
Cdd:PLN03130 1358 RRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTII 1437
|
490 500
....*....|....*....|....*..
gi 447178945 540 DADTILVLHRGQAVEQGTHQQLLAAQG 566
Cdd:PLN03130 1438 DCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
72-564 |
4.54e-45 |
|
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: 168.00 E-value: 4.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 72 VGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPvgqvisrvtndTEVIRDLyvTVVATVLRSAA 151
Cdd:COG4618 67 LGLYAVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRAALRGGGGAA-----------AQALRDL--DTLRQFLTGPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 152 LVGAM--------LVAMFSLDWRMALVAImIFPVVLVVMVIYQRYST-PIVRRVRAYLADINDGFN------EIINGMSV 216
Cdd:COG4618 134 LFALFdlpwapifLAVLFLFHPLLGLLAL-VGALVLVALALLNERLTrKPLKEANEAAIRANAFAEaalrnaEVIEAMGM 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 217 IQQFRQqaRFGERMGEASRSH---------YMARMQTLRLdgfllrpllslfsslilcGL--LMLfGFSA----SGTIEV 281
Cdd:COG4618 213 LPALRR--RWQRANARALALQarasdraggFSALSKFLRL------------------LLqsAVL-GLGAylviQGEITP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 282 GVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERVFELMdgprQQYGNDDRPLQ----SGTIEVDNVSFAY-RDDNLV 356
Cdd:COG4618 272 GAMIAASILMGRALAPIEQAIGGWKQFVSARQAYRRLNELL----AAVPAEPERMPlprpKGRLSVENLTVVPpGSKRPI 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVT 436
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 437 LGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQ 516
Cdd:COG4618 428 RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALA 507
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 447178945 517 HALAAVREH-TTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAA 564
Cdd:COG4618 508 AAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
339-565 |
1.98e-44 |
|
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: 158.53 E-value: 1.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 339 GTIEVDNVSFAYrDDNL--VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQG 416
Cdd:cd03288 18 GEIKIHDLCVRY-ENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 417 VAMVQQDPVVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQ 496
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 497 ILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQ 565
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-318 |
1.02e-42 |
|
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: 155.36 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNL-------------PLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNR 91
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLpgllglapllgpdPLALLLLAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 92 AAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVA 171
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 172 IMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLdgfl 251
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARL---- 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447178945 252 LRPLLSLFSSLILCGLLMLFGFSA----SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18564 237 QALLSPVVDVLVAVGTALVLWFGAwlvlAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
341-552 |
1.41e-42 |
|
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: 150.83 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDN-LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAM 419
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLADTflanvtlgrdiseervwqaletvqLAElarsmsdgiytplgeqgNNLSVGQKQLLALARVLVETPQILI 499
Cdd:cd03246 81 LPQDDELFSGS------------------------IAE-----------------NILSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447178945 500 LDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVDADTILVLHRGQA 552
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAgATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
27-318 |
2.77e-42 |
|
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: 153.74 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 27 IAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLkvVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMD 106
Cdd:cd18542 3 LAILALLLATALNLLIPLLIRRIIDSVIGGGLREL--LWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 107 AALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQ 186
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 187 RYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSLIlcG 266
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQI--V 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447178945 267 LLMLFG--FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18542 239 LVLWVGgyLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
341-563 |
5.48e-42 |
|
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: 152.20 E-value: 5.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRD-DNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrpLSSLSHSAL---RQG 416
Cdd:TIGR04520 1 IEVENVSFSYPEsEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLweiRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 417 VAMVQQDP-------VVLAD-TF-LANVTLGRDISEERVWQALETVQLAELARsmsdgiYTPlgeqgNNLSVGQKQLLAL 487
Cdd:TIGR04520 79 VGMVFQNPdnqfvgaTVEDDvAFgLENLGVPREEMRKRVDEALKLVGMEDFRD------REP-----HLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 488 ARVLVETPQILILDEATASIDSGTEQAIqhaLAAVR-----EHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLL 562
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEV---LETIRklnkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIF 224
|
.
gi 447178945 563 A 563
Cdd:TIGR04520 225 S 225
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
25-318 |
1.09e-41 |
|
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: 152.19 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLplKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDL--EALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVI 184
Cdd:cd18552 79 FDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 185 YQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSLIl 264
Cdd:cd18552 159 IGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAI- 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 265 cGLLMLFG--FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18552 238 -ALVLWYGgyQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
25-318 |
1.15e-41 |
|
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: 152.17 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKV----VAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQL 100
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVdfsgLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 101 RTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLV 180
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 181 VMVIYQRYSTPIVRRVRAYLADINdGF-NEIINGMSVIQQFRQQARFGERMGE--------ASRSHYMAR--MQTLRLDG 249
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELN-GYiEEMISGQKVVKAFNREEEAIEEFDEineelykaSFKAQFYSGllMPIMNFIN 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447178945 250 FLLRPllslfsslilcgLLMLFG--FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18547 240 NLGYV------------LVAVVGglLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
341-591 |
3.27e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 153.52 E-value: 3.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRD-DNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLT---EGEIRLDGRPLSSLSHSALRQG 416
Cdd:COG1123 5 LEVRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 417 VAMVQQDPvvlaDTFLANVTLGRDISE-------------ERVWQALETVQLAELARSmsdgiYTplgeqgNNLSVGQKQ 483
Cdd:COG1123 85 IGMVFQDP----MTQLNPVTVGDQIAEalenlglsraearARVLELLEAVGLERRLDR-----YP------HQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 484 LLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREH--TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQ 560
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEE 229
|
250 260 270
....*....|....*....|....*....|.
gi 447178945 561 LLAAQGRYWQMYQLQLAGEELAASVREEESL 591
Cdd:COG1123 230 ILAAPQALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
311-561 |
4.29e-39 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 154.17 E-value: 4.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 311 AVVAGERVFElmdgPRQQYGNDDRPLQSGTIEVDNVSFAYRDD-NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMG 389
Cdd:PTZ00243 1283 ADVTGTVVIE----PASPTSAAPHPVQAGSLVFEGVQMRYREGlPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMR 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 390 YYPLTEGEIRLDGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYTP 469
Cdd:PTZ00243 1359 MVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSR 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 470 LGEQGNNLSVGQKQLLALARVLVETPQILIL-DEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLH 548
Cdd:PTZ00243 1439 VLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMD 1518
|
250
....*....|...
gi 447178945 549 RGQAVEQGTHQQL 561
Cdd:PTZ00243 1519 HGAVAEMGSPREL 1531
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
341-562 |
4.55e-39 |
|
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: 143.65 E-value: 4.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMV 420
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVVLAD-TFLANVTLGR-----------DISEERVWQALETVQLAELA-RSMsdgiytplgeqgNNLSVGQKQLLAL 487
Cdd:COG1120 81 PQEPPAPFGlTVRELVALGRyphlglfgrpsAEDREAVEEALERTGLEHLAdRPV------------DELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 488 ARVLVETPQILILDEATASIDsgteqaIQH---------ALAAVREHTTLVVI-----AHRLstivdADTILVLHRGQAV 553
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLD------LAHqlevlellrRLARERGRTVVMVLhdlnlAARY-----ADRLVLLKDGRIV 217
|
....*....
gi 447178945 554 EQGTHQQLL 562
Cdd:COG1120 218 AQGPPEEVL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
290-564 |
5.82e-39 |
|
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: 150.05 E-value: 5.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 290 YLGRLNEpliELTTQQAMLQQAVVAGERVFELMDGPRQQYGNDDRPLqsgtIEVDNVSFAY----RDDNLVLKNINLSVP 365
Cdd:COG1123 217 DDGRIVE---DGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPL----LEVRNLSKRYpvrgKGGVRAVDDVSLTLR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 366 SRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---ALRQGVAMVQQDPvvlADTFLANVTLGRDIS 442
Cdd:COG1123 290 RGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRRRVQMVFQDP---YSSLNPRMTVGDIIA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 443 E--------------ERVWQALETVQLAELARSMSdgiytPlgeqgNNLSVGQKQLLALARVLVETPQILILDEATASID 508
Cdd:COG1123 367 EplrlhgllsraerrERVAELLERVGLPPDLADRY-----P-----HELSGGQRQRVAIARALALEPKLLILDEPTSALD 436
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 509 SGTEQAIQHALAAVRE--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLAA 564
Cdd:COG1123 437 VSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
341-551 |
7.49e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.88 E-value: 7.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMV 420
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVVLADTFLANVTL-----GRDISEERVWQALETVQLAELArsmsdgiytpLGEQGNNLSVGQKQLLALARVLVETP 495
Cdd:COG4619 80 PQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDI----------LDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447178945 496 QILILDEATASIDSGTEQAIQHALAAVREH--TTLVVIAH------RLstivdADTILVLHRGQ 551
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSHdpeqieRV-----ADRVLTLEAGR 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
341-565 |
1.47e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsslshSALRQGVAMV 420
Cdd:COG1121 7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVVLADtFLAN----VTLGRD-----------ISEERVWQALETVQLAELARsmsdgiyTPLGEqgnnLSVGQKQLL 485
Cdd:COG1121 81 PQRAEVDWD-FPITvrdvVLMGRYgrrglfrrpsrADREAVDEALERVGLEDLAD-------RPIGE----LSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 486 ALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQaVEQGTHQQLLA 563
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREyFDRVLLLNRGL-VAHGPPEEVLT 227
|
..
gi 447178945 564 AQ 565
Cdd:COG1121 228 PE 229
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
341-564 |
1.81e-37 |
|
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: 139.17 E-value: 1.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYR---DDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGV 417
Cdd:COG1124 2 LEVRNLSVSYGqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDP-----------VVLADTFLAnvtLGRDISEERVWQALETVQLAE--LARSMSDgiytplgeqgnnLSVGQKQL 484
Cdd:COG1124 82 QMVFQDPyaslhprhtvdRILAEPLRI---HGLPDREERIAELLEQVGLPPsfLDRYPHQ------------LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 485 LALARVLVETPQILILDEATASIDSGTEQAIQHALAAVRE--HTTLVVIAHRLStIVD--ADTILVLHRGQAVEQGTHQQ 560
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVAD 225
|
....
gi 447178945 561 LLAA 564
Cdd:COG1124 226 LLAG 229
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-318 |
2.05e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 140.36 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDN-MVAKNNLP--LKVVAGLAAAYVGLQLFAaglhYAQSLLFNRAAVGVVQQLR 101
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLvTIGSKSLGllLGLALLLLGAYLLRALLN----FLRIYLNHVAEQKVVADLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 102 TDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVV 181
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 182 MVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFllrpLLSLFSS 261
Cdd:cd18778 157 AWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAI----FHPLMEF 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447178945 262 LILCGLLMLFGFSA----SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18778 233 LTSLGTVLVLGFGGrlvlAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
341-561 |
2.26e-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: 138.47 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNlVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPL-----TEGEIRLDGRPLSSLSHS--AL 413
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQGVAMVQQDPVVLADTFLANVTLG--------RDISEERVWQALETVQL-AELARSMSdgiytplgeqGNNLSVGQKQL 484
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiklKEELDERVEEALRKAALwDEVKDRLH----------ALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 485 LALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAH------RLstivdADTILVLHRGQAVEQGTH 558
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFGPT 224
|
...
gi 447178945 559 QQL 561
Cdd:cd03260 225 EQI 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
341-554 |
6.13e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.11 E-value: 6.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSA---LRQGV 417
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVVLAD-TFLANVTL-----GRDISE--ERVWQALETVQLAELARSMsdgiytPlgeqgNNLSVGQKQLLALAR 489
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALplrvtGKSRKEirRRVREVLDLVGLSDKAKAL------P-----HELSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 490 VLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIA-HRLStIVDA--DTILVLHRGQAVE 554
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLE-LVDRmpKRVLELEDGRLVR 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
342-550 |
2.18e-36 |
|
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: 134.97 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 342 EVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSalrqgVAMVQ 421
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 422 QDPVVLAD---TFLANVTLGRD-----------ISEERVWQALETVQLAELARSmsdgiytPLGEqgnnLSVGQKQLLAL 487
Cdd:cd03235 75 QRRSIDRDfpiSVRDVVLMGLYghkglfrrlskADKAKVDEALERVGLSELADR-------QIGE----LSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447178945 488 ARVLVETPQILILDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRG 550
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
357-505 |
3.26e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.39 E-value: 3.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMVQQDPVVLAD-TFLANV 435
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 436 TLGRDI-------SEERVWQALETVqlaelarSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATA 505
Cdd:pfam00005 81 RLGLLLkglskreKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
25-298 |
6.73e-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: 135.85 E-value: 6.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVI 184
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 185 YQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSLIL 264
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 447178945 265 CGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPL 298
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-318 |
1.24e-35 |
|
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: 135.72 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDN--MVAKNNLPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRT 102
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDvlIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 103 DVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVM 182
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 183 VIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMqtlRLDGFLLRPLLSLFSSL 262
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANI---RAEKLWATFFPLLTFLT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 263 ILCGLLML-FG--FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18563 238 SLGTLIVWyFGgrQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
341-551 |
2.03e-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: 132.21 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDD----NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshsalrqg 416
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 417 VAMVQQDPVVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQ 496
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 497 ILILDEATASIDSGT-----EQAIQHALAAVRehtTLVVIAHRLSTIVDADTILVLHRGQ 551
Cdd:cd03250 148 IYLLDDPLSAVDAHVgrhifENCILGLLLNNK---TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
342-556 |
3.79e-35 |
|
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: 130.63 E-value: 3.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 342 EVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMvq 421
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 422 qdpvvladtflanvtlgrdiseerVWQALETVQLAELA-RSMsdgiytplgeqgNNLSVGQKQLLALARVLVETPQILIL 500
Cdd:cd03214 78 ------------------------VPQALELLGLAHLAdRPF------------NELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447178945 501 DEATASIDSGTEQAIQ---HALAAVREHTTLVVI-----AHRLstivdADTILVLHRGQAVEQG 556
Cdd:cd03214 122 DEPTSHLDIAHQIELLellRRLARERGKTVVMVLhdlnlAARY-----ADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
341-563 |
1.68e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 132.06 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRD-DNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAM 419
Cdd:PRK13635 6 IRVEHISFRYPDaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDP------------VVLAdtfLANVTLGRDISEERVWQALETVQLAELARsmsdgiytplgEQGNNLSVGQKQLLAL 487
Cdd:PRK13635 86 VFQNPdnqfvgatvqddVAFG---LENIGVPREEMVERVDQALRQVGMEDFLN-----------REPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 488 ARVLVETPQILILDEATASIDSgteQAIQHALAAVRE-----HTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLL 562
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDP---RGRREVLETVRQlkeqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
.
gi 447178945 563 A 563
Cdd:PRK13635 229 K 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
341-556 |
2.06e-34 |
|
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: 128.58 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDN-LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShSALRQGVAM 419
Cdd:cd03247 1 LSINNVSFSYPEQEqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLADTFLANVtlgrdiseervwqaletvqlaelarsmsdgiytplgeqGNNLSVGQKQLLALARVLVETPQILI 499
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 500 LDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQG 556
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
269-572 |
4.31e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 139.01 E-value: 4.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 269 MLFGFSAS-------------------GTIEVG----VLYAFI---SYLGRLneplielTTQQAMLQQAVVAGERVFELM 322
Cdd:PTZ00265 1068 MLWGFSQSaqlfinsfaywfgsflirrGTILVDdfmkSLFTFLftgSYAGKL-------MSLKGDSENAKLSFEKYYPLI 1140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 323 -----------DGPRQQYGNDDRplqsGTIEVDNVSFAY--RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMG 389
Cdd:PTZ00265 1141 irksnidvrdnGGIRIKNKNDIK----GKIEIMDVNFRYisRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMR 1216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 390 YYPL------------------------------------------------------TEGEIRLDGRPLSSLSHSALRQ 415
Cdd:PTZ00265 1217 FYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRN 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 416 GVAMVQQDPVVLADTFLANVTLGR-DISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVET 494
Cdd:PTZ00265 1297 LFSIVSQEPMLFNMSIYENIKFGKeDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLRE 1376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 495 PQILILDEATASIDSGTEQAIQHALAAVREHT--TLVVIAHRLSTIVDADTILVLHR----GQAVE-QGTHQQLLAAQGR 567
Cdd:PTZ00265 1377 PKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQDG 1456
|
....*
gi 447178945 568 YWQMY 572
Cdd:PTZ00265 1457 VYKKY 1461
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
341-549 |
4.43e-34 |
|
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: 128.74 E-value: 4.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDN---LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSalrqgV 417
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVVLA-DTFLANVTLG-------RDISEERVWQALETVQLAELARSMsdgiytPlgeqgNNLSVGQKQLLALAR 489
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqgvpKAEARERAEELLELVGLSGFENAY------P-----HQLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 490 VLVETPQILILDEATASIDSGTEQAIQHALAAV--REHTTLVVIAHRLS-TIVDADTILVLHR 549
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
341-556 |
1.03e-33 |
|
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: 128.01 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNL---VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS---HSALR 414
Cdd:cd03257 2 LEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 415 QGVAMVQQDPV-----------VLADTFLANVTL-GRDISEERVWQALETVQLAE-LARSMsdgiytPlgeqgNNLSVGQ 481
Cdd:cd03257 82 KEIQMVFQDPMsslnprmtigeQIAEPLRIHGKLsKKEARKEAVLLLLVGVGLPEeVLNRY------P-----HELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 482 KQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREH--TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElgLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
341-561 |
1.13e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 129.49 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDN-LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAM 419
Cdd:PRK13648 8 IVFKNVSFQYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDP-------VVLADTF--LANVTLGRDISEERVWQALETVQLAELARSmsdgiytplgeQGNNLSVGQKQLLALARV 490
Cdd:PRK13648 88 VFQNPdnqfvgsIVKYDVAfgLENHAVPYDEMHRRVSEALKQVDMLERADY-----------EPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 491 LVETPQILILDEATASIDSGTEQAIQHALAAVRE--HTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQL 561
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
341-566 |
1.15e-33 |
|
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: 129.49 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDD----NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS---LSHSAL 413
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQGVAMVQQDP-------VVLADtfLA----NVTLGRDISEERVWQALETVQLAE--LARSmsdgiytPLgeqgnNLSVG 480
Cdd:TIGR04521 81 RKKVGLVFQFPehqlfeeTVYKD--IAfgpkNLGLSEEEAEERVKEALELVGLDEeyLERS-------PF-----ELSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 481 QKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVR--EHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGT 557
Cdd:TIGR04521 147 QMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkeKGLTVILVTHSMEDVAEyADRVIVMHKGKIVLDGT 226
|
250
....*....|....*
gi 447178945 558 ------HQQLLAAQG 566
Cdd:TIGR04521 227 prevfsDVDELEKIG 241
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
335-562 |
1.26e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 129.34 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 335 PLQSGTIEVDNVSFAYRDD-NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAL 413
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQGVAMVQQDP-------VVLAD-TF-LANvtlgRDISEERVWQALEtvqlaELARSMsdGIYTPLGEQGNNLSVGQKQL 484
Cdd:PRK13632 82 RKKIGIIFQNPdnqfigaTVEDDiAFgLEN----KKVPPKKMKDIID-----DLAKKV--GMEDYLDKEPQNLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 485 LALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHT--TLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLL 562
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
342-551 |
2.78e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 124.66 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 342 EVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMVQ 421
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 422 QdpvvladtflanvtlgrdiseervwqaletvqlaelarsmsdgiytplgeqgnnLSVGQKQLLALARVLVETPQILILD 501
Cdd:cd00267 80 Q------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447178945 502 EATASIDSGTEQAIQHALAA-VREHTTLVVIAHRLSTIVDA-DTILVLHRGQ 551
Cdd:cd00267 106 EPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
25-318 |
6.44e-33 |
|
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: 127.93 E-value: 6.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNnlplkVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGG-----SSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVI 184
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 185 YQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSLil 264
Cdd:cd18551 156 LGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLA-- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 265 cgLLMLFGFS----ASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18551 234 --LLVVLGVGgarvASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
341-550 |
1.40e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 125.97 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDN---LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSalrqgV 417
Cdd:COG1116 8 LELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVVLA-DTFLANVTLGRDIS-------EERVWQALETVQLAELARSMsdgiytPlgeqgNNLSVGQKQLLALAR 489
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRgvpkaerRERARELLELVGLAGFEDAY------P-----HQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 490 VLVETPQILILDEATASIDSGTEQAIQHALAAV--REHTTLVVIAH------RLstivdADTILVLHRG 550
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHdvdeavFL-----ADRVVVLSAR 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
341-551 |
1.77e-32 |
|
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: 124.52 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNL---VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAL---- 413
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQGVAMVQQDPVVLAD-TFLANVTLGRDIS-------EERVWQALETVQLAELARSMsdgiytPlgeqgNNLSVGQKQLL 485
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLLAgvpkkerRERAEELLERVGLGDRLNHY------P-----SELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 486 ALARVLVETPQILILDEATASIDSGTEQAIQHALAAVRE--HTTLVVIAHRLSTIVDADTILVLHRGQ 551
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-502 |
2.05e-32 |
|
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: 131.46 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 13 RLLAYGSPWrkPLGIAVLMmwvAAAAEVSGPLLIsYFIDNMVAKnnlPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRA 92
Cdd:COG4615 5 RLLLRESRW--LLLLALLL---GLLSGLANAGLI-ALINQALNA---TGAALARLLLLFAGLLVLLLLSRLASQLLLTRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 93 AVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVtVVATVLRSAALVGAMLVAMFSLDWRMALVAI 172
Cdd:COG4615 76 GQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-RLPELLQSVALVLGCLAYLAWLSPPLFLLTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 173 mifpVVLVVMVIYQRYStpiVRRVRAYLA--------------DINDGFNEI-INGMsviqqfRQQARFGERMGEASRsh 237
Cdd:COG4615 155 ----VLLGLGVAGYRLL---VRRARRHLRrareaedrlfkhfrALLEGFKELkLNRR------RRRAFFDEDLQPTAE-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 238 ymaRMQTLRLDGFLLRPLLSLFSSLILCGL--LMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAG 315
Cdd:COG4615 220 ---RYRDLRIRADTIFALANNWGNLLFFALigLILFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVAL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 316 ERVFEL---MDGPRQQYGNDDRPLQSG---TIEVDNVSFAYRDDN----LVLKNINLSVPSRNFVALVGHTGSGKSTLAS 385
Cdd:COG4615 297 RKIEELelaLAAAEPAAADAAAPPAPAdfqTLELRGVTYRYPGEDgdegFTLGPIDLTIRRGELVFIVGGNGSGKSTLAK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 386 LLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAmvqqdpVVLADTFLANVTLGRD--ISEERVWQALETVQLAELArSMS 463
Cdd:COG4615 377 LLTGLYRPESGEILLDGQPVTADNREAYRQLFS------AVFSDFHLFDRLLGLDgeADPARARELLERLELDHKV-SVE 449
|
490 500 510
....*....|....*....|....*....|....*....
gi 447178945 464 DGIYTPLgeqgnNLSVGQKQLLALARVLVETPQILILDE 502
Cdd:COG4615 450 DGRFSTT-----DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
341-555 |
4.22e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 123.61 E-value: 4.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNL---VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAL---- 413
Cdd:COG1136 5 LELRNLTKSYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQGVAMVQQDPVVLAD-TFLANVTL-------GRDISEERVWQALETVQLAELARSMsdgiytPlgeqgNNLSVGQKQLL 485
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALplllagvSRKERRERARELLERVGLGDRLDHR------P-----SQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447178945 486 ALARVLVETPQILILDEATASIDSGTEQAIQHALAA-VREH-TTLVVIAHRLSTIVDADTILVLHRGQAVEQ 555
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
22-318 |
5.97e-32 |
|
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: 125.28 E-value: 5.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 22 RKPLGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLplKVVAGLAAAYVGLQLFAAGLHYaqslLFNRAA----VGVV 97
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTL--DGLTGFILLYLGLILIQALSVF----LFIRLAgkieMGVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 98 QQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPV 177
Cdd:cd18540 75 YDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 178 VLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLS 257
Cdd:cd18540 155 LAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLF 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 258 LFSSLIlcGLLMLFG--FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18540 235 LGSIAT--ALVLWYGgiLVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
341-564 |
7.29e-32 |
|
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: 123.07 E-value: 7.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNL---VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAL---R 414
Cdd:cd03258 2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 415 QGVAMV-QQDPVVLADTFLANVTL-------GRDISEERVWQALETVQLAELARSmsdgiYtPlgeqgNNLSVGQKQLLA 486
Cdd:cd03258 82 RRIGMIfQHFNLLSSRTVFENVALpleiagvPKAEIEERVLELLELVGLEDKADA-----Y-P-----AQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 487 LARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHT--TLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLA 563
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 447178945 564 A 564
Cdd:cd03258 231 N 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
341-553 |
4.15e-31 |
|
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: 118.69 E-value: 4.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSALRQGVAM 419
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQdpvvladtflanvtlgrdiseervwqaletvqlaelarsmsdgiytplgeqgnnLSVGQKQLLALARVLVETPQILI 499
Cdd:cd03216 80 VYQ------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 500 LDEATASIdsgTEQAIQHALAAVR----EHTTLVVIAHRLSTIVD-ADTILVLHRGQAV 553
Cdd:cd03216 106 LDEPTAAL---TPAEVERLFKVIRrlraQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
25-318 |
1.32e-30 |
|
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: 121.44 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLkvVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSA--LWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLyVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVI 184
Cdd:cd18543 79 FAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRF-LAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 185 YQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSLIL 264
Cdd:cd18543 158 FRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 447178945 265 cGLLMLFGFSA-SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18543 238 -AVLALGGWLVaNGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
341-551 |
1.41e-30 |
|
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: 117.50 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDdNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQgVAMV 420
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPvvladTFLANVTlgrdiseerVWQALEtvqlaelarsmsdgiytplgeqgnnLSVGQKQLLALARVLVETPQILIL 500
Cdd:cd03230 79 PEEP-----SLYENLT---------VRENLK-------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447178945 501 DEATASIDSGTEQAIQHALAA-VREHTTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGR 172
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
341-544 |
3.62e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 117.58 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAyRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSALRQGVAMV 420
Cdd:COG4133 3 LEAENLSCR-RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 -QQDPVVLADTFLANVTL-----GRDISEERVWQALETVQLAELARsmsdgiyTPLGeqgnNLSVGQKQLLALARVLVET 494
Cdd:COG4133 81 gHADGLKPELTVRENLRFwaalyGLRADREAIDEALEAVGLAGLAD-------LPVR----QLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447178945 495 PQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIA-HRLSTIVDADTI 544
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
71-562 |
4.22e-30 |
|
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: 126.56 E-value: 4.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 71 YVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLY-VTVVATVLRS 149
Cdd:TIGR01271 931 YVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLpLTLFDFIQLT 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 150 AALVGAMLVAmfSLDWRMALVAIMIFPVVLVVMVIYQRYSTPIVRRVRAylADINDGFNEII---NGMSVIQQFRQQARF 226
Cdd:TIGR01271 1011 LIVLGAIFVV--SVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLES--EARSPIFSHLItslKGLWTIRAFGRQSYF 1086
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 227 GERMGEASRSH---YMARMQTLRLDGFLlrpllslfsslilCGLLMLFGFSASGTI----------EVGVLYAFISylgr 293
Cdd:TIGR01271 1087 ETLFHKALNLHtanWFLYLSTLRWFQMR-------------IDIIFVFFFIAVTFIaigtnqdgegEVGIILTLAM---- 1149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 294 lnepLIELTTQQAMLQQAVVAG-----ERVFELMDGPRQ--QYGNDDRPLQSGTI------------------EVDNVSF 348
Cdd:TIGR01271 1150 ----NILSTLQWAVNSSIDVDGlmrsvSRVFKFIDLPQEepRPSGGGGKYQLSTVlvienphaqkcwpsggqmDVQGLTA 1225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 349 AYRDD-NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPlTEGEIRLDGRPLSSLSHSALRQGVAMVQQDPVVL 427
Cdd:TIGR01271 1226 KYTEAgRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIF 1304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 428 ADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASI 507
Cdd:TIGR01271 1305 SGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 447178945 508 DSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLL 562
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
341-565 |
6.28e-30 |
|
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: 117.60 E-value: 6.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---ALRQGV 417
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVVLAD-TFLANV--------TLGRDISEERVWQALETVQLAELARSMSDgiytplgeqgnNLSVGQKQLLALA 488
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVafplrehtRLSEEEIREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 489 RVLVETPQILILDEATASIDSGTEQAIQHALAAVREH--TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLAAQ 565
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
341-561 |
2.21e-29 |
|
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: 116.51 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQ---GV 417
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMV-QQDPVVLADTFLANVTLGR---------------DISEERVWQALETVQLAELARSMSDgiytplgeqgnNLSVGQ 481
Cdd:cd03256 81 GMIfQQFNLIERLSVLENVLSGRlgrrstwrslfglfpKEEKQRALAALERVGLLDKAYQRAD-----------QLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 482 KQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIA--HRLSTIVD-ADTILVLHRGQAVEQGTH 558
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVslHQVDLAREyADRIVGLKDGRIVFDGPP 229
|
...
gi 447178945 559 QQL 561
Cdd:cd03256 230 AEL 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
354-556 |
2.81e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.66 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 354 NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSALRQGVAMVQQDPVVLAD-TF 431
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 432 LANVTLGRDISEERV--WQALETvQLAELARSMsdGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIds 509
Cdd:COG1129 97 AENIFLGREPRRGGLidWRAMRR-RARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASL-- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447178945 510 gTEQAIQHALAAVR----EHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:COG1129 172 -TEREVERLFRIIRrlkaQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTG 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
341-564 |
4.52e-29 |
|
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: 117.46 E-value: 4.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLK---NINLSVPSRNFVALVGHTGSGKSTLASLLMGYYP---LTEGEIRLDGRPLSSLSHSALR 414
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 415 Q----GVAMVQQDPV-----------VLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDgiYtPlgeqgNNLSV 479
Cdd:COG0444 82 KirgrEIQMIFQDPMtslnpvmtvgdQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDR--Y-P-----HELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 480 GQKQLLALARVLVETPQILILDEATASIDsGTEQA-IQHALAAVRE--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQ 555
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALD-VTIQAqILNLLKDLQRelGLAILFITHDLGVVAEiADRVAVMYAGRIVEE 232
|
....*....
gi 447178945 556 GTHQQLLAA 564
Cdd:COG0444 233 GPVEELFEN 241
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
25-318 |
4.92e-29 |
|
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: 116.74 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDnMVAKNNLPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAID-ALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVM-- 182
Cdd:cd18541 80 FAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVyr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 183 ---VIYQRYstpivRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLF 259
Cdd:cd18541 160 lgkKIHKRF-----RKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLI 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 260 SSlilcGLLMLFGFSA----SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18541 235 GL----SFLIVLWYGGrlviRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
356-557 |
6.92e-29 |
|
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: 114.84 E-value: 6.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 356 VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSALRQGVAMVQQDPVVLAD-TFLA 433
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 434 NVTLGRDIS-----------------EERVWQALETVQLAELArsmsdgiYTPLGeqgnNLSVGQKQLLALARVLVETPQ 496
Cdd:cd03219 95 NVMVAAQARtgsglllararreereaRERAEELLERVGLADLA-------DRPAG----ELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 497 ILILDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGT 557
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
341-556 |
7.60e-29 |
|
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: 114.04 E-value: 7.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSA---LRQGV 417
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVVLAD-TFLANVTLGRDISE-------ERVWQALETVQLAELARSMSdgiytplgeqgNNLSVGQKQLLALAR 489
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFALEVTGvppreirKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 490 VLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTilvlHRGQAVEQG 556
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTR----HRVIALERG 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
341-557 |
1.72e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 116.74 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLshSALRQGVAMV 420
Cdd:COG3842 6 LELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL--PPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDP-------VvladtfLANVTLG---RDIS----EERVWQALETVQLAELARSMsdgiytPlgeqgNNLSVGQKQLLA 486
Cdd:COG3842 83 FQDYalfphltV------AENVAFGlrmRGVPkaeiRARVAELLELVGLEGLADRY------P-----HQLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 487 LARVLVETPQILILDEATASIDSGTEQAIQHALAAV--REHTTLVVIAHRLS---TIvdADTILVLHRGQAVEQGT 557
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqrELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
341-556 |
1.80e-28 |
|
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: 113.00 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLshSALRQGVAMV 420
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVV-----LADTF---LANVTLGRDISEERVWQALETVQLAELARSMSDGiytplgeqgnnLSVGQKQLLALARVLV 492
Cdd:cd03259 78 FQDYALfphltVAENIafgLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 493 ETPQILILDEATASIDSGTEQAIQHALAAVRE--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
341-566 |
1.81e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.83 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMV 420
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDP--VVLADTFLANVT-------LGRDISEERVWQALETVQLAELARsmsdgiytplgEQGNNLSVGQKQLLALARVL 491
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAfgpvnmgLDKDEVERRVEEALKAVRMWDFRD-----------KPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 492 VETPQILILDEATASIDSGTEQAIQHALAAV-REHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQG-----THQQLLAA 564
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGdksllTDEDIVEQ 233
|
..
gi 447178945 565 QG 566
Cdd:PRK13647 234 AG 235
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
28-318 |
3.62e-28 |
|
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: 114.12 E-value: 3.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 28 AVLMMWVAAAAEVSGPLLISYFIDN-MVAKNNLPLKVVAGLAAAYVGLQlfaAGLHYAQSLLFNRAAVGVVQQLRTDVMD 106
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAaLGGGDTASLNQIALLLLGLFLLQ---AVFSFFRIYLFARVGERVVADLRKDLYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 107 AALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAA-LVGAmLVAMFSLDWRMALVAIMIFPVVLVVMVIY 185
Cdd:cd18576 78 HLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILtLIGG-VVLLFFISWKLTLLMLATVPVVVLVAVLF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 186 QRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLrpllslfsslilc 265
Cdd:cd18576 157 GRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFS------------- 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 266 GLLMLFGFSA-------------SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18576 224 SFIIFLLFGAivavlwyggrlvlAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
28-290 |
5.68e-28 |
|
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: 113.81 E-value: 5.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 28 AVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPlkVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDA 107
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLD--VLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 108 ALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQR 187
Cdd:cd18557 79 LLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 188 YSTPIVRRVRAYLADINDGFNEIINGMSVIQQF----RQQARFGERMGEASRShymARMQTLRLDGFllrplLSLFSSLI 263
Cdd:cd18557 159 YIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFsaeeKEIRRYSEALDRSYRL---ARKKALANALF-----QGITSLLI 230
|
250 260 270
....*....|....*....|....*....|.
gi 447178945 264 LCGLLMLFGFSA----SGTIEVGVLYAFISY 290
Cdd:cd18557 231 YLSLLLVLWYGGylvlSGQLTVGELTSFILY 261
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
341-565 |
7.55e-28 |
|
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: 112.00 E-value: 7.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---ALRQGV 417
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVVLAD-TFLANV--------TLGRDISEERVWQALETVQLAELARSM-SDgiytplgeqgnnLSVGQKQLLAL 487
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVafplrehtDLSEAEIRELVLEKLELVGLPGAADKMpSE------------LSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 488 ARVLVETPQILILDEATASIDSGTEQAIQHALAAVRE--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLAA 564
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLAS 232
|
.
gi 447178945 565 Q 565
Cdd:COG1127 233 D 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
340-565 |
1.16e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.17 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAyRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAM 419
Cdd:PRK13548 2 MLEARNLSVR-LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLADtFLAN--VTLGRDI-------SEERVWQALETVQLAELA-RSmsdgiYTplgeqgnNLSVGQKQLLALAR 489
Cdd:PRK13548 81 LPQHSSLSFP-FTVEevVAMGRAPhglsraeDDALVAAALAQVDLAHLAgRD-----YP-------QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 490 VLV------ETPQILILDEATASIDSGTEQAIQHALA--AVREHTTLVVIAHRLS-TIVDADTILVLHRGQAVEQGTHQQ 560
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARqlAHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
....*
gi 447178945 561 LLAAQ 565
Cdd:PRK13548 228 VLTPE 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
341-567 |
1.16e-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: 111.49 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQgVAMV 420
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVVLADT-------FLANVtlgRDISEERVWQALEtvQLAELARsMSDGIYTPLGEqgnnLSVGQKQLLALARVLVE 493
Cdd:COG4555 80 PDERGLYDRLtvrenirYFAEL---YGLFDEELKKRIE--ELIELLG-LEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 494 TPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIA-HRLSTIVD-ADTILVLHRGQAVEQGTHQQLLAAQGR 567
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
341-557 |
1.29e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.59 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNL-VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYY---PLTEGEIRLDGRPLSSLSHSALRQG 416
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 417 VAMVQQDPvvlaDTFLANVTLGRDIS---EER----------VWQALETVQLAELARSmsdgiytplgeQGNNLSVGQKQ 483
Cdd:PRK13640 86 VGIVFQNP----DNQFVGATVGDDVAfglENRavprpemikiVRDVLADVGMLDYIDS-----------EPANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 484 LLALARVLVETPQILILDEATASID-SGTEQaiqhALAAVRE-----HTTLVVIAHRLSTIVDADTILVLHRGQAVEQGT 557
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDpAGKEQ----ILKLIRKlkkknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-318 |
1.87e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 112.19 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLkvVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGL--LVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVI 184
Cdd:cd18550 79 YAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 185 YQRYSTPIVRRVRAYLADINDGFNEI--INGMSVIQQFRQQ----ARFGERMGEAS----RSHYMARMQTLRLDGFllrp 254
Cdd:cd18550 159 VGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREddeaARFARRSRELRdlgvRQALAGRWFFAALGLF---- 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 255 llslfsslILCGLLMLFGFS----ASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18550 235 --------TAIGPALVYWVGgllvIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
341-557 |
2.26e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.72 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDN-----LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-ALR 414
Cdd:PRK13633 5 IKCKNVSYKYESNEestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 415 QGVAMVQQDP-------VVLADTFLANVTLGRDISE--ERVWQALETVQLAELARsmsdgiYTPlgeqgNNLSVGQKQLL 485
Cdd:PRK13633 85 NKAGMVFQNPdnqivatIVEEDVAFGPENLGIPPEEirERVDESLKKVGMYEYRR------HAP-----HLLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447178945 486 ALARVLVETPQILILDEATASID-SGTEQAIQHALAAVREH-TTLVVIAHRLSTIVDADTILVLHRGQAVEQGT 557
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDpSGRREVVNTIKELNKKYgITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
341-556 |
2.95e-27 |
|
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: 110.56 E-value: 2.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFaYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEG-EIRLDGRPLSSLSHSALRQGVAM 419
Cdd:COG1119 4 LELRNVTV-RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDpvvLADTFLANVT--------------LGRDISEE---RVWQALETVQLAELARsmsdgiyTPLGEqgnnLSVGQK 482
Cdd:COG1119 83 VSPA---LQLRFPRDETvldvvlsgffdsigLYREPTDEqreRARELLELLGLAHLAD-------RPFGT----LSQGEQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 483 QLLALARVLVETPQILILDEATASID-SGTEQAIQ--HALAAvREHTTLVVIAHRLSTIVDADT-ILVLHRGQAVEQG 556
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDlGARELLLAllDKLAA-EGAPTLVLVTHHVEEIPPGIThVLLLKDGRVVAAG 225
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
339-570 |
3.23e-27 |
|
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: 111.10 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 339 GTIEVDNVSFAYRDD-NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPlTEGEIRLDGRPLSSLSHSALRQGV 417
Cdd:cd03289 1 GQMTVKDLTAKYTEGgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQI 497
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 498 LILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQGRYWQ 570
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
341-563 |
4.42e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 109.45 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL-SHSALRQGVAM 419
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLAD-TFLANVTLGRDI-SEERVWQALETV-----QLAELarsmsdgiytpLGEQGNNLSVGQKQLLALARVLV 492
Cdd:cd03224 80 VPEGRRIFPElTVEENLLLGAYArRRAKRKARLERVyelfpRLKER-----------RKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 493 ETPQILILDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLA 563
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
99-568 |
4.42e-27 |
|
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: 117.35 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 99 QLRTDVMDAALRQPL----SEFDTQPVGQVISRVTNDTEVIRDLYVTVvaTVLRSAALvgAMLVAMFSLdWR------MA 168
Cdd:TIGR00957 388 RIKTAVMGAVYRKALvitnSARKSSTVGEIVNLMSVDAQRFMDLATYI--NMIWSAPL--QVILALYFL-WLnlgpsvLA 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 169 LVAIMIF--PVVLVVMVIYQRYStpiVRRVRAYLADINDgFNEIINGMSVIQQFRQQARF-----GERMGEAS---RSHY 238
Cdd:TIGR00957 463 GVAVMVLmvPLNAVMAMKTKTYQ---VAHMKSKDNRIKL-MNEILNGIKVLKLYAWELAFldkveGIRQEELKvlkKSAY 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 239 MARMQTLrldgfllrPLLSLFSSLILCGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:TIGR00957 539 LHAVGTF--------TWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 319 FELMDGPRQQYGN-DDRPLQSG---TIEVDNVSFAY-RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPL 393
Cdd:TIGR00957 611 RIFLSHEELEPDSiERRTIKPGegnSITVHNATFTWaRDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 394 TEGeirldgrplsslsHSALRQGVAMVQQDPVVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQ 473
Cdd:TIGR00957 691 VEG-------------HVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEK 757
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 474 GNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAI-QHALA--AVREHTTLVVIAHRLSTIVDADTILVLHRG 550
Cdd:TIGR00957 758 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfEHVIGpeGVLKNKTRILVTHGISYLPQVDVIIVMSGG 837
|
490
....*....|....*...
gi 447178945 551 QAVEQGTHQQLLAAQGRY 568
Cdd:TIGR00957 838 KISEMGSYQELLQRDGAF 855
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
340-557 |
1.67e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.37 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAYRD----DNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS--SLSHSAL 413
Cdd:PRK13637 2 SIKIENLTHIYMEgtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQGVAMVQQDP--VVLADTF-------LANVTLGRDISEERVWQALETVQLA-ELARSMSdgiytPLgeqgnNLSVGQKQ 483
Cdd:PRK13637 82 RKKVGLVFQYPeyQLFEETIekdiafgPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKS-----PF-----ELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 484 LLALARVLVETPQILILDEATASIDSGTEQAIqhaLAAVRE-----HTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGT 557
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEI---LNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
28-318 |
1.83e-26 |
|
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: 109.56 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 28 AVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLP-----LKVVAGLAAAYVglqlFAAGLhyaQSLLFNRAAVGVVQQLRT 102
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREafyraVLLLLLLSVLSG----LFSGL---RGGCFSYAGTRLVRRLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 103 DVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVM 182
Cdd:cd18572 74 DLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALIT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 183 VIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQF----RQQARFGERMgeasrshYMARMQTLRLDGFLLRPLLSL 258
Cdd:cd18572 154 KVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFateeREARRYERAL-------DKALKLSVRQALAYAGYVAVN 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 259 FSSLILCGLLMLF---GFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18572 227 TLLQNGTQVLVLFyggHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
341-551 |
1.99e-26 |
|
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: 106.12 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS--HSALRQGVA 418
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 419 MVQQDPVVLAD-TFLANVTLGrdiseervwqaletvqlaelarsmsdgiytplgeqgnnLSVGQKQLLALARVLVETPQI 497
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 498 LILDEATASIDSGTEQAIQHALAAVREH--TTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
27-318 |
7.21e-26 |
|
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: 107.87 E-value: 7.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 27 IAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLplKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMD 106
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIDEGIANGDL--SYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 107 AALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQ 186
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 187 RYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLdgFLLRPLLSLFSSLILCG 266
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRL--MALLNPLMMLIMNLAIV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447178945 267 LLMLFG--FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18548 239 AILWFGghLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
357-553 |
7.23e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.27 E-value: 7.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSALRQGVAMVQQDPvVLADTF--LA 433
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHF-MLVPNLtvAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 434 NVTLGRdisEERVWQALETVQLAELARSMSD--GIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIdsgT 511
Cdd:COG3845 100 NIVLGL---EPTKGGRLDRKAARARIRELSEryGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL---T 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447178945 512 EQAIQHALAAVR----EHTTLVVIAHRLSTIVD-ADTILVLHRGQAV 553
Cdd:COG3845 174 PQEADELFEILRrlaaEGKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
341-554 |
9.69e-26 |
|
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: 105.59 E-value: 9.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDN---LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAL---- 413
Cdd:COG4181 9 IELRGLTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQGVAMVQQD-PVVLADTFLANVTL-----GRDISEERVWQALETVQLAELA----RSMSDgiytplGEQgnnlsvgqkQ 483
Cdd:COG4181 89 ARHVGFVFQSfQLLPTLTALENVMLplelaGRRDARARARALLERVGLGHRLdhypAQLSG------GEQ---------Q 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 484 LLALARVLVETPQILILDEATASIDSGTEQAIQHALAAV-REH-TTLVVIAHRLSTIVDADTILVLHRGQAVE 554
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERgTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-556 |
1.70e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNlVLKNINLSVPSRNFVALVGHTGSGKSTLASL---LMGYYP--LTEGEIRLDGRPLSSLSHSALRQ 415
Cdd:PRK14247 4 IEIRDLKVSFGQVE-VLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPeaRVSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 416 GVAMVQQDPVVLAD-TFLANVTLGRDIS---------EERVWQALETVQLAElarSMSDGIYTPLGEqgnnLSVGQKQLL 485
Cdd:PRK14247 83 RVQMVFQIPNPIPNlSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWD---EVKDRLDAPAGK----LSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 486 ALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAH------RLStivdaDTILVLHRGQAVEQG 556
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
341-557 |
6.81e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.93 E-value: 6.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDN---LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGyypL---TEGEIRLDGRPLSSLSHSAL- 413
Cdd:COG1135 2 IELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---LerpTSGSVLVDGVDLTALSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 --RQGVAMV-QQDPVVLADTFLANVTL--------GRDIsEERVWQALETVQLAELARSmsdgiYtPlgeqgNNLSVGQK 482
Cdd:COG1135 79 aaRRKIGMIfQHFNLLSSRTVAENVALpleiagvpKAEI-RKRVAELLELVGLSDKADA-----Y-P-----SQLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 483 QLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVRE--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGT 557
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
341-557 |
1.20e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 103.62 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAL--RQGVA 418
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 419 MVQQDP--VVLADTFLANVTLG-------RDISEERVWQALETVqlaelarSMSDGIYTPlgeqGNNLSVGQKQLLALAR 489
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEDVAFGplnlglsKEEVEKRVKEALKAV-------GMEGFENKP----PHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 490 VLVETPQILILDEATASIDSGTEQAIQHALAAV-REHTTLVVIAHRLSTI-VDADTILVLHRGQAVEQGT 557
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGT 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
341-561 |
1.58e-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: 102.32 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLshSALRQGVAMV 420
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL--PPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVVLAD-TFLANVTLG-------RDISEERVWQALETVQLAELARSMSDgiytplgeqgnNLSVGQKQLLALARVLV 492
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlrlkklpKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447178945 493 ETPQILILDEATASIDSGTEQAIQHALAAVREH--TTLVVIAHRLS-TIVDADTILVLHRGQAVEQGTHQQL 561
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElgITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
342-533 |
2.29e-24 |
|
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: 101.18 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 342 EVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshSALRQGVAMVQ 421
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 422 QDP--VVLADTFLANVTLGRDI---SEERVWQALETVQLAELARSMsdgiytPLgeqgnNLSVGQKQLLALARVLVETPQ 496
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKEldaGNEQAETVLKDLDLYALKERH------PL-----SLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447178945 497 ILILDEATASIDSGTEQAIQHA---LAAvrEHTTLVVIAH 533
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELireLAA--QGKAVIVITH 184
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
341-563 |
2.33e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.18 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRD----DNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS----A 412
Cdd:PRK13634 3 ITFQKVEHRYQYktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 413 LRQGVAMVQQDPvvlaDTFLANVTLGRDIS-------------EERVWQALETVQLAE--LARSMSDgiytplgeqgnnL 477
Cdd:PRK13634 83 LRKKVGIVFQFP----EHQLFEETVEKDICfgpmnfgvseedaKQKAREMIELVGLPEelLARSPFE------------L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 478 SVGQKQLLALARVLVETPQILILDEATASID-SGTEQAIQHALAAVREHT-TLVVIAHRLSTIVD-ADTILVLHRGQAVE 554
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpKGRKEMMEMFYKLHKEKGlTTVLVTHSMEDAARyADQIVVMHKGTVFL 226
|
....*....
gi 447178945 555 QGTHQQLLA 563
Cdd:PRK13634 227 QGTPREIFA 235
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-318 |
2.95e-24 |
|
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: 103.41 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVV-------------AGLAAAYVGLQLFAAGLHYAQSLLFNR 91
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFLPLVpaslgpadprgqlWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 92 AAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVA 171
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 172 IMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFL 251
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAF 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 252 LRPLLSLFSSLILC-----GLLMLFG-FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18565 241 FPVIRLVAGAGFVAtfvvgGYWVLDGpPLFTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
341-563 |
6.20e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.73 E-value: 6.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDD--NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVA 418
Cdd:PRK13650 5 IEVKNLTFKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 419 MVQQDP-------VVLADTF--LANVTLGRDISEERVWQALETVQLAELARsmsdgiytplgEQGNNLSVGQKQLLALAR 489
Cdd:PRK13650 85 MVFQNPdnqfvgaTVEDDVAfgLENKGIPHEEMKERVNEALELVGMQDFKE-----------REPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 490 VLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIA--HRLSTIVDADTILVLHRGQAVEQGTHQQLLA 563
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISitHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
341-565 |
7.22e-24 |
|
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: 100.84 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMV 420
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 -QQDPVVLADTFLANVTL-------GRDISEERVWQALETVQL--AELARSMSDgiytplgeqgnNLSVGQKQLLALARV 490
Cdd:cd03295 81 iQQIGLFPHMTVEENIALvpkllkwPKEKIRERADELLALVGLdpAEFADRYPH-----------ELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 491 LVETPQILILDEATASIDSGTEQAIQHALAAVRE--HTTLVVIAHRL-STIVDADTILVLHRGQAVEQGTHQQLLAAQ 565
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
310-554 |
9.82e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 105.27 E-value: 9.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 310 QAVVagERVFEL---MDGPRQQYGNDDR--PLQSGTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLA 384
Cdd:COG4178 329 RATV--DRLAGFeeaLEAADALPEAASRieTSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 385 SLLMGYYPLTEGEIRldgRPLsslshsalRQGVAMVQQDPVVLADTFLANVT---LGRDISEERVWQALETVQLAELARS 461
Cdd:COG4178 407 RAIAGLWPYGSGRIA---RPA--------GARVLFLPQRPYLPLGTLREALLypaTAEAFSDAELREALEAVGLGHLAER 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 462 MSDgiytplgEQ--GNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIV 539
Cdd:COG4178 476 LDE-------EAdwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAA 548
|
250
....*....|....*
gi 447178945 540 DADTILVLHRGQAVE 554
Cdd:COG4178 549 FHDRVLELTGDGSWQ 563
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
336-563 |
1.11e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.08 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 336 LQSGTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL--SSLSHSAL 413
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQGVAMVQQDP-------VVLADTFLA--NVTLGRDISEERVWQALETVQLAELARSMSdgiytplgeqgNNLSVGQKQL 484
Cdd:PRK13636 81 RESVGMVFQDPdnqlfsaSVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKDKPT-----------HCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 485 LALARVLVETPQILILDEATASIDS-GTEQAIQHALAAVRE-HTTLVVIAHRLSTI-VDADTILVLHRGQAVEQGTHQQL 561
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPmGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEV 229
|
..
gi 447178945 562 LA 563
Cdd:PRK13636 230 FA 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
356-556 |
1.55e-23 |
|
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: 98.39 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 356 VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGY--YPLTEGEIRLDGRPLSSlshSALRQGVAMVQQDpvvlaDTFLA 433
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDK---RSFRKIIGYVPQD-----DILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 434 NVTlgrdiseerVWQALETVqlAELaRSmsdgiytplgeqgnnLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQ 513
Cdd:cd03213 96 TLT---------VRETLMFA--AKL-RG---------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447178945 514 AIQHALAA-VREHTTLVVIAHRLSTIV--DADTILVLHRGQAVEQG 556
Cdd:cd03213 149 QVMSLLRRlADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
341-557 |
4.05e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 99.38 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNL--------VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS--- 409
Cdd:PRK10419 4 LNVSGLSHHYAHGGLsgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 410 HSALRQGVAMVQQDPVvlaDTFLANVTLGRDISE-----------ERVWQALETVQLAELARSMSDgiytPLGEQgnnLS 478
Cdd:PRK10419 84 RKAFRRDIQMVFQDSI---SAVNPRKTVREIIREplrhllsldkaERLARASEMLRAVDLDDSVLD----KRPPQ---LS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 479 VGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREH--TTLVVIAHRLStIVD--ADTILVLHRGQAVE 554
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfgTACLFITHDLR-LVErfCQRVMVMDNGQIVE 232
|
...
gi 447178945 555 QGT 557
Cdd:PRK10419 233 TQP 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
341-556 |
4.06e-23 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 97.65 E-value: 4.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDdNLVLKNINLSVPSrNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSALRQGVAMV 420
Cdd:cd03264 1 LQLENLTKRYGK-KRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQD----PVVLADTFLANVTLGRDIS----EERVWQALETVQLAELA-RSMSDgiytplgeqgnnLSVGQKQLLALARVL 491
Cdd:cd03264 78 PQEfgvyPNFTVREFLDYIAWLKGIPskevKARVDEVLELVNLGDRAkKKIGS------------LSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 492 VETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
310-547 |
5.38e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 104.34 E-value: 5.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 310 QAVVAGERVFELMD-GPRQQYGNDDRPLQS-GTIEVDNVSFAY--RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLAS 385
Cdd:PTZ00265 350 KSLEATNSLYEIINrKPLVENNDDGKKLKDiKKIQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILK 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 386 LLMGYYPLTEGEIRL-DGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLG-------------------------- 438
Cdd:PTZ00265 430 LIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenkn 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 439 --------------------------------RDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLA 486
Cdd:PTZ00265 510 krnscrakcagdlndmsnttdsneliemrknyQTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRIS 589
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 487 LARVLVETPQILILDEATASIDSGTEQAIQHALAAVR--EHTTLVVIAHRLSTIVDADTILVL 547
Cdd:PTZ00265 590 IARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
341-563 |
9.87e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.14 E-value: 9.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH-SALRQGVAM 419
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPvvlaDTFLANVTLGRDIS---EERVWQALETVQLAELARSmSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQ 496
Cdd:PRK13644 82 VFQNP----ETQFVGRTVEEDLAfgpENLCLPPIEIRKRVDRALA-EIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 497 ILILDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLA 563
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
341-565 |
9.88e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.13 E-value: 9.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLvlkNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShSALRqGVAMV 420
Cdd:COG3840 2 LRLDDLTYRYGDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-PAER-PVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVVLAD-TFLANVTLGRD----ISEE---RVWQALETVQLAELARSMSDgiytplgeqgnNLSVGQKQLLALARVLV 492
Cdd:COG3840 77 FQENNLFPHlTVAQNIGLGLRpglkLTAEqraQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 493 -ETPqILILDEATASIDSGTEQAIQHALAAV-REH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLAAQ 565
Cdd:COG3840 146 rKRP-ILLLDEPFSALDPALRQEMLDLVDELcRERgLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
341-563 |
1.16e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 98.24 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLV--LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVA 418
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 419 MVQQDP--VVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGiytpLGEQGNNLSVGQKQLLALARVLVETPQ 496
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDF----KTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 497 ILILDEATASIDSGTEQAIQHALAAVRE--HTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLA 563
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
28-318 |
2.37e-22 |
|
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: 97.58 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 28 AVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVVAGLAAAYVGLQ-LFAAG--LHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALALLgVFVVGaaANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVI 184
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 185 YQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSLIL 264
Cdd:cd18573 161 YGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447178945 265 CGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18573 241 SVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
339-561 |
2.56e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.61 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 339 GTIEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLshSALRQGVA 418
Cdd:COG3839 2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL--PPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 419 MVQQDPVV-----LADtflaNVTLG---RDIS----EERVWQALETVQLAELARSMSDgiytplgeqgnNLSVGQKQLLA 486
Cdd:COG3839 79 MVFQSYALyphmtVYE----NIAFPlklRKVPkaeiDRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 487 LARVLVETPQILILDEATASIDsgteqaiqhalAAVREH--TTLVVIAHRL-STIV----D-------ADTILVLHRGQA 552
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLD-----------AKLRVEmrAEIKRLHRRLgTTTIyvthDqveamtlADRIAVMNDGRI 212
|
....*....
gi 447178945 553 VEQGTHQQL 561
Cdd:COG3839 213 QQVGTPEEL 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
120-561 |
2.74e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 101.98 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 120 PVGQVISRVTNDTEVIRDLYVTVVAtvLRSAALvgAMLVAMFSLDWRMAlVAIMIFPVVLVVMVIYQrysTPIVRRVRA- 198
Cdd:PLN03232 396 ASGKVTNMITTDANALQQIAEQLHG--LWSAPF--RIIVSMVLLYQQLG-VASLFGSLILFLLIPLQ---TLIVRKMRKl 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 199 -----YLADINDGF-NEIINGMSVIQQFRQQARFGERMgEASRSHYMARMQTLRL----DGFLLRPLLSLFSSLILcGLL 268
Cdd:PLN03232 468 tkeglQWTDKRVGIiNEILASMDTVKCYAWEKSFESRI-QGIRNEELSWFRKAQLlsafNSFILNSIPVVVTLVSF-GVF 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 269 MLFGfsasGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERVFELMDGPRQQYGNDDrPLQSGT--IEVDNV 346
Cdd:PLN03232 546 VLLG----GDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNP-PLQPGApaISIKNG 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 347 SFAY--RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGeirldgrplsslSHSALRQGVAMVQQDP 424
Cdd:PLN03232 621 YFSWdsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAET------------SSVVIRGSVAYVPQVS 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 425 VVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEAT 504
Cdd:PLN03232 689 WIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 505 ASIDSG-TEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQL 561
Cdd:PLN03232 769 SALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
357-564 |
2.81e-22 |
|
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: 100.53 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPlTEGEIRLDGRPLSSLSHSA---LRQGVAMVQQDPV-------- 425
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPFgslsprmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 426 ---VLADTFLA-NVTLGRDISEERVWQALETVQLAELARSMsdgiYtPlgeqgNNLSVGQKQLLALARVLVETPQILILD 501
Cdd:COG4172 381 vgqIIAEGLRVhGPGLSAAERRARVAEALEEVGLDPAARHR----Y-P-----HEFSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 502 EATASIDSgTEQA-------------------IQHALAAVREhttlvvIAHRlstivdadtILVLHRGQAVEQGTHQQLL 562
Cdd:COG4172 451 EPTSALDV-SVQAqildllrdlqrehglaylfISHDLAVVRA------LAHR---------VMVMKDGKVVEQGPTEQVF 514
|
..
gi 447178945 563 AA 564
Cdd:COG4172 515 DA 516
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
341-551 |
3.63e-22 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 94.90 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH--SALRQGVA 418
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKniNELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 419 MVQQDPVVLAD-TFLANVTLG--------RDISEERVWQALETVQLAELARSMsdgiytPlgeqgNNLSVGQKQLLALAR 489
Cdd:cd03262 80 MVFQQFNLFPHlTVLENITLApikvkgmsKAEAEERALELLEKVGLADKADAY------P-----AQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 490 VLVETPQILILDEATASIDS---GTEQAIQHALAavREHTTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPelvGEVLDVMKDLA--EEGMTMVVVTHEMGFAREvADRVIFMDDGR 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
341-562 |
3.90e-22 |
|
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: 95.48 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDdnLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSalRQGVAMV 420
Cdd:cd03299 1 LKVENLSKDWKE--FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVVLAD-TFLANVTLG-RDISEERVWQALETVQLAELArsmsdGIYTPLGEQGNNLSVGQKQLLALARVLVETPQIL 498
Cdd:cd03299 77 PQNYALFPHmTVYKNIAYGlKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 499 ILDEATASIDSGTEQAIQHALAAVREH--TTLVVIAHRLSTI-VDADTILVLHRGQAVEQGTHQQLL 562
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEfgVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
341-556 |
4.03e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 94.59 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNlVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLsHSALRQGVAMV 420
Cdd:cd03268 1 LKTNDLTKTYGKKR-VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQD---PVVLADTFLANVTLGRDISEERVWQALETVQLAELARsmsdgiytplgEQGNNLSVGQKQLLALARVLVETPQI 497
Cdd:cd03268 79 EAPgfyPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAK-----------KKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447178945 498 LILDEATASIDSGTEQAIQHALAAVREHTTLVVIA-HRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
22-318 |
7.87e-22 |
|
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: 95.98 E-value: 7.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 22 RKPLGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLkvVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAvgvvQQLR 101
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINL--LNIISIGLILLYLFQSLLSYIRSYLLLKLS----QKLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 102 TDVMDAALRQ----PLSEFDTQPVGQVISRVtNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPV 177
Cdd:cd18570 75 IRLILGYFKHllklPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 178 VLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMgeasRSHYMARMQTLRLDGFLLRPLLS 257
Cdd:cd18570 154 YILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKI----EKKFSKLLKKSFKLGKLSNLQSS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447178945 258 LFSSLILCGLLMLFGFSA----SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18570 230 IKGLISLIGSLLILWIGSylviKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
336-551 |
1.19e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 94.74 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 336 LQSGT-IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsslshSALR 414
Cdd:PRK11247 7 LNQGTpLLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 415 QGVAMVQQDPVVLA-DTFLANVTLG-RDISEERVWQALETVQLAELArsmsdgiytplGEQGNNLSVGQKQLLALARVLV 492
Cdd:PRK11247 81 EDTRLMFQDARLLPwKKVIDNVGLGlKGQWRDAALQALAAVGLADRA-----------NEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447178945 493 ETPQILILDEATASIDSGTEQAIQHALAAV-REHT-TLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGfTVLLVTHDVSEAVAmADRVLLIEEGK 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
341-564 |
1.77e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 94.47 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVS--FAYRDDNL------VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSA 412
Cdd:PRK15112 5 LEVRNLSktFRYRTGWFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 413 LRQGVAMVQQDPV-----------VLADTFLANVTLGRDISEERVWQALETVQLAElarsmSDGIYTPlgeqgNNLSVGQ 481
Cdd:PRK15112 85 RSQRIRMIFQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQVGLLP-----DHASYYP-----HMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 482 KQLLALARVLVETPQILILDEATASID-SGTEQAIQHALAAVREH--TTLVVIAHRLSTIVDADTILVLHRGQAVEQGTH 558
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDmSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
....*.
gi 447178945 559 QQLLAA 564
Cdd:PRK15112 235 ADVLAS 240
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
308-563 |
2.10e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 99.43 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 308 LQQAVVAGERVfeLMDGPrqqygnddrPLQSG--TIEVDNVSFAY--RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTL 383
Cdd:PLN03130 591 LEELLLAEERV--LLPNP---------PLEPGlpAISIKNGYFSWdsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSL 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 384 ASLLMGYYPLTEGeirldgrplsslSHSALRQGVAMVQQDPVVLADTFLANVTLGRDISEERVWQALETVQLAELARSMS 463
Cdd:PLN03130 660 ISAMLGELPPRSD------------ASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLP 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 464 DGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGT-EQAIQHALAAVREHTTLVVIAHRLSTIVDAD 542
Cdd:PLN03130 728 GGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgRQVFDKCIKDELRGKTRVLVTNQLHFLSQVD 807
|
250 260
....*....|....*....|.
gi 447178945 543 TILVLHRGQAVEQGTHQQLLA 563
Cdd:PLN03130 808 RIILVHEGMIKEEGTYEELSN 828
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-564 |
2.87e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.57 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 342 EVDNVS--FAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS------SLSHSAL 413
Cdd:PRK14246 9 DVFNISrlYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQGVAMVQQDP-----VVLADTfLANVTLGRDISEERVWQAL--ETVQLAELARSMSDGIYTPlgeqGNNLSVGQKQLLA 486
Cdd:PRK14246 89 RKEVGMVFQQPnpfphLSIYDN-IAYPLKSHGIKEKREIKKIveECLRKVGLWKEVYDRLNSP----ASQLSGGQQQRLT 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 487 LARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLAA 564
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
302-561 |
3.13e-21 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 94.15 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 302 TTQQAMLQQAVVAGERVFELMDGPRQQygNDDRPLQSGTievDNVSFAYRDD--NLVLKNINLSVPSRNFVALVGHTGSG 379
Cdd:cd03291 1 TTGVIMENVTAFWDEGFGELLEKAKQE--NNDRKHSSDD---NNLFFSNLCLvgAPVLKNINLKIEKGEMLAITGSTGSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 380 KSTLASLLMGYYPLTEGEIRLDGRplsslshsalrqgVAMVQQDPVVLADTFLANVTLGRDISEERVWQALETVQLAELA 459
Cdd:cd03291 76 KTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 460 RSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAI-QHALAAVREHTTLVVIAHRLSTI 538
Cdd:cd03291 143 TKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHL 222
|
250 260
....*....|....*....|...
gi 447178945 539 VDADTILVLHRGQAVEQGTHQQL 561
Cdd:cd03291 223 KKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
357-563 |
4.33e-21 |
|
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: 93.48 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQ----GVAMVQQDPVVLAD-TF 431
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 432 LANVTLG-------RDISEERVWQALETVQLAELARSMSDgiytplgeqgnNLSVGQKQLLALARVLVETPQILILDEAT 504
Cdd:cd03294 120 LENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447178945 505 ASIDSGTEQAIQ-HALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLA 563
Cdd:cd03294 189 SALDPLIRREMQdELLRLQAELqKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
25-304 |
4.81e-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: 93.67 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMmwvaAAAEVSGPLLISYFIDNMVAKNNLPLkvVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18549 8 LFCAVLI----AALDLVFPLIVRYIIDDLLPSKNLRL--ILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTND----TEVI----RDLYVTVVatvlrsaALVGAMLVaMFSLDWRMALVAIMIFP 176
Cdd:cd18549 82 FEHLQKLSFSFFDNNKTGQLMSRITNDlfdiSELAhhgpEDLFISII-------TIIGSFII-LLTINVPLTLIVFALLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 177 VVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLL 256
Cdd:cd18549 154 LMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMN 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 257 SLFsslilcGLL----MLFG--FSASGTIEVGVLYAFISYLGRLNEP---LIELTTQ 304
Cdd:cd18549 234 FFT------NLLnlvvLVAGgyFIIKGEITLGDLVAFLLYVNVFIKPirrLVNFTEQ 284
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
341-557 |
7.80e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 94.10 E-value: 7.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDN---LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAL---R 414
Cdd:PRK11153 2 IELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 415 QGVAMVQQDPVVLAD-TFLANVTL-------GRDISEERVWQALETVQLAELARSmsdgiYtPlgeqgNNLSVGQKQLLA 486
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALplelagtPKAEIKARVTELLELVGLSDKADR-----Y-P-----AQLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447178945 487 LARVLVETPQILILDEATASIDSGTEQAIQHALAAV-RE-HTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGT 557
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
340-565 |
1.62e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.20 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAYRDDNLV----LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL----SSLSHS 411
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 412 ALRQGVAMVQQDPVV--LADTFLANVTLG-------RDISEERVWQALETVQLAELARSMSdgiytPLgeqgnNLSVGQK 482
Cdd:PRK13641 82 KLRKKVSLVFQFPEAqlFENTVLKDVEFGpknfgfsEDEAKEKALKWLKKVGLSEDLISKS-----PF-----ELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 483 QLLALARVLVETPQILILDEATASID-SGTEQAIQHALAAVREHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQ 560
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDpEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKE 231
|
....*
gi 447178945 561 LLAAQ 565
Cdd:PRK13641 232 IFSDK 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
340-561 |
1.83e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.22 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSfAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLsHSALRQgVAM 419
Cdd:PRK10851 2 SIEIANIK-KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL-HARDRK-VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLAD-TFLANVTLG-----------RDISEERVWQALETVQLAELA-RSMSdgiytplgeqgnNLSVGQKQLLA 486
Cdd:PRK10851 79 VFQHYALFRHmTVFDNIAFGltvlprrerpnAAAIKAKVTQLLEMVQLAHLAdRYPA------------QLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 487 LARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHT--TLVVIAHRLSTIVD-ADTILVLHRGQaVEQ-GTHQQL 561
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEvADRVVVMSQGN-IEQaGTPDQV 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
341-557 |
2.74e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.34 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRD----DNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS----A 412
Cdd:PRK13649 3 INLQNVSYTYQAgtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 413 LRQGVAMVQQDP--VVLADTFLANVTLGRD---ISEErvwqalETVQLAELARSMSdGIYTPLGEQGN-NLSVGQKQLLA 486
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVLKDVAFGPQnfgVSQE------EAEALAREKLALV-GISESLFEKNPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 487 LARVLVETPQILILDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGT 557
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
357-553 |
3.25e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.23 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLT--EGEIRLDGRPL--SSLSHSAlRQGVAMVQQDPVVLAD-TF 431
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELqaSNIRDTE-RAGIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 432 LANVTLGRDISE------ERVWQALETVqLAELARSMSdgIYTPLGeqgnNLSVGQKQLLALARVLVETPQILILDEATA 505
Cdd:PRK13549 100 LENIFLGNEITPggimdyDAMYLRAQKL-LAQLKLDIN--PATPVG----NLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447178945 506 SIdsgTEQAIQHALAAVRE----HTTLVVIAHRLSTIVD-ADTILVLHRGQAV 553
Cdd:PRK13549 173 SL---TESETAVLLDIIRDlkahGIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
70-229 |
3.34e-20 |
|
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: 91.38 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 70 AYVGLQLFAAGlhYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRS 149
Cdd:cd18577 54 VYLGIGSFVLS--YIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 150 -AALVGAMLVAmFSLDWRMALVAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGE 228
Cdd:cd18577 132 lSTFIAGFIIA-FIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIK 210
|
.
gi 447178945 229 R 229
Cdd:cd18577 211 R 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-556 |
4.18e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.90 E-value: 4.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSfAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLT-----EGEIRLDGRPLSSLSHSAL-- 413
Cdd:PRK14267 5 IETVNLR-VYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIev 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQGVAMVQQDPVVLAD-TFLANVTLG---------RDISEERVWQALETVQLAelarsmsDGIYTPLGEQGNNLSVGQKQ 483
Cdd:PRK14267 84 RREVGMVFQYPNPFPHlTIYDNVAIGvklnglvksKKELDERVEWALKKAALW-------DEVKDRLNDYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447178945 484 LLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
341-550 |
4.82e-20 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 88.93 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEI----RLDGRPLSSLSHSALRQG 416
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 417 VAMVQQDPVVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQ 496
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 497 ILILDEATASIDSGTEQAIQHA--LAAVREHT-TLVVIAHRLSTIVDADTILVLHRG 550
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKrTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
337-564 |
6.97e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 90.16 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 337 QSGTIEVDNVSFAYRDDNL--------VLKNINLSVPSRNFVALVGHTGSGKSTLASLL-------MGYYplTEGEIRLD 401
Cdd:PRK14271 9 QSGAADVDAAAPAMAAVNLtlgfagktVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYR--YSGDVLLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 402 GRPLSSLSHS-ALRQGVAMVQQDPVVLADTFLANVTLG---RDISEERVWQALETVQLAELArsMSDGIYTPLGEQGNNL 477
Cdd:PRK14271 87 GRSIFNYRDVlEFRRRVGMLFQRPNPFPMSIMDNVLAGvraHKLVPRKEFRGVAQARLTEVG--LWDAVKDRLSDSPFRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 478 SVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEG 244
|
....*...
gi 447178945 557 THQQLLAA 564
Cdd:PRK14271 245 PTEQLFSS 252
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
336-556 |
1.06e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.17 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 336 LQSGTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPlsslSHSALRQ 415
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP----TRQALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 416 G-VAMVQQD-------PVVLADTflanVTLGR-------DISEERVWQALEtvqlAELAR-SMSDGIYTPLGEqgnnLSV 479
Cdd:PRK15056 78 NlVAYVPQSeevdwsfPVLVEDV----VMMGRyghmgwlRRAKKRDRQIVT----AALARvDMVEFRHRQIGE----LSG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 480 GQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVR-EHTTLVVIAHRLSTIVDADTILVLHRGQAVEQG 556
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
341-561 |
1.23e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.09 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMV 420
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDP-------VVLADTFLANVTLGRDIS--EERVWQALETVQLAELARSMSdgiytplgeqgNNLSVGQKQLLALARVL 491
Cdd:PRK13652 84 FQNPddqifspTVEQDIAFGPINLGLDEEtvAHRVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 492 VETPQILILDEATASID-SGTEQAIQHALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQL 561
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDpQGVKELIDFLNDLPETYgMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
341-555 |
1.67e-19 |
|
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: 87.31 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLshSALRQGVAMV 420
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVVLAD-TFLANVTLG-------RDISEERVWQALETVQLAELarsmsdgiytpLGEQGNNLSVGQKQLLALARVLV 492
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFGlklrkvpKDEIDERVREVAELLQIEHL-----------LDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 493 ETPQILILDEATASIDSGTEQA-------IQHALAAvrehTTLVVIAHRLSTIVDADTILVLHRGQaVEQ 555
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQmraelkrLQQRLGT----TTIYVTHDQVEAMTMADRIAVMNDGQ-IQQ 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
356-565 |
1.75e-19 |
|
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: 93.05 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 356 VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshsalrqgVAMVQQDPVVLADTFLANV 435
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 436 TLGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAI 515
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447178945 516 -QHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQ 565
Cdd:TIGR01271 588 fESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
341-556 |
1.77e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 86.81 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSfAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMG--YYPLTEGEIRLDGRPLSSLS-HSALRQGV 417
Cdd:cd03217 1 LEIKDLH-VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPpEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVvladtflanvtlgrdiseervwqALETVQLAELARSMSDGiytplgeqgnnLSVGQKQLLALARVLVETPQI 497
Cdd:cd03217 80 FLAFQYPP-----------------------EIPGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 498 LILDEatasIDSG--------TEQAIQHALaavREHTTLVVIAH--RLSTIVDADTILVLHRGQAVEQG 556
Cdd:cd03217 126 AILDE----PDSGldidalrlVAEVINKLR---EEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
340-561 |
2.58e-19 |
|
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: 87.39 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslSHSALRQGVAM 419
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLAD-TFLANVTLG---RDISE--------ERVWQALETVQLAELARSMSdgiytplgeqgNNLSVGQKQLLAL 487
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAFGlrvKPRSErppeaeirAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 488 ARVLVETPQILILDEATASIDSGTEQAIQHALAAVRE--HTTLVVIAHRLSTIVD-ADTILVLHRGQaVEQ-GTHQQL 561
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEvADRVVVMNKGR-IEQvGTPDEV 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
341-561 |
8.14e-19 |
|
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: 85.25 E-value: 8.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDD-NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAlRQGVAM 419
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA-RQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDpvvlaDTFLANVT-------------LGRDISEERVWQALETVQLAELARSMSdgiytplgeqgNNLSVGQKQLLA 486
Cdd:cd03263 80 CPQF-----DALFDELTvrehlrfyarlkgLPKSEIKEEVELLLRVLGLTDKANKRA-----------RTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 487 LARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTI-VDADTILVLHRGQAVEQGTHQQL 561
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
28-290 |
1.12e-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: 86.77 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 28 AVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPL--KVVAGLAAAYVGLQLFAAGLHYAQSLLFNRaavgVVQQLRTDVM 105
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALlnRAFLLLLAVALVLALASALRFYLVSWLGER----VVADLRKAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 106 DAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAA-LVGAmLVAMFSLDWRMALVAIMIFPVVLVVMVI 184
Cdd:cd18575 77 AHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLlLIGG-LVMLFITSPKLTLLVLLVIPLVVLPIIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 185 YQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLrpllslfsslil 264
Cdd:cd18575 156 FGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLT------------ 223
|
250 260 270
....*....|....*....|....*....|....*....
gi 447178945 265 cGLLMLFGFSA-------------SGTIEVGVLYAFISY 290
Cdd:cd18575 224 -ALVIFLVFGAivfvlwlgahdvlAGRMSAGELSQFVFY 261
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
357-556 |
1.42e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-ALRQGVAMVQQDPVVLAD-TFLAN 434
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 435 VTLGRdISEERVWqALETVQLAEL---ARSMSD--GIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIds 509
Cdd:PRK09700 101 LYIGR-HLTKKVC-GVNIIDWREMrvrAAMMLLrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL-- 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447178945 510 gTEQAIQHALAAVR----EHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:PRK09700 177 -TNKEVDYLFLIMNqlrkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
340-562 |
1.72e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 87.12 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAYRDDNLvLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSALRQGVAM 419
Cdd:COG1118 2 SIEVRNISKRFGSFTL-LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-NLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDP-------VvlADtflaNV-------TLGRDISEERVWQALETVQLAELARSmsdgiYtPlgeqgNNLSVGQKQLL 485
Cdd:COG1118 80 VFQHYalfphmtV--AE----NIafglrvrPPSKAEIRARVEELLELVQLEGLADR-----Y-P-----SQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 486 ALARVLVETPQILILDEATASIDsgteqaiqhalAAVR--------------EHTTLVVI-----AHRLstivdADTILV 546
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALD-----------AKVRkelrrwlrrlhdelGGTTVFVThdqeeALEL-----ADRVVV 206
|
250
....*....|....*.
gi 447178945 547 LHRGQAVEQGTHQQLL 562
Cdd:COG1118 207 MNQGRIEQVGTPDEVY 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
356-547 |
1.77e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.82 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 356 VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLshsaLRQGVAMVQQDPVVLADTflanV 435
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAY----VPQRSEVPDSLPLTVRDL----V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 436 TLGR-----------DISEERVWQALETVQLAELARSmsdgiytPLGEqgnnLSVGQKQLLALARVLVETPQILILDEAT 504
Cdd:NF040873 79 AMGRwarrglwrrltRDDRAAVDDALERVGLADLAGR-------QLGE----LSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447178945 505 ASIDSGTEQAIQHALA-AVREHTTLVVIAHRLSTIVDADTILVL 547
Cdd:NF040873 148 TGLDAESRERIIALLAeEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
341-556 |
1.82e-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: 84.08 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLvlkNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSalRQGVAMV 420
Cdd:cd03298 1 VRLDKIRFSYGEQPM---HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVVLAD-TFLANVTLGR-------DISEERVWQALETVQLAELARSMSDgiytplgeqgnNLSVGQKQLLALARVLV 492
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGLspglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 493 ETPQILILDEATASIDSGTEQAIQHALAAVREHT--TLVVIAHRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
371-563 |
1.83e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 86.56 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 371 ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSA---LRQGVAMVQQDPV-----------VLADTFLANVT 436
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNPYgslnprkkvgqILEEPLLINTS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 437 LGRDISEERVWQALETVQLaelaRSMSDGIYTPLgeqgnnLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQ 516
Cdd:PRK11308 125 LSAAERREKALAMMAKVGL----RPEHYDRYPHM------FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447178945 517 HALAAVRE--HTTLVVIAHRLStIVD--ADTILVLHRGQAVEQGTHQQLLA 563
Cdd:PRK11308 195 NLMMDLQQelGLSYVFISHDLS-VVEhiADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
341-557 |
2.64e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.92 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsALRQGVAMV 420
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--AENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVVLAD-TFLANVTLG--------RDIsEERVWQALETVQLAELARSmsdgiytplgeQGNNLSVGQKQLLALARVL 491
Cdd:PRK09452 92 FQSYALFPHmTVFENVAFGlrmqktpaAEI-TPRVMEALRMVQLEEFAQR-----------KPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 492 VETPQILILDEATASIDSGTEQAIQHALAAVREHT--TLVVIAH-RLSTIVDADTILVLHRGQAVEQGT 557
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
341-557 |
3.74e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.17 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDN----LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSA---- 412
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 413 LRQGVAMVQQDP--VVLADTFLANVTLGRD---ISEERVWQ-ALETVQLAELARSMSDGiyTPLgeqgnNLSVGQKQLLA 486
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQnfgIPKEKAEKiAAEKLEMVGLADEFWEK--SPF-----ELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 487 LARVLVETPQILILDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGT 557
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
341-556 |
4.92e-18 |
|
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: 83.35 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDN---------------------LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIR 399
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgevgefWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 400 LDGRPlsslsHSALRQGVAmvqqdpvvladtFLANVTlGRD----------ISEERVWQAL-ETVQLAELArsmsDGIYT 468
Cdd:cd03220 81 VRGRV-----SSLLGLGGG------------FNPELT-GREniylngrllgLSRKEIDEKIdEIIEFSELG----DFIDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 469 PLGeqgnNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIA-HRLSTIVD-ADTILV 546
Cdd:cd03220 139 PVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALV 214
|
250
....*....|
gi 447178945 547 LHRGQAVEQG 556
Cdd:cd03220 215 LEKGKIRFDG 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
341-556 |
7.14e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 82.33 E-value: 7.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNlVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAL-----RQ 415
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIgylpeER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 416 GV---AMVQQDPVVLADtfLANVTLGRDISEERVWqaLETVQLAELArsmsdgiYTPLGEqgnnLSVGQKQLLALARVLV 492
Cdd:cd03269 80 GLypkMKVIDQLVYLAQ--LKGLKKEEARRRIDEW--LERLELSEYA-------NKRVEE----LSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 493 ETPQILILDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
341-534 |
7.76e-18 |
|
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: 81.05 E-value: 7.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldGRPLSSlshsalrqGVAMV 420
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGE--------DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPvvladtFLANVTLgRDiseervwqaletvQLaelarsmsdgIYtPLGEqgnNLSVGQKQLLALARVLVETPQILIL 500
Cdd:cd03223 70 PQRP------YLPLGTL-RE-------------QL----------IY-PWDD---VLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....*
gi 447178945 501 DEATASIDSGTEQAIqhaLAAVREH-TTLVVIAHR 534
Cdd:cd03223 116 DEATSALDEESEDRL---YQLLKELgITVISVGHR 147
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
341-564 |
9.53e-18 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 86.66 E-value: 9.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDN---LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYP----LTEGEIRLDGRPLSSLSHSAL 413
Cdd:COG4172 7 LSVEDLSVAFGQGGgtvEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQ----GVAMVQQDPVV-----------LADTFLANVTLGRDISEERVWQALETVQLAELARSMSDgiYtPlgeqgNNLS 478
Cdd:COG4172 87 RRirgnRIAMIFQEPMTslnplhtigkqIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDA--Y-P-----HQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 479 VGQKQLLALARVLVETPQILILDEATASIDSgTEQA-IQHALAA-VREH-TTLVVIAHRLStIVD--ADTILVLHRGQAV 553
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQAqILDLLKDlQRELgMALLLITHDLG-VVRrfADRVAVMRQGEIV 236
|
250
....*....|.
gi 447178945 554 EQGTHQQLLAA 564
Cdd:COG4172 237 EQGPTAELFAA 247
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
341-567 |
9.63e-18 |
|
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: 81.64 E-value: 9.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAyRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMV 420
Cdd:TIGR01189 1 LAARNLACS-RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVVLADTFLANVTLGRDI--SEER-VWQALETVQLAELArsmsdgiYTPLGEqgnnLSVGQKQLLALARVLVETPQI 497
Cdd:TIGR01189 80 HLPGLKPELSALENLHFWAAIhgGAQRtIEDALAAVGLTGFE-------DLPAAQ----LSAGQQRRLALARLWLSRRPL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 498 LILDEATASIDSgteQAIQHALAAVREHttlvviahrlstivdadtilvLHRGQAVEQGTHQQLLAAQGR 567
Cdd:TIGR01189 149 WILDEPTTALDK---AGVALLAGLLRAH---------------------LARGGIVLLTTHQDLGLVEAR 194
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
331-554 |
1.08e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.45 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 331 NDDRPLqsgtIEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTL----ASLLMgyyPlTEGEIRLDGRPLS 406
Cdd:PRK10247 2 QENSPL----LQLQNVGYLA-GDAKILNNISFSLRAGEFKLITGPSGCGKSTLlkivASLIS---P-TSGTLLFEGEDIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 407 SLSHSALRQGVAMVQQDPVVLADTFLANVTLGRDIseeRVWQALETVQLAELAR-SMSDGIytpLGEQGNNLSVGQKQLL 485
Cdd:PRK10247 73 TLKPEIYRQQVSYCAQTPTLFGDTVYDNLIFPWQI---RNQQPDPAIFLDDLERfALPDTI---LTKNIAELSGGEKQRI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447178945 486 ALARVLVETPQILILDEATASIDSGTEQ---AIQHALaaVREHTTLVV-IAHRLSTIVDADTILVL--HRGQAVE 554
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHnvnEIIHRY--VREQNIAVLwVTHDKDEINHADKVITLqpHAGEMQE 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
341-561 |
1.37e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.39 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsSLSHSALRQ-GVAM 419
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---DVTHRSIQQrDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLADTFLA-NV-----TLGRDISE--ERVWQALETVQLAELARSMSDGIytplgeqgnnlSVGQKQLLALARVL 491
Cdd:PRK11432 83 VFQSYALFPHMSLGeNVgyglkMLGVPKEErkQRVKEALELVDLAGFEDRYVDQI-----------SGGQQQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 492 VETPQILILDEATASIDSGTEQAIQHALAAVREH---TTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQL 561
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfniTSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
340-562 |
1.39e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAYRDDNlVLKNINLSVPSRNFVALVGHTGSGKSTL----ASLLMgyyPLTeGEIRLDGRPLSSLSHSALRQ 415
Cdd:PRK11231 2 TLRTENLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLlkcfARLLT---PQS-GTVFLGDKPISMLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 416 GVAMVQQDPVVLAD-TFLANVTLGR-----------DISEERVWQALETVQLAELA-RSMSDgiytplgeqgnnLSVGQK 482
Cdd:PRK11231 77 RLALLPQHHLTPEGiTVRELVAYGRspwlslwgrlsAEDNARVNQAMEQTRINHLAdRRLTD------------LSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 483 QLLALARVLVETPQILILDEATASIDsgteqaIQHALAAVR-------EHTTLVVIAHRLSTIVD-ADTILVLHRGQAVE 554
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLD------INHQVELMRlmrelntQGKTVVTVLHDLNQASRyCDHLVVLANGHVMA 218
|
....*...
gi 447178945 555 QGTHQQLL 562
Cdd:PRK11231 219 QGTPEEVM 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
340-565 |
1.52e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.79 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAM 419
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDpVVLADTFLANVtlGRDISEERVWQALETVQLAELARsMSDGIYTPLgeqgnNLSVGQKQLLALARVLVETPQILI 499
Cdd:PRK10522 402 VFTD-FHLFDQLLGPE--GKPANPALVEKWLERLKMAHKLE-LEDGRISNL-----KLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 500 LDEATASIDSGTEQAI-QHALAAVREH-TTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQ 565
Cdd:PRK10522 473 LDEWAADQDPHFRREFyQVLLPLLQEMgKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASR 540
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
332-565 |
1.80e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.53 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 332 DDRPLQSGTIEVDNVSFAYRDDNLvLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS 411
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 412 ALRQGVAMV-QQDPVVLADTFLANVTLGR-----------DISEERVWQALETVQLAELARSMSDgiytplgeqgnNLSV 479
Cdd:PRK10575 82 AFARKVAYLpQQLPAAEGMTVRELVAIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVD-----------SLSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 480 GQKQLLALARVLVETPQILILDEATASIDSGTE---QAIQHALAAVREHTTLVVIaHRLSTIVD-ADTILVLHRGQAVEQ 555
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQvdvLALVHRLSQERGLTVIAVL-HDINMAARyCDYLVALRGGEMIAQ 229
|
250
....*....|
gi 447178945 556 GTHQQLLAAQ 565
Cdd:PRK10575 230 GTPAELMRGE 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
342-564 |
1.90e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.46 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 342 EVDNVSfayrdDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSALRQGVAMV 420
Cdd:COG1129 258 EVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 ----QQDPVVLADTFLANVTLGR----------DISEERvwqaletvqlaELARSMSD--GIYTPLGEQG-NNLSVGQKQ 483
Cdd:COG1129 333 pedrKGEGLVLDLSIRENITLASldrlsrggllDRRRER-----------ALAEEYIKrlRIKTPSPEQPvGNLSGGNQQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 484 LLALARVLVETPQILILDEATASIDSGTEQAIQHALAA-VREHTTLVVIAHRLSTIVD-ADTILVLHRGQAV-----EQG 556
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRElAAEGKAVIVISSELPELLGlSDRILVMREGRIVgeldrEEA 481
|
....*...
gi 447178945 557 THQQLLAA 564
Cdd:COG1129 482 TEEAIMAA 489
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
351-552 |
2.66e-17 |
|
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: 80.61 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 351 RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMVQQDPVVLADT 430
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 431 FLANVTLGRDI-SEERVWQALETVQLaelaRSMSDGIYtplgeqgNNLSVGQKQLLALARVLVETPQILILDEATASIDS 509
Cdd:cd03231 90 VLENLRFWHADhSDEQVEEALARVGL----NGFEDRPV-------AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447178945 510 GTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQA 552
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLGFK 201
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
335-576 |
3.34e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 335 PLQSGT---IEVDN--VSFAYR--------DDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPlTEGEIRLD 401
Cdd:PRK15134 267 PLPEPAsplLDVEQlqVAFPIRkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 402 GRPLSSLSHSAL---RQGVAMVQQDPVVLADTFLaNV-------------TLGRDISEERVWQALETVQLAELARSMSDG 465
Cdd:PRK15134 346 GQPLHNLNRRQLlpvRHRIQVVFQDPNSSLNPRL-NVlqiieeglrvhqpTLSAAQREQQVIAVMEEVGLDPETRHRYPA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 466 iytplgeqgnNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTL--VVIAHRLStIVDA-- 541
Cdd:PRK15134 425 ----------EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLH-VVRAlc 493
|
250 260 270
....*....|....*....|....*....|....*
gi 447178945 542 DTILVLHRGQAVEQGTHQQLLAAQGrywQMYQLQL 576
Cdd:PRK15134 494 HQVIVLRQGEVVEQGDCERVFAAPQ---QEYTRQL 525
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
348-563 |
5.16e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.59 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 348 FAYRDDNlVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL--SSLSHSALRQGVAMVQQDPv 425
Cdd:PRK13638 9 FRYQDEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQDP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 426 vlaDTFLANVTLGRDISeervwQALETVQLA--ELARSMSDGIyTPLGEQG------NNLSVGQKQLLALARVLVETPQI 497
Cdd:PRK13638 87 ---EQQIFYTDIDSDIA-----FSLRNLGVPeaEITRRVDEAL-TLVDAQHfrhqpiQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 498 LILDEATASID-SGTEQAIQHALAAVREHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLA 563
Cdd:PRK13638 158 LLLDEPTAGLDpAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-551 |
5.17e-17 |
|
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: 79.01 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 342 EVDNVSFAYRddnlvLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSALRQGVAMV 420
Cdd:cd03215 6 EVRGLSVKGA-----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 qqdpvvladtflanvtlgrdiSEERVWQALetVQLAELARSMSDGIYtplgeqgnnLSVGQKQLLALARVLVETPQILIL 500
Cdd:cd03215 81 ---------------------PEDRKREGL--VLDLSVAENIALSSL---------LSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447178945 501 DEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGlCDRILVMYEGR 181
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-562 |
7.08e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.85 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLtEGEIRLDGRPL--------SSLSHSA 412
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRVEffnqniyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 413 LRQGVAMVQQDPVVLADTFLANVTLGRDISEERVWQALE-TVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVL 491
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDdIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 492 VETPQILILDEATASIDSGTEQAIQHAL--AAVREHTTLVVIAHRLSTIVD-ADTILVLHR-----GQAVEQGTHQQLL 562
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGLTKKIF 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
357-553 |
7.37e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 83.63 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSALRQGVAMVQQD-PVVLADTFLAN 434
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 435 VTLGRD------ISEERVWQALETVqLAELarsmsdGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASId 508
Cdd:PRK10982 94 MWLGRYptkgmfVDQDKMYRDTKAI-FDEL------DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447178945 509 sgTEQAIQHALAAVRE----HTTLVVIAHRLSTIVD-ADTILVLHRGQAV 553
Cdd:PRK10982 166 --TEKEVNHLFTIIRKlkerGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
333-536 |
7.84e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.86 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 333 DRPLqsgtIEVDNVSFAYRDDNL---VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS 409
Cdd:PRK11629 2 NKIL----LQCDNLCKRYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 410 HSA---LR-QGVAMVQQDPVVLAD-TFLANVTLGRDISEERVWQALETvqlaelARSM--SDGIYTPLGEQGNNLSVGQK 482
Cdd:PRK11629 78 SAAkaeLRnQKLGFIYQFHHLLPDfTALENVAMPLLIGKKKPAEINSR------ALEMlaAVGLEHRANHRPSELSGGER 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 483 QLLALARVLVETPQILILDEATASIDSGTEQAIQHALAA--VREHTTLVVIAHRLS 536
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
341-551 |
8.57e-17 |
|
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: 77.49 E-value: 8.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRldgrplsslSHSALRqgVAMV 420
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------WGSTVK--IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQdpvvladtflanvtlgrdiseervwqaletvqlaelarsmsdgiytplgeqgnnLSVGQKQLLALARVLVETPQILIL 500
Cdd:cd03221 69 EQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447178945 501 DEATASIDSGTEQAIQHALAAvrEHTTLVVIAH-R--LSTIvdADTILVLHRGQ 551
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
357-553 |
2.34e-16 |
|
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: 82.18 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLT--EGEIRLDGRPL--SSLSHSAlRQGVAMVQQDPVVLAD-TF 431
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLkaSNIRDTE-RAGIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 432 LANVTLGRDISEE--RVWQALETVQLAELARSMS---DGIYTPLGEQGnnlsVGQKQLLALARVLVETPQILILDEATAS 506
Cdd:TIGR02633 96 AENIFLGNEITLPggRMAYNAMYLRAKNLLRELQldaDNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447178945 507 IdsgTEQAIQHALAAVRE----HTTLVVIAHRLSTI-VDADTILVLHRGQAV 553
Cdd:TIGR02633 172 L---TEKETEILLDIIRDlkahGVACVYISHKLNEVkAVCDTICVIRDGQHV 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
355-561 |
2.34e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 79.26 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 355 LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL-SHSALRQGVAMVQQD-------PVV 426
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVRTFQHvrlfremTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 427 ----------LADTFLANV--TLGRDISE----ERVWQALETVQLAELArsmsdgiytplGEQGNNLSVGQKQLLALARV 490
Cdd:PRK11300 99 enllvaqhqqLKTGLFSGLlkTPAFRRAEsealDRAATWLERVGLLEHA-----------NRQAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447178945 491 LVETPQILILDEATASIDSGTEQAIQHALAAVREH--TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQL 561
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhnVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
320-561 |
3.82e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 80.26 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 320 ELMDGPRQQYGNDDRPLqsgtIEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIR 399
Cdd:PRK11607 3 DAIPRPQAKTRKALTPL----LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 400 LDGRPLSSLShSALRQGVAMVQQDPVVLADTFLANVTLG-------RDISEERVWQALETVQLAELARsmsdgiytplgE 472
Cdd:PRK11607 78 LDGVDLSHVP-PYQRPINMMFQSYALFPHMTVEQNIAFGlkqdklpKAEIASRVNEMLGLVHMQEFAK-----------R 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 473 QGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREH--TTLVVIAH-RLSTIVDADTILVLHR 549
Cdd:PRK11607 146 KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIMNR 225
|
250
....*....|..
gi 447178945 550 GQAVEQGTHQQL 561
Cdd:PRK11607 226 GKFVQIGEPEEI 237
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
43-318 |
5.36e-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: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 43 PLLISYFIDNMVAKNNLPL--KVVAGLAAAYVGLQLFA---AGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFD 117
Cdd:cd18554 19 PLILKYIVDDVIQGSSLTLdeKVYKLFTIIGIMFFIFLilrPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 118 TQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPV-VLVVMVIYQRYSTPIVRRV 196
Cdd:cd18554 99 NNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFyILAVKYFFGRLRKLTKERS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 197 RAyLADINDGFNEIINGMSVIQQF----RQQARFGERMGE-ASRSHYMARMQTLRLDGFLLRPLLslfsslilcGLLMLF 271
Cdd:cd18554 179 QA-LAEVQGFLHERIQGMSVIKSFalekHEQKQFDKRNGHfLTRALKHTRWNAKTFSAVNTITDL---------APLLVI 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 447178945 272 GFSA----SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18554 249 GFAAylviEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
340-524 |
5.81e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.27 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAyRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAM 419
Cdd:PRK09536 3 MIDVSDLSVE-FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLAD-TFLANVTLGR-----------DISEERVWQALETVQLAELA-RSMSdgiytplgeqgnNLSVGQKQLLA 486
Cdd:PRK09536 82 VPQDTSLSFEfDVRQVVEMGRtphrsrfdtwtETDRAAVERAMERTGVAQFAdRPVT------------SLSGGERQRVL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447178945 487 LARVLVETPQILILDEATASIDsgteqaIQHA---LAAVRE 524
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLD------INHQvrtLELVRR 184
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
341-556 |
6.16e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 6.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNlVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQ-GVAM 419
Cdd:PRK15439 12 LCARSISKQYSGVE-VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLAD-TFLANVTLG---RDISEERVwQALetvqLAELARSMSdgiytpLGEQGNNLSVGQKQLLALARVLVETP 495
Cdd:PRK15439 91 VPQEPLLFPNlSVKENILFGlpkRQASMQKM-KQL----LAALGCQLD------LDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 496 QILILDEATASIDSG-TEQAIQHALAAVREHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:PRK15439 160 RILILDEPTASLTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSG 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
341-556 |
6.47e-16 |
|
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: 77.37 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYR--------------------DDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL 400
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 401 DG-RPLSSLSHSALRQGVAMVQQDPVV----LADTFLANVTLgRDISEERVWQAL-ETVQLAELARSMsdgiYTPLgeqg 474
Cdd:cd03267 81 AGlVPWKRRKKFLRRIGVVFGQKTQLWwdlpVIDSFYLLAAI-YDLPPARFKKRLdELSELLDLEELL----DTPV---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 475 NNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHAL-AAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:cd03267 152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLkEYNRERgTTVLLTSHYMKDIEAlARRVLVIDKGR 231
|
....*
gi 447178945 552 AVEQG 556
Cdd:cd03267 232 LLYDG 236
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
357-556 |
7.73e-16 |
|
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: 77.12 E-value: 7.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL--------------SSLSHSALRQGVAMVQQ 422
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepgpdrmvvfqnySLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 423 DpvVLADtflanvtLGRDISEERVWQALETVQLAELARSMSDgiytplgeqgnNLSVGQKQLLALARVLVETPQILILDE 502
Cdd:TIGR01184 81 R--VLPD-------LSKSERRAIVEEHIALVGLTEAADKRPG-----------QLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 503 ATASIDSGTEQAIQHALAAVRE--HTTLVVIAHRL-STIVDADTILVLHRGQAVEQG 556
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
27-322 |
8.08e-16 |
|
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: 78.31 E-value: 8.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 27 IAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVVAGLaaaYVGLQLFA-AGLHYAQSLLFNRAAVGVVQQLRTDVM 105
Cdd:cd18580 3 LLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGV---YAALLVLAsVLLVLLRWLLFVLAGLRASRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 106 DAALRQPLSEFDTQPVGQVISRVTNDTEVI-RDLYVTVVATVLRSAALVGAMLVAMFSLDWrMALVaimiFPVVLVVMVI 184
Cdd:cd18580 80 RSVLRAPMSFFDTTPSGRILNRFSKDIGLIdEELPLALLDFLQSLFSVLGSLIVIAIVSPY-FLIV----LPPLLVVYYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 185 YQRYSTPIVRRVR----AYLADINDGFNEIINGMSVIQQFRQQARFGERMGE----ASRSHYM----ARMQTLRLDGFLL 252
Cdd:cd18580 155 LQRYYLRTSRQLRrlesESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRlldaSQRAFYLllavQRWLGLRLDLLGA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 253 RPLlslfsslilcGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERVFELM 322
Cdd:cd18580 235 LLA----------LVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
341-564 |
8.21e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.52 E-value: 8.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYR---DDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYP-----LTEGEIRLDGRPLSSLSHSA 412
Cdd:PRK15134 6 LAIENLSVAFRqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 413 LRQ----GVAMVQQDPVV-----------LADTFLANVTLGRDISEERVWQALETVQLAELARSMSDgiyTPlgeqgNNL 477
Cdd:PRK15134 86 LRGvrgnKIAMIFQEPMVslnplhtlekqLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTD---YP-----HQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 478 SVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVRE--HTTLVVIAHRLStIVD--ADTILVLHRGQAV 553
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLS-IVRklADRVAVMQNGRCV 236
|
250
....*....|.
gi 447178945 554 EQGTHQQLLAA 564
Cdd:PRK15134 237 EQNRAATLFSA 247
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
341-535 |
1.13e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.12 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNlVLKNINLSVPSRNFVALVGHTGSGKSTLASLL--MG-YYP--LTEGEIRLDGRPLSSLSHSA--L 413
Cdd:PRK14239 6 LQVSDLSVYYNKKK-ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdLNPevTITGSIVYNGHNIYSPRTDTvdL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQGVAMVQQDPVVLADTFLANVTLGRDISEERVWQAL-ETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLV 492
Cdd:PRK14239 85 RKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLdEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447178945 493 ETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRL 535
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
340-532 |
1.13e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSfAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAm 419
Cdd:PRK13539 2 MLEGEDLA-CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 vQQDPVVLADTFLANVTLGRDI---SEERVWQALETVQLAELArsmsdgiYTPlgeqGNNLSVGQKQLLALARVLVETPQ 496
Cdd:PRK13539 80 -HRNAMKPALTVAENLEFWAAFlggEELDIAAALEAVGLAPLA-------HLP----FGYLSAGQKRRVALARLLVSNRP 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 447178945 497 ILILDEATASIDSGTEQAIQHALAAVREHTTLVVIA 532
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
355-556 |
1.18e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 76.54 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 355 LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMG---YYPLTEGEIRLDGRPLSSlshSALRQGVAMVQQDPVVLAD-- 429
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGlt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 430 -----TFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYTPlgeqgnNLSVGQKQLLALARVLVETPQILILDEAT 504
Cdd:cd03234 98 vretlTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVK------GISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447178945 505 ASIDSGTEQAIQHALA--AVREHTTLVVIAHRLSTIVDA-DTILVLHRGQAVEQG 556
Cdd:cd03234 172 SGLDSFTALNLVSTLSqlARRNRIVILTIHQPRSDLFRLfDRILLLSSGEIVYSG 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
356-564 |
1.23e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 78.41 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 356 VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYP----LTEGEIRLDGRPLSSLSHSALRQ----GVAMVQQDPVVL 427
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERRKiigrEIAMIFQEPSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 428 ADtflANVTLGRDISEE--------RVWQ--------ALETVQ----------LAELARSMSDGIytplgeqgnnlsvGQ 481
Cdd:COG4170 102 LD---PSAKIGDQLIEAipswtfkgKWWQrfkwrkkrAIELLHrvgikdhkdiMNSYPHELTEGE-------------CQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 482 KQLLALArvLVETPQILILDEATASIDSGTEQAIQHALAAVRE--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTH 558
Cdd:COG4170 166 KVMIAMA--IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLESISQwADTITVLYCGQTVESGPT 243
|
....*.
gi 447178945 559 QQLLAA 564
Cdd:COG4170 244 EQILKS 249
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
340-576 |
1.34e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.51 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAYRD----DNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSA--- 412
Cdd:PRK13646 2 TIRFDNVSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 413 -LRQGVAMVQQDPVvlADTFLANV---------TLGRDISE--ERVWQALetVQLAELARSMSDgiyTPLgeqgnNLSVG 480
Cdd:PRK13646 82 pVRKRIGMVFQFPE--SQLFEDTVereiifgpkNFKMNLDEvkNYAHRLL--MDLGFSRDVMSQ---SPF-----QMSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 481 QKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAA--VREHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGT 557
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTS 229
|
250
....*....|....*....
gi 447178945 558 HQQLLaAQGRYWQMYQLQL 576
Cdd:PRK13646 230 PKELF-KDKKKLADWHIGL 247
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
25-247 |
1.38e-15 |
|
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: 77.45 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAevsgplLISYFIDNMVAKNnLPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDV 104
Cdd:cd18584 4 LGLLAALLIIAQAW------LLARIIAGVFLEG-AGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 105 MDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVI 184
Cdd:cd18584 77 LARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMIL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 185 YQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRL 247
Cdd:cd18584 157 IGKAAQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRV 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
356-555 |
1.77e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.97 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 356 VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SALR-QGVAMVQQdpvvladTF 431
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRaKHVGFVFQ-------SF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 432 LANVTLgrdiseervwQALETVQLAELARSMSD--------------GIYTPLGEQGNNLSVGQKQLLALARVLVETPQI 497
Cdd:PRK10584 98 MLIPTL----------NALENVELPALLRGESSrqsrngakalleqlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 498 LILDEATASIDSGTEQAIQHALAAV-REH-TTLVVIAHRLSTIVDADTILVLHRGQAVEQ 555
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLnREHgTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
338-557 |
1.86e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 338 SGTIEVDNVSFAYR---------------------DDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEG 396
Cdd:COG1134 2 SSMIEVENVSKSYRlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 397 EIRLDGR--PLSSLS---HSAL--RQGVamvqqdpvvladtFLANVTLG---RDIsEERVwqaLETVQLAELarsmSDGI 466
Cdd:COG1134 82 RVEVNGRvsALLELGagfHPELtgRENI-------------YLNGRLLGlsrKEI-DEKF---DEIVEFAEL----GDFI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 467 YTPLGeqgnNLSVGQKQLLALARVLVETPQILILDEATASIDsgteQAIQH-ALAAVRE----HTTLVVIAHRLSTIVD- 540
Cdd:COG1134 141 DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD----AAFQKkCLARIRElresGRTVIFVSHSMGAVRRl 212
|
250
....*....|....*..
gi 447178945 541 ADTILVLHRGQAVEQGT 557
Cdd:COG1134 213 CDRAIWLEKGRLVMDGD 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
340-559 |
2.72e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.82 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLmgyyPLTE----GEIRLDGRPLSsLSHS---- 411
Cdd:PRK11124 2 SIQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL----NLLEmprsGTLNIAGNHFD-FSKTpsdk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 412 ---ALRQGVAMV-QQDPVVLADTFLANVT--------LGRDISEERVWQALETVQLAELARSMsdgiytPLgeqgnNLSV 479
Cdd:PRK11124 76 airELRRNVGMVfQQYNLWPHLTVQQNLIeapcrvlgLSKDQALARAEKLLERLRLKPYADRF------PL-----HLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 480 GQKQLLALARVLVETPQILILDEATASIDSG-TEQ--AIQHALAAVreHTTLVVIAHRlstiVD-----ADTILVLHRGQ 551
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQivSIIRELAET--GITQVIVTHE----VEvarktASRVVYMENGH 218
|
....*...
gi 447178945 552 AVEQGTHQ 559
Cdd:PRK11124 219 IVEQGDAS 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
316-564 |
2.98e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.51 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 316 ERVFELMDGPR--QQYGNDDRPLQSGTIEVDNVSFAYrddnlvLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPL 393
Cdd:PRK10762 231 DSLIEMMVGRKleDQYPRLDKAPGEVRLKVDNLSGPG------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 394 TEGEIRLDGRPLSSLS-HSALRQGVAMVQQDP----VVLADTFLANVTLG--RDISEE--RVWQALETVQLAELARSMSd 464
Cdd:PRK10762 305 TSGYVTLDGHEVVTRSpQDGLANGIVYISEDRkrdgLVLGMSVKENMSLTalRYFSRAggSLKHADEQQAVSDFIRLFN- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 465 gIYTPLGEQG-NNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVR-EHTTLVVIAHRLSTIVD-A 541
Cdd:PRK10762 384 -IKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmS 462
|
250 260
....*....|....*....|....*...
gi 447178945 542 DTILVLHRGQ-----AVEQGTHQQLLAA 564
Cdd:PRK10762 463 DRILVMHEGRisgefTREQATQEKLMAA 490
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
342-564 |
3.54e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.43 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 342 EVDNVSfAYRDDNLVLK---NINLSVPSRNFVALVGHTGSGKSTLASLLMGYYP-LTEGEIRLDGRPLS-SLSHSALRQG 416
Cdd:PRK13549 261 EVRNLT-AWDPVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKiRNPQQAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 417 VAMVQQDP----VVLADTFLANVTL---GRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNnLSVGQKQLLALAR 489
Cdd:PRK13549 340 IAMVPEDRkrdgIVPVMGVGKNITLaalDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIAR-LSGGNQQKAVLAK 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 490 VLVETPQILILDEATASIDSGTEQAIQHALAA-VREHTTLVVIAHRLSTIVD-ADTILVLH----RGQAVEQG-THQQLL 562
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVLGlSDRVLVMHegklKGDLINHNlTQEQVM 498
|
..
gi 447178945 563 AA 564
Cdd:PRK13549 499 EA 500
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
341-563 |
3.56e-15 |
|
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: 75.27 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDdNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSALRQGVAM 419
Cdd:cd03218 1 LRAENLSKRYGK-RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLAD-TFLANV-------TLGRDISEERVWQALETVQLAELARSMsdgiytplgeqGNNLSVGQKQLLALARVL 491
Cdd:cd03218 80 LPQEASIFRKlTVEENIlavleirGLSKKEREEKLEELLEEFHITHLRKSK-----------ASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447178945 492 VETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIA-HRLSTIVD-ADTILVLHRGQAVEQGTHQQLLA 563
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
68-323 |
3.89e-15 |
|
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: 76.72 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 68 AAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDtQP---VGQVISRVTNDTEVIRDLYVTVVA 144
Cdd:cd18578 55 ALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFD-DPensTGALTSRLSTDASDVRGLVGDRLG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 145 TVLRS-AALVGAMLVAmFSLDWRMALVAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQ 223
Cdd:cd18578 134 LILQAiVTLVAGLIIA-FVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 224 ARFGERMGEASRSHYMARMQTLRLDGFllrpllslfsslilcgllmLFGFSASGTIevgVLYAFISYLGRLnepLI---E 300
Cdd:cd18578 213 DYFLEKYEEALEEPLKKGLRRALISGL-------------------GFGLSQSLTF---FAYALAFWYGGR---LVangE 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 447178945 301 LTTQQAM----------------------LQQAVVAGERVFELMD 323
Cdd:cd18578 268 YTFEQFFivfmalifgaqsagqafsfapdIAKAKAAAARIFRLLD 312
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
341-535 |
4.24e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.59 E-value: 4.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSfAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGeIRLDGRPL--------SSLSHSA 412
Cdd:PRK14243 11 LRTENLN-VYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTfhgknlyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 413 LRQGVAMVQQDPVVLADTFLANVTLGRDIS------EERVWQALETVQLAelarsmsDGIYTPLGEQGNNLSVGQKQLLA 486
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYGARINgykgdmDELVERSLRQAALW-------DEVKDKLKQSGLSLSGGQQQRLC 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447178945 487 LARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRL 535
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
345-550 |
4.86e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.99 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 345 NVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSalRQGVAMVQQDP 424
Cdd:PRK11000 8 NVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 425 VVLADTFLA-NVTLGRDIS-------EERVWQALETVQLAELarsmsdgiytpLGEQGNNLSVGQKQLLALARVLVETPQ 496
Cdd:PRK11000 85 ALYPHLSVAeNMSFGLKLAgakkeeiNQRVNQVAEVLQLAHL-----------LDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 497 ILILDEATASIDSG--TEQAIQHALAAVREHTTLVVIAH-RLSTIVDADTILVLHRG 550
Cdd:PRK11000 154 VFLLDEPLSNLDAAlrVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAG 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
340-564 |
5.03e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.17 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAYRDdNLVLKNINLSVPSRNFVALVGHTGSGKST-LASLLMGYYP----LTEGEIRLDG-RPLSSLSH--S 411
Cdd:PRK11264 3 AIEVKNLVKKFHG-QTVLHGIDLEVKPGEVVAIIGPSGSGKTTlLRCINLLEQPeagtIRVGDITIDTaRSLSQQKGliR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 412 ALRQGVAMVQQDPVVLAD-TFLANVTLG--------RDISEERVWQALETVQLAELARSMSdgiytplgeqgNNLSVGQK 482
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHrTVLENIIEGpvivkgepKEEATARARELLAKVGLAGKETSYP-----------RRLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 483 QLLALARVLVETPQILILDEATASIDSgteQAIQHALAAVR----EHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGT 557
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGP 227
|
....*..
gi 447178945 558 HQQLLAA 564
Cdd:PRK11264 228 AKALFAD 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
341-563 |
5.97e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.54 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGY--YPLTEGEI----------------RLDG 402
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 403 RP-----------------LSSLSHSALRQGVAMVQQDPVVL--ADTFLANV-----TLGRDiSEERVWQALETVQLAEL 458
Cdd:TIGR03269 80 EPcpvcggtlepeevdfwnLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVlealeEIGYE-GKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 459 ARSMSdgiytplgEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHAL--AAVREHTTLVVIAHRLS 536
Cdd:TIGR03269 159 SHRIT--------HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*...
gi 447178945 537 TIVD-ADTILVLHRGQAVEQGTHQQLLA 563
Cdd:TIGR03269 231 VIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
341-554 |
6.13e-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: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVP--SRnfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLdgrplsslsHSALRQGVa 418
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDrgDR--IGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---------GETVKIGY- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 419 mVQQDPVVLADtflanvtlgrdisEERVWQALEtvQLAELARSMS------------DGIYTPLGeqgnNLSVGQKQLLA 486
Cdd:COG0488 383 -FDQHQEELDP-------------DKTVLDELR--DGAPGGTEQEvrgylgrflfsgDDAFKPVG----VLSGGEKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447178945 487 LARVLVETPQILILDEATASIDSGTEQAIQHALAavrEHT-TLVVIAH-R--LSTIvdADTILVLHRGQAVE 554
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD---DFPgTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
351-551 |
6.17e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.68 E-value: 6.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 351 RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQ--------GVamvqq 422
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllylghqpGI----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 423 DPVVLADTFLA-NVTLGRDISEERVWQALETVQLAE----LARSmsdgiytplgeqgnnLSVGQKQLLALARVLVETPQI 497
Cdd:PRK13538 86 KTELTALENLRfYQRLHGPGDDEALWEALAQVGLAGfedvPVRQ---------------LSAGQQRRVALARLWLTRAPL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 498 LILDEATASID-SGTEQAIQHaLAAVREHTTLVVIA--HRLStiVDADTILVLHRGQ 551
Cdd:PRK13538 151 WILDEPFTAIDkQGVARLEAL-LAQHAEQGGMVILTthQDLP--VASDKVRKLRLGQ 204
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
356-550 |
7.01e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 78.28 E-value: 7.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 356 VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDgrplsslshsalrQGVAMVQQDPVVLADTFLANV 435
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 436 TLGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAI 515
Cdd:PTZ00243 742 LFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447178945 516 QH-----ALAAvrehTTLVVIAHRLSTIVDADTILVLHRG 550
Cdd:PTZ00243 822 VEecflgALAG----KTRVLATHQVHVVPRADYVVALGDG 857
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
356-547 |
7.54e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.74 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 356 VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslSHSALRqGVaMVQQDPVVLADTFLANV 435
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAER-GV-VFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 436 TLGRDIS----EERVWQALETVQLAELARSMSDGIYtplgeqgnNLSVGQKQLLALARVLVETPQILILDEATASIDSGT 511
Cdd:PRK11248 92 AFGLQLAgvekMQRLEIAHQMLKKVGLEGAEKRYIW--------QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 447178945 512 EQAIQHALAAVREHT--TLVVIAHRLSTIVDADTILVL 547
Cdd:PRK11248 164 REQMQTLLLKLWQETgkQVLLITHDIEEAVFMATELVL 201
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
28-318 |
8.22e-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: 75.04 E-value: 8.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 28 AVLMMWVAAAAEVSGPLLISYFIDNMVAKNNL-----PLKVVAGLAAAyvglQLFAAGLhyaQSLLFNRAAVGVVQQLRT 102
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQdkfsrAIIIMGLLAIA----SSVAAGI---RGGLFTLAMARLNIRIRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 103 DVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVM 182
Cdd:cd18784 74 LLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 183 VIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQArfgermGEASRshYMARMQ-TLRLDGFLLRPLLSLFSS 261
Cdd:cd18784 154 KVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANED------GEANR--YSEKLKdTYKLKIKEALAYGGYVWS 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447178945 262 LILCGLLMLFG-------FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18784 226 NELTELALTVStlyygghLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
28-318 |
1.18e-14 |
|
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: 74.98 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 28 AVLMMWVAAAAEVSGPLLISYFIDNMV---------AKNNLpLKVVAGLAAAYVGLQLFAAglhyAQSLLFNRAAVGVVQ 98
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTnhsgsggeeALRAL-NQAVLILLGVVLIGSIATF----LRSWLFTLAGERVVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 99 QLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVV 178
Cdd:cd18780 76 RLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 179 LVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEA-SRSHYMARMQTLRLDGFLlrplls 257
Cdd:cd18780 156 SIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKiNESYLLGKKLARASGGFN------ 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447178945 258 lfsslilcGLLMLFGFSA-------------SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18780 230 --------GFMGAAAQLAivlvlwyggrlviDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
341-561 |
1.34e-14 |
|
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: 73.17 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrpLSSLSHSA-LRQGVAM 419
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPReVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLAD-TFLANVT-------LGRDISEERVWQALETVQLAELArsmsdgiytplGEQGNNLSVGQKQLLALARVL 491
Cdd:cd03265 78 VFQDLSVDDElTGWENLYiharlygVPGAERRERIDELLDFVGLLEAA-----------DRLVKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 492 VETPQILILDEATASIDSGTEQAI-QHALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQL 561
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVwEYIEKLKEEFgMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
356-554 |
1.78e-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: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 356 VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMVqqDPVVLADTFLANV 435
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRK--GDFKDAVELLNAV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 436 TLGrdiseervwqaleTVQLaeLARSMSdgiytplgeqgnNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAI 515
Cdd:COG2401 123 GLS-------------DAVL--WLRRFK------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447178945 516 QHALA-AVREH-TTLVVIAHRlSTIVDA---DTILVLHRGQAVE 554
Cdd:COG2401 176 ARNLQkLARRAgITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
334-557 |
2.11e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.50 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 334 RPLQSGTI-EVDNVSFAYRDDN----LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLD------- 401
Cdd:PRK13631 14 NPLSDDIIlRVKNLYCVFDEKQenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 402 -GRPLSSLSHSA--------LRQGVAMVQQDP-------VVLADTFLANVTLGRDISEERVWQA--LETVQLAE--LARS 461
Cdd:PRK13631 94 kNNHELITNPYSkkiknfkeLRRRVSMVFQFPeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKfyLNKMGLDDsyLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 462 msdgiytPLGeqgnnLSVGQKQLLALARVLVETPQILILDEATASID-SGTEQAIQHALAAVREHTTLVVIAHRLSTIVD 540
Cdd:PRK13631 174 -------PFG-----LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpKGEHEMMQLILDAKANNKTVFVITHTMEHVLE 241
|
250
....*....|....*...
gi 447178945 541 -ADTILVLHRGQAVEQGT 557
Cdd:PRK13631 242 vADEVIVMDKGKILKTGT 259
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
43-318 |
3.68e-14 |
|
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: 73.40 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 43 PLLISYFIDNMVAKNNLPLKVVagLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVG 122
Cdd:cd18782 22 PLLFQVIIDKVLVQQDLATLYV--IGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 123 QVISRVtNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLAD 202
Cdd:cd18782 100 ELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 203 INDGFNEIINGMSVIQ----QFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSLILCGLLMLFGfsasGT 278
Cdd:cd18782 179 TQSYLVESLTGIQTVKaqnaELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLR----GE 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 447178945 279 IEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18782 255 LTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
341-563 |
4.21e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.22 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRD-DNLVLK---NINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIR-------LDGRPLSSLS 409
Cdd:TIGR03269 280 IKVRNVSKRYISvDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 410 HSALRQGVAMVQQDPVVLAD-TFLANVT--LGRDISEE-RVWQALETVQLAELARSMSDGIytpLGEQGNNLSVGQKQLL 485
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPHrTVLDNLTeaIGLELPDElARMKAVITLKMVGFDEEKAEEI---LDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 486 ALARVLVETPQILILDEATASIDSGTEQAIQHALAAVRE--HTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLL 562
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
.
gi 447178945 563 A 563
Cdd:TIGR03269 517 E 517
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
343-504 |
4.44e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 343 VDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshsaLRqgVAMVQQ 422
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 423 DPVVLAD-TFLANVTLGRdiseERVWQALETVQLAELARSMSDGIYTPLGE---------------------QG------ 474
Cdd:COG0488 69 EPPLDDDlTVLDTVLDGD----AELRALEAELEELEAKLAEPDEDLERLAElqeefealggweaearaeeilSGlgfpee 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 447178945 475 ------NNLSVGQKQLLALARVLVETPQILILDEAT 504
Cdd:COG0488 145 dldrpvSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
373-561 |
4.47e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.59 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 373 VGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---ALRQGVAMVQQDPvvladtfLANV----TLGRDISEE- 444
Cdd:PRK15079 53 VGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDP-------LASLnprmTIGEIIAEPl 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 445 RVWQA-LETVQLAELARSMSD--GIYTPL-GEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALA 520
Cdd:PRK15079 126 RTYHPkLSRQEVKDRVKAMMLkvGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQ 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447178945 521 AVREHT--TLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQL 561
Cdd:PRK15079 206 QLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
316-564 |
4.93e-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: 74.86 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 316 ERVFELMDGP--RQQYGNDDRPLQSGTIEVDNVSfAYRDDNLVLK---NINLSVPSRNFVALVGHTGSGKSTLASLLMGY 390
Cdd:TIGR02633 231 DDIITMMVGReiTSLYPHEPHEIGDVILEARNLT-CWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 391 YP-LTEGEIRLDGRPLSSLS-HSALRQGVAMVQQDP----VVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSD 464
Cdd:TIGR02633 310 YPgKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQR 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 465 ------GIYTPLGeqgnNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAA-VREHTTLVVIAHRLST 537
Cdd:TIGR02633 390 lkvktaSPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAE 465
|
250 260 270
....*....|....*....|....*....|...
gi 447178945 538 IVD-ADTILVLHRGQA----VEQG-THQQLLAA 564
Cdd:TIGR02633 466 VLGlSDRVLVIGEGKLkgdfVNHAlTQEQVLAA 498
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
354-562 |
6.16e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.91 E-value: 6.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 354 NLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQ----GVAMVQQDPVVLAD 429
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 430 -TFLANVTLGRDIS-------EERVWQALETVQLAELARSMSDgiytplgeqgnNLSVGQKQLLALARVLVETPQILILD 501
Cdd:PRK10070 121 mTVLDNTAFGMELAginaeerREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447178945 502 EATASIDSGTEQAIQHALAAV--REHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLL 562
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
338-581 |
8.27e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.35 E-value: 8.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 338 SGTIEVDNVSFAYRDDN----LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGE-IRLDGRPLSSLSH-- 410
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtIVGDYAIPANLKKik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 411 --SALRQGVAMVQQDP-------VVLADTFLANVTLGRDISE--ERVWQALETVQLAE--LARSmsdgiytPLgeqgnNL 477
Cdd:PRK13645 84 evKRLRKEIGLVFQFPeyqlfqeTIEKDIAFGPVNLGENKQEayKKVPELLKLVQLPEdyVKRS-------PF-----EL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 478 SVGQKQLLALARVLVETPQILILDEATASID-SGTEQAIQHALAAVREHTT-LVVIAHRLSTIVD-ADTILVLHRGQAVE 554
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpKGEEDFINLFERLNKEYKKrIIMVTHNMDQVLRiADEVIVMHEGKVIS 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 447178945 555 QG------THQQLLAA-----QGRYWQMYQLQLAGEEL 581
Cdd:PRK13645 232 IGspfeifSNQELLTKieidpPKLYQLMYKLKNKGIDL 269
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
341-561 |
9.62e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.72 E-value: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAyRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAL---RQGV 417
Cdd:PRK11831 8 VDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVVLAD-TFLANVT--------LGRDISEERVWQALETVQLAELARSMSdgiytplgeqgNNLSVGQKQLLALA 488
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAyplrehtqLPAPLLHSTVMMKLEAVGLRGAAKLMP-----------SELSGGMARRAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 489 RVLVETPQILILDEATASIDSGTE-------QAIQHALAavrehTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQ 560
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMgvlvkliSELNSALG-----VTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQA 230
|
.
gi 447178945 561 L 561
Cdd:PRK11831 231 L 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
340-563 |
1.01e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.08 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAYRDDNLVlKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSALRQGVA 418
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVV-EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 419 MVQQDPVVLA-----DTFLANVTLGRDISEE----RVWQALETVQLAELARSMsdgiytplgeqGNNLSVGQKQLLALAR 489
Cdd:PRK10895 82 YLPQEASIFRrlsvyDNLMAVLQIRDDLSAEqredRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 490 VLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIA-HRLSTIVDA-DTILVLHRGQAVEQGTHQQLLA 563
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVcERAYIVSQGHLIAHGTPTEILQ 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
341-562 |
1.04e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.89 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrpLSSLSHSA----LRQG 416
Cdd:PRK09493 2 IEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVderlIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 417 VAMV-QQDPVVLADTFLANVTLG--------RDISEERVWQALETVQLAELArsmsdgiytplGEQGNNLSVGQKQLLAL 487
Cdd:PRK09493 79 AGMVfQQFYLFPHLTALENVMFGplrvrgasKEEAEKQARELLAKVGLAERA-----------HHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 488 ARVLVETPQILILDEATASIDSGTEQ---AIQHALAavREHTTLVVIAHRLSTIVDADTILV-LHRGQAVEQGTHQQLL 562
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHevlKVMQDLA--EEGMTMVIVTHEIGFAEKVASRLIfIDKGRIAEDGDPQVLI 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
343-564 |
1.38e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 343 VDNVSFAYRDDNL---VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR----------PLSSLS 409
Cdd:PRK10261 15 VENLNIAFMQEQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 410 HSALRQ----GVAMVQQDPVvladTFLANV-TLGRDISEE-RVWQALETVQLAELARSMSDGIYTP-----LGEQGNNLS 478
Cdd:PRK10261 95 AAQMRHvrgaDMAMIFQEPM----TSLNPVfTVGEQIAESiRLHQGASREEAMVEAKRMLDQVRIPeaqtiLSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 479 VGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVV--IAHRLSTIVD-ADTILVLHRGQAVEQ 555
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVAEiADRVLVMYQGEAVET 250
|
....*....
gi 447178945 556 GTHQQLLAA 564
Cdd:PRK10261 251 GSVEQIFHA 259
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
341-515 |
1.56e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 70.29 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSA---LRQGV 417
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVVLAD-TFLANVTL--------GRDIsEERVWQALETVQLAELARSMsdgiytPLgeqgnNLSVGQKQLLALA 488
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIpliiagasGDDI-RRRVSAALDKVGLLDKAKNF------PI-----QLSGGEQQRVGIA 149
|
170 180
....*....|....*....|....*..
gi 447178945 489 RVLVETPQILILDEATASIDSGTEQAI 515
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGI 176
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
360-557 |
1.64e-13 |
|
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: 74.28 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 360 INLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSALRQGVAMVQQDPVVLADTFLANVTLGR 439
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 440 DISEERVWqalETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHAL 519
Cdd:TIGR01257 1028 AQLKGRSW---EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|....*....
gi 447178945 520 AAVREHTTLVVIAHRLSTI-VDADTILVLHRGQAVEQGT 557
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGT 1143
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
357-554 |
2.24e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLT--EGEIRLDGRP--LSSLSHSAlRQGVAMVQQDpvvladtfL 432
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVcrFKDIRDSE-ALGIVIIHQE--------L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 433 A---------NVTLGRDISEERV--WQA--LETVQLaeLARSmsdGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILI 499
Cdd:NF040905 88 AlipylsiaeNIFLGNERAKRGVidWNEtnRRAREL--LAKV---GLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 500 LDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVE 554
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
341-565 |
3.40e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.02 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDdNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAlRQGVAMV 420
Cdd:PRK13536 42 IDLAGVSKSYGD-KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQ-DPVVLADTFLAN-VTLGRDISEERvwQALETV--QLAELARsMSDGIYTPLGEqgnnLSVGQKQLLALARVLVETPQ 496
Cdd:PRK13536 120 PQfDNLDLEFTVRENlLVFGRYFGMST--REIEAVipSLLEFAR-LESKADARVSD----LSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 497 ILILDEATASIDSGTEQAIQHALAAV--REHTTLVVI-----AHRLstivdADTILVLHRGQAVEQGTHQQLLAAQ 565
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLlaRGKTILLTThfmeeAERL-----CDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
345-556 |
3.91e-13 |
|
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: 68.86 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 345 NVSFAYRDDNLVLKnINLSVPSrNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL----SSLSHSALRQGVA-M 419
Cdd:cd03297 3 CVDIEKRLPDFTLK-IDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGlV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQDPVVLADTFLANVTLGRDISEE-----RVWQALETVQLAELARSMSDGiytplgeqgnnLSVGQKQLLALARVLVET 494
Cdd:cd03297 81 FQQYALFPHLNVRENLAFGLKRKRNredriSVDELLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447178945 495 PQILILDEATASIDSGTEQAIQHALAAVREHTTLVVI--AHRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:cd03297 150 PELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIfvTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
357-567 |
5.57e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSALRQGVAMVQQD-PVVLADTFLAN 434
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAStTAALAAGVAIIYQElHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 435 VTLGR-----DISEERVWQALETVQLAELARSMSDGiyTPLGEqgnnLSVGQKQLLALARVLVETPQILILDEATASIDS 509
Cdd:PRK11288 100 LYLGQlphkgGIVNRRLLNYEAREQLEHLGVDIDPD--TPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 510 -GTEQ--AIQHALAAvrEHTTLVVIAHRLSTIVD-ADTILVLHRGQ------AVEQGTHQQLLAAQ-GR 567
Cdd:PRK11288 174 rEIEQlfRVIRELRA--EGRVILYVSHRMEEIFAlCDAITVFKDGRyvatfdDMAQVDRDQLVQAMvGR 240
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
43-318 |
1.16e-12 |
|
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: 68.69 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 43 PLLISYFIDNMVAKNNLPLKVVagLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVG 122
Cdd:cd18555 22 PILTQYVIDNVIVPGNLNLLNV--LGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 123 QVISRVtNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLAD 202
Cdd:cd18555 100 DLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 203 INDGFNEIINGMSVI--------------QQFRQQARFGERmgeasRSHYMARMQTLrldgfllrpllslFSSLILCGLL 268
Cdd:cd18555 179 VQSYLTETLYGIETIkslgsekniykkweNLFKKQLKAFKK-----KERLSNILNSI-------------SSSIQFIAPL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447178945 269 MLFGFSA----SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18555 241 LILWIGAylviNGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
341-565 |
1.85e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrdDNLVLKnINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG----------RPLSSL-- 408
Cdd:PRK10771 2 LKLTDITWLY--HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttppsrRPVSMLfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 409 -----SHSALRQgvamvqqdpvvladtflaNVTLG-----RDISEERVwqaletvQLAELARSMsdGIYTPLGEQGNNLS 478
Cdd:PRK10771 79 ennlfSHLTVAQ------------------NIGLGlnpglKLNAAQRE-------KLHAIARQM--GIEDLLARLPGQLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 479 VGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAV--REHTTLVVIAHRLStivDADTI----LVLHRGQA 552
Cdd:PRK10771 132 GGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVcqERQLTLLMVSHSLE---DAARIaprsLVVADGRI 208
|
250
....*....|...
gi 447178945 553 VEQGTHQQLLAAQ 565
Cdd:PRK10771 209 AWDGPTDELLSGK 221
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
341-564 |
2.03e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.61 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLVLK---NINLSVPSRNFVALVGHTGSGKSTLASLLMGY--YP--LTEGEIRLDGRPLSSLSHSAL 413
Cdd:PRK11022 4 LNVDKLSVHFGDESAPFRavdRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPgrVMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 414 RQ----GVAMVQQDPVV-LADTFlanvTLGRDISE--------ERVWQALETVQLAELArsmsdGIYTP---LGEQGNNL 477
Cdd:PRK11022 84 RNlvgaEVAMIFQDPMTsLNPCY----TVGFQIMEaikvhqggNKKTRRQRAIDLLNQV-----GIPDPasrLDVYPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 478 SVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAV--REHTTLVVIAHRLSTIVD-ADTILVLHRGQAVE 554
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEaAHKIIVMYAGQVVE 234
|
250
....*....|
gi 447178945 555 QGTHQQLLAA 564
Cdd:PRK11022 235 TGKAHDIFRA 244
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
357-562 |
2.33e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.69 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYP---LTEGEIRLDGRPLSSlshSALRQGVAMVQQD----PVVLAD 429
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDA---KEMRAISAYVQQDdlfiPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 430 ---TFLANVTLGRDISE----ERVWQALETVQLAELARSMsdgIYTPLGEQGnnLSVGQKQLLALARVLVETPQILILDE 502
Cdd:TIGR00955 118 ehlMFQAHLRMPRRVTKkekrERVDEVLQALGLRKCANTR---IGVPGRVKG--LSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 503 ATASIDSGTEQAIQHALA--AVREHTTLVVIAHRLSTIVDA-DTILVLHRGQAVEQGTHQQLL 562
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKglAQKGKTIICTIHQPSSELFELfDKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
357-551 |
4.33e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSALRQGVAMVQQDPVVLAD-TFLAN 434
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQlTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 435 VTLGRDISEE--RV-WQALETVQLAELAR-SMSDGIYTPLGEqgnnLSVGQKQLLALARVLVETPQILILDEATasiDSG 510
Cdd:PRK10762 100 IFLGREFVNRfgRIdWKKMYAEADKLLARlNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPT---DAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447178945 511 TEQAIQHALAAVRE----HTTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:PRK10762 173 TDTETESLFRVIRElksqGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
341-556 |
4.44e-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: 65.85 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDN---LVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSALRQGV 417
Cdd:cd03266 2 ITADALTKRFRDVKktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDPVVLAD-TFLANVT-------LGRDISEERVWQALETVQLAELarsmsdgiytpLGEQGNNLSVGQKQLLALAR 489
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEyfaglygLKGDELTARLEELADRLGMEEL-----------LDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447178945 490 VLVETPQILILDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
342-553 |
5.75e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.13 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 342 EVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQ-GVAMV 420
Cdd:COG3845 259 EVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlGVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDP----VVLADTFLANVTLGRdISEERVWQA--LETVQLAELARSMSD-------GIYTPLGeqgnNLSVGQKQLLAL 487
Cdd:COG3845 339 PEDRlgrgLVPDMSVAENLILGR-YRRPPFSRGgfLDRKAIRAFAEELIEefdvrtpGPDTPAR----SLSGGNQQKVIL 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 488 ARVLVETPQILILDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVD-ADTILVLHRGQAV 553
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
29-290 |
6.50e-12 |
|
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: 66.72 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 29 VLMMWVAAAAEV---SGPLLISYFIDNMVAKNNLPLKVVagLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVM 105
Cdd:cd18567 5 LQILLLSLALELfalASPLYLQLVIDEVIVSGDRDLLTV--LAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 106 DAALRQPLSEFDTQPVGQVISRVtNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVV-MVI 184
Cdd:cd18567 83 RHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLrLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 185 YQRY----STPIVRRVRAyladiNDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFllrpllslfs 260
Cdd:cd18567 162 YPPLrratEEQIVASAKE-----QSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQIL---------- 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 447178945 261 slILCGLLMLFGFSA------------SGTIEVGVLYAFISY 290
Cdd:cd18567 227 --FSAANGLLFGLENilviylgallvlDGEFTVGMLFAFLAY 266
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
74-318 |
6.90e-12 |
|
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: 66.34 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 74 LQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALV 153
Cdd:cd18589 45 LTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 154 GAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQArfgermGEA 233
Cdd:cd18589 125 LFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEE------GEA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 234 SRshYMARMQ-TLRLDGFLLRPLLSLFSSLILCGLLMLFG-------FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQ 305
Cdd:cd18589 199 QR--YRQRLQkTYRLNKKEAAAYAVSMWTSSFSGLALKVGilyyggqLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYY 276
|
250
....*....|...
gi 447178945 306 AMLQQAVVAGERV 318
Cdd:cd18589 277 PSVMKAVGSSEKI 289
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
335-565 |
9.12e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.37 E-value: 9.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 335 PLQSGTIEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAlR 414
Cdd:PRK13537 2 PMSVAPIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 415 QGVAMVQQ----DP--------VVLADTFlanvTLGRDISEERVWQALETVQLAELARSmsdgiytPLGEqgnnLSVGQK 482
Cdd:PRK13537 80 QRVGVVPQfdnlDPdftvrenlLVFGRYF----GLSAAAARALVPPLLEFAKLENKADA-------KVGE----LSGGMK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 483 QLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAV--REHTTLVVI-----AHRLstivdADTILVLHRGQAVEQ 555
Cdd:PRK13537 145 RRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlaRGKTILLTThfmeeAERL-----CDRLCVIEEGRKIAE 219
|
250
....*....|
gi 447178945 556 GTHQQLLAAQ 565
Cdd:PRK13537 220 GAPHALIESE 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
344-565 |
1.05e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 344 DNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMVQQD 423
Cdd:PRK10253 11 EQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 424 PVVLADTFLANV------------TLGRDISEERVWQALETVQLAELARSMSDgiytplgeqgnNLSVGQKQLLALARVL 491
Cdd:PRK10253 90 ATTPGDITVQELvargryphqplfTRWRKEDEEAVTKAMQATGITHLADQSVD-----------TLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 492 VETPQILILDEATASIDSGTEQAIQHALAAV-REHT-TLVVIAHRLSTIVDADTILV-LHRGQAVEQGTHQQLLAAQ 565
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGyTLAAVLHDLNQACRYASHLIaLREGKIVAQGAPKEIVTAE 235
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
71-248 |
1.17e-11 |
|
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: 65.95 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 71 YVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSA 150
Cdd:cd18604 49 YALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLEST 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 151 ALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERM 230
Cdd:cd18604 129 LSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEM 208
|
170 180
....*....|....*....|....*.
gi 447178945 231 GE-------ASRSHYMA-RMQTLRLD 248
Cdd:cd18604 209 LRridrysrAFRYLWNLnRWLSVRID 234
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
25-248 |
1.64e-11 |
|
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: 65.19 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 25 LGIAVLMMWVAAAAEVSGPLLISYFIDNmvaKNNLPLKVVAGLAAAYVGLQ-LFAAGLHYAQSLLFNRAAvgvvQQLRTD 103
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTED---FFGLSQGFYIGIYAGLGVLQaIFLFLFGLLLAYLGIRAS----KRLHNK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 104 VMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDlyvtVVATVLRSAALVGAMLVAMFSL-----DWRMALVAIMIFpVV 178
Cdd:cd18606 74 ALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDN----ELPDSLRMFLYTLSSIIGTFILiiiylPWFAIALPPLLV-LY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 179 LVVMVIYQRYSTPIVR-----RVRAYLAdindgFNEIINGMSVIQQFRQQARFGERMGEA----SRSHYM----ARMQTL 245
Cdd:cd18606 149 YFIANYYRASSRELKRlesilRSFVYAN-----FSESLSGLSTIRAYGAQDRFIKKNEKLidnmNRAYFLtianQRWLAI 223
|
...
gi 447178945 246 RLD 248
Cdd:cd18606 224 RLD 226
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
101-536 |
1.90e-11 |
|
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: 67.08 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 101 RTDVMDAALRQPLSEFDTQPVGQVISRVTN-DTEVIRDLYVTVVATVLRSAALVGAML-VAMFSLDWRMALVAIM---IF 175
Cdd:TIGR00954 167 RVRLTRYLYSKYLSGFTFYKVSNLDSRIQNpDQLLTQDVEKFCDSVVELYSNLTKPILdVILYSFKLLTALGSVGpagLF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 176 PVVLVVMVIYQRYSTPIVRRV---RAYLADINDGFNEIINGMSVIQQFRQQARfgERmgEASRSHYMARMQTLRLDGFLL 252
Cdd:TIGR00954 247 AYLFATGVVLTKLRPPIGKLTveeQALEGEYRYVHSRLIMNSEEIAFYQGNKV--EK--ETVMSSFYRLVEHLNLIIKFR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 253 RPLLSLFSslilcgLLMLFGFSASGTIEVGVLYAFISYLG----RLNEPLIELTTQQAMLQQAVVAGER----------- 317
Cdd:TIGR00954 323 FSYGFLDN------IVAKYTWSAVGLVAVSIPIFDKTHPAflemSEEELMQEFYNNGRLLLKAADALGRlmlagrdmtrl 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 318 ------VFELMD------GPRQQYGNDDRPLQSGT--------------------IEVDNVSFAYRDDNLVLKNINLSVP 365
Cdd:TIGR00954 397 agftarVDTLLQvlddvkSGNFKRPRVEEIESGREggrnsnlvpgrgiveyqdngIKFENIPLVTPNGDVLIESLSFEVP 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 366 SRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG---------RPLSSLshSALRqgvamvqqDPVVLADTFLANVT 436
Cdd:TIGR00954 477 SGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAkgklfyvpqRPYMTL--GTLR--------DQIIYPDSSEDMKR 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 437 lgRDISEERVWQALETVQLAE-LARSMSdgiYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAI 515
Cdd:TIGR00954 547 --RGLSDKDLEQILDNVQLTHiLEREGG---WSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM 621
|
490 500
....*....|....*....|.
gi 447178945 516 QHALAAVRehTTLVVIAHRLS 536
Cdd:TIGR00954 622 YRLCREFG--ITLFSVSHRKS 640
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
329-564 |
2.21e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 329 YGNDDRPLQSGTIEVDNVSFAyrddnlVLKN-INLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS 407
Cdd:PRK11288 246 YGYRPRPLGEVRLRLDGLKGP------GLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 408 LS-HSALRQGVAMVQQDPVVLADTFLANVTLGRDISEER--------VWQALETVQLAELARSMSdgIYTPLGEQG-NNL 477
Cdd:PRK11288 320 RSpRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRhhlragclINNRWEAENADRFIRSLN--IKTPSREQLiMNL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 478 SVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQ---HALAAvrEHTTLVVIAHRLSTIVD-ADTILVLHRGQAV 553
Cdd:PRK11288 398 SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYnviYELAA--QGVAVLFVSSDLPEVLGvADRIVVMREGRIA 475
|
250
....*....|....*.
gi 447178945 554 -----EQGTHQQLLAA 564
Cdd:PRK11288 476 gelarEQATERQALSL 491
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
356-563 |
2.56e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.22 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 356 VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-------------ALRQGVAMVQQ 422
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 423 DPVVLAD-TFLANVT--------LGRDISEERVWQALETVQLAELARsmsdgiytplGEQGNNLSVGQKQLLALARVLVE 493
Cdd:PRK10619 100 HFNLWSHmTVLENVMeapiqvlgLSKQEARERAVKYLAKVGIDERAQ----------GKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447178945 494 TPQILILDEATASIDS---GTEQAIQHALAavREHTTLVVIAHRLSTIVDADT-ILVLHRGQAVEQGTHQQLLA 563
Cdd:PRK10619 170 EPEVLLFDEPTSALDPelvGEVLRIMQQLA--EEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
356-553 |
3.29e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 66.29 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 356 VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSAL----RQGVAMVQQdpvvlADTF 431
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQ-----RYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 432 LANVTLGRDISEERVWQALETVQLAELARSMSD--GIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASID- 508
Cdd:PRK10535 98 LSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQrlGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDs 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447178945 509 -SGTE-QAIQHALAAvREHTTLVViAHRLSTIVDADTILVLHRGQAV 553
Cdd:PRK10535 178 hSGEEvMAILHQLRD-RGHTVIIV-THDPQVAAQAERVIEIRDGEIV 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
340-579 |
6.18e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.59 E-value: 6.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslshSALRQGVA- 418
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 419 ----------M-VQQDPVVLADtfLANVTLGRDISEERVWqaLETVQLAELArsmsdgiYTPLGEqgnnLSVGQKQLLAL 487
Cdd:COG4152 76 lpeerglypkMkVGEQLVYLAR--LKGLSKAEAKRRADEW--LERLGLGDRA-------NKKVEE----LSKGNQQKVQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 488 ARVLVETPQILILDEATASIDSgteQAIQHALAAVREH----TTLVVIAHRLSTiVD--ADTILVLHRGQAVEQGTHQQL 561
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDP---VNVELLKDVIRELaakgTTVIFSSHQMEL-VEelCDRIVIINKGRKVLSGSVDEI 216
|
250
....*....|....*...
gi 447178945 562 LAAQGRywQMYQLQLAGE 579
Cdd:COG4152 217 RRQFGR--NTLRLEADGD 232
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
370-562 |
6.98e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 370 VALVGHTGSGKSTLASLLMGYYPlTEGEIRLDGRPLSSLSHS--ALRQGVAMVQQDPVVLADTFLanvTLGRDISEERVW 447
Cdd:PRK03695 25 LHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAelARHRAYLSQQQTPPFAMPVFQ---YLTLHQPDKTRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 448 QALETVqLAELARSMsdGIYTPLGEQGNNLSVGQKQLLALARVLVET-------PQILILDEATASIDSGTEQAIQHALA 520
Cdd:PRK03695 101 EAVASA-LNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQVwpdinpaGQLLLLDEPMNSLDVAQQAALDRLLS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447178945 521 AV-REHTTLVVIAHRLS-TIVDADTILVLHRGQAVEQGTHQQLL 562
Cdd:PRK03695 178 ELcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
345-561 |
9.07e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.59 E-value: 9.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 345 NVSFAYRDDNLVLKN-INLSVPSRNFVALVGHTGSGKSTLASLLMGYYP---LTEGEIRLDGRPLSSLSHSALR----QG 416
Cdd:PRK09473 19 RVTFSTPDGDVTAVNdLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGREILNLPEKELNklraEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 417 VAMVQQDPVV-------LADTFLANVTLGRDIS-----EERVwQALETVQLAELARSMsdGIYTplgeqgNNLSVGQKQL 484
Cdd:PRK09473 99 ISMIFQDPMTslnpymrVGEQLMEVLMLHKGMSkaeafEESV-RMLDAVKMPEARKRM--KMYP------HEFSGGMRQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 485 LALARVLVETPQILILDEATASIDSGTEQAIQHALAAV-RE-HTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQL 561
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREfNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
71-230 |
1.02e-10 |
|
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: 63.01 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 71 YVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSA 150
Cdd:cd18602 56 YAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 151 ALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQRYSTPIVRrvrayLADINDG-----FNEIINGMSVIQQFRQQAR 225
Cdd:cd18602 136 LLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQR-----LDNITKSpvfshFSETLGGLTTIRAFRQQAR 210
|
....*
gi 447178945 226 FGERM 230
Cdd:cd18602 211 FTQQM 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
341-561 |
1.08e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.34 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYY---PLTEGEIRLDGRPLSSLSHSA--LRQ 415
Cdd:PRK09984 5 IRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRLArdIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 416 GVA----MVQQDPVVLADTFLANVTLG---------------RDISEERVWQALETVQLAELARsmsdgiytplgEQGNN 476
Cdd:PRK09984 84 SRAntgyIFQQFNLVNRLSVLENVLIGalgstpfwrtcfswfTREQKQRALQALTRVGMVHFAH-----------QRVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 477 LSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREH--TTLVVIAHRLSTIVD-ADTILVLHRGQAV 553
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRyCERIVALRQGHVF 232
|
....*...
gi 447178945 554 EQGTHQQL 561
Cdd:PRK09984 233 YDGSSQQF 240
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
336-563 |
1.10e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 336 LQSGTIEVDNVSFAYRDDNlVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSA-LR 414
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 415 QGVAMVQQDPVVLAD-TFLANVTLGRDISEERVWQaletvQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVE 493
Cdd:PRK11614 80 EAVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQ-----ERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447178945 494 TPQILILDEATASIDSGTEQAIQHALAAVREH--TTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLA 563
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgmTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
22-318 |
1.50e-10 |
|
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: 62.58 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 22 RKPLGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVVagLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLR 101
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNL--ILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 102 TDVMDAALRQPLSEFDTQPVGQVISRVtNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAI-MIFPVVLV 180
Cdd:cd18568 79 SDFYKHLLSLPLSFFASRKVGDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLaFIPLYVLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 181 VMviyqrYSTPIVRR----VRAYLADINDGFNEIINGMSVI------QQFRQQarfgermGEASRSHYM-ARMQTLRLDG 249
Cdd:cd18568 158 TL-----LSSPKLKRnsreIFQANAEQQSFLVEALTGIATIkalaaeRPIRWR-------WENKFAKALnTRFRGQKLSI 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447178945 250 FLLRPLLSLFSSLILcgLLMLFG--FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18568 226 VLQLISSLINHLGTI--AVLWYGayLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
352-569 |
1.67e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.73 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 352 DDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGY--YPLTEGEIRLDGRPLSSLS-HSALRQGVAMVQQDPVVL- 427
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVEIp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 428 --ADTFLANVTLGrDISEERVWQALETVQLAELAR------SMSDGIYTPLGEQGnnLSVGQKQLLALARVLVETPQILI 499
Cdd:PRK09580 92 gvSNQFFLQTALN-AVRSYRGQEPLDRFDFQDLMEekiallKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447178945 500 LDEATASIDSGTEQAIQHALAAVR-EHTTLVVIAH--RLSTIVDADTILVLHRGQAVEQGTHQ--QLLAAQGRYW 569
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTlvKQLEEQGYGW 243
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
353-563 |
1.73e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.50 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 353 DNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQgvamvqqdpvVLADTFL 432
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK----------LVSDEWQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 433 ANVT---------LGRDISEERVWQALETVQLAELARSMsdGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEA 503
Cdd:PRK10938 85 RNNTdmlspgeddTGRTTAEIIQDEVKDPARCEQLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447178945 504 TASIDSGTEQAIQHALAAV-REHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLA 563
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLhQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
340-502 |
3.42e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.78 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShSALRqGVAM 419
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE-PADR-DIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQD----P-VVLADTF---LANVTLGRDISEERVWQALETVQLAELarsmsdgiytpLGEQGNNLSVGQKQLLALARVL 491
Cdd:PRK11650 81 VFQNyalyPhMSVRENMaygLKIRGMPKAEIEERVAEAARILELEPL-----------LDRKPRELSGGQRQRVAMGRAI 149
|
170
....*....|.
gi 447178945 492 VETPQILILDE 502
Cdd:PRK11650 150 VREPAVFLFDE 160
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
356-533 |
3.44e-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: 60.53 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 356 VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL--DGRPLSsLSHSALRQGVAMVQQD---------- 423
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVD-LAQASPREILALRRRTigyvsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 424 -PVVLADTFLANVTL----GRDISEERVWQALETVQLAELARSMSdgiytPlgeqgNNLSVGQKQLLALARVLVETPQIL 498
Cdd:COG4778 105 iPRVSALDVVAEPLLergvDREEARARARELLARLNLPERLWDLP-----P-----ATFSGGEQQRVNIARGFIADPPLL 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 447178945 499 ILDEATASIDSGTEQA----IQHALAAvreHTTLVVIAH 533
Cdd:COG4778 175 LLDEPTASLDAANRAVvvelIEEAKAR---GTAIIGIFH 210
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
353-510 |
3.45e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.50 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 353 DNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMG--YYPLTEGEIRLDGRPLSSLS-HSALRQGVAMVQQDP----V 425
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEVDVSTvSDAIDAGLAYVTEDRkgygL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 426 VLADTFLANVTLG--RDISEERVWQALETVQLAELAR-SM---SDGIYTPLGeqgnNLSVGQKQLLALARVLVETPQILI 499
Cdd:NF040905 352 NLIDDIKRNITLAnlGKVSRRGVIDENEEIKVAEEYRkKMnikTPSVFQKVG----NLSGGNQQKVVLSKWLFTDPDVLI 427
|
170
....*....|.
gi 447178945 500 LDEATASIDSG 510
Cdd:NF040905 428 LDEPTRGIDVG 438
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
61-229 |
4.06e-10 |
|
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: 61.01 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 61 LKVVAGLAAAYVGLQLFAAGLHYAQSLlfnRAAVGVVQQLrtdvMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYV 140
Cdd:cd18605 45 LTVYGFLAGLNSLFTLLRAFLFAYGGL---RAARRLHNKL----LSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 141 TVVATVLRSAA-LVGAMLVAMFSLDWrmalvaimIFPVVLVVMVIY---QRYSTPIVRRVRAyLADINDG-----FNEII 211
Cdd:cd18605 118 FILNILLAQLFgLLGYLVVICYQLPW--------LLLLLLPLAFIYyriQRYYRATSRELKR-LNSVNLSplythFSETL 188
|
170
....*....|....*...
gi 447178945 212 NGMSVIQQFRQQARFGER 229
Cdd:cd18605 189 KGLVTIRAFRKQERFLKE 206
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
28-247 |
7.29e-10 |
|
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: 60.37 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 28 AVLMMWVAAAAEVSGPLLISYFIDNMVAknNLPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDA 107
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFA--GGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 108 ALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLrsAALVGAMLV--AMFSLDWRMALVAIMIFPVVLVVMVIY 185
Cdd:cd18561 79 LLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLL--VALLGPLLIliYLFFLDPLVALILLVFALLIPLSPALW 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447178945 186 QRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRL 247
Cdd:cd18561 157 DRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAV 218
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
357-545 |
1.25e-09 |
|
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: 57.72 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLasLLMGYYplTEGEIRL-DGRPLSSlshsalRQGVAMVQQdpvvLadTFLANV 435
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLiSFLPKFS------RNKLIFIDQ----L--QFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 436 TLGrdiseervwqaletvqlaelarsmsdgiYTPLGEQGNNLSVGQKQLLALARVLVETPQ--ILILDEATASIDsgtEQ 513
Cdd:cd03238 75 GLG----------------------------YLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH---QQ 123
|
170 180 190
....*....|....*....|....*....|....*.
gi 447178945 514 AIQHALAAVR----EHTTLVVIAHRLSTIVDADTIL 545
Cdd:cd03238 124 DINQLLEVIKglidLGNTVILIEHNLDVLSSADWII 159
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
351-550 |
1.72e-09 |
|
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: 57.64 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 351 RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLL-----MGYyplTEGEIRLDGRPLSslshSALRQGVAMVQQdpv 425
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLD----KNFQRSTGYVEQ--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 426 vlADTFLANVTLgrdiseervwqaLETVQLAELARSmsdgiytplgeqgnnLSVGQKQLLALARVLVETPQILILDEATA 505
Cdd:cd03232 87 --QDVHSPNLTV------------REALRFSALLRG---------------LSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447178945 506 SIDSGTEQAIQHALAAVREH--TTLVVIAHRLSTIVDA-DTILVLHRG 550
Cdd:cd03232 138 GLDSQAAYNIVRFLKKLADSgqAILCTIHQPSASIFEKfDRLLLLKRG 185
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
370-562 |
1.83e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.78 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR-----PLSSLSHSA----LRQGVAMVQQDPvvlADTFLANVTLGRD 440
Cdd:PRK11701 35 LGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAErrrlLRTEWGFVHQHP---RDGLRMQVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 441 ISE------ERVW-----QALETVQLAELARSMSDgiytplgEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDS 509
Cdd:PRK11701 112 IGErlmavgARHYgdiraTAGDWLERVEIDAARID-------DLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447178945 510 GTeQA-------------------IQHALAAVRehttlvVIAHRLstivdadtiLVLHRGQAVEQGTHQQLL 562
Cdd:PRK11701 185 SV-QArlldllrglvrelglavviVTHDLAVAR------LLAHRL---------LVMKQGRVVESGLTDQVL 240
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
43-318 |
2.26e-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: 58.75 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 43 PLLISYFIDNMVAKNNLP-LKV-VAGLAAAYvglqLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQP 120
Cdd:cd18566 22 PLFILQVYDRVIPNESIPtLQVlVIGVVIAI----LLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 121 VGQVISRVtNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQrystPIVRRVRAYL 200
Cdd:cd18566 98 SGAHLERL-NSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLG----PILRRALKER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 201 ADIND---GF-NEIINGMSVIQQF----RQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSLILCGLLMLFg 272
Cdd:cd18566 173 SRADErrqNFlIETLTGIHTIKAMamepQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVI- 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 447178945 273 fsaSGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18566 252 ---NGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
360-564 |
5.11e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.28 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 360 INLSVPSRNFVALVGHTGSGKSTLASLLMGY----YPLTEGEIRLDGRPLSSLSHSALRQ----GVAMVQQDPVVLADtf 431
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKlvghNVSMIFQEPQSCLD-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 432 lANVTLGRDISEE--------RVWQA-----------LETVQLAELARSMSDGIYtplgeqgnNLSVGQKQLLALARVLV 492
Cdd:PRK15093 104 -PSERVGRQLMQNipgwtykgRWWQRfgwrkrraielLHRVGIKDHKDAMRSFPY--------ELTEGECQKVMIAIALA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447178945 493 ETPQILILDEATASIDSGTEQAIQHALAAVREH--TTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLAA 564
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVTT 249
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
342-515 |
7.02e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 342 EVDNVSfayRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSALRQGVAMV 420
Cdd:PRK09700 267 EVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPvvlADT-FLANVTLGRDISEER------------VWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLAL 487
Cdd:PRK09700 344 TESR---RDNgFFPNFSIAQNMAISRslkdggykgamgLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLI 420
|
170 180
....*....|....*....|....*...
gi 447178945 488 ARVLVETPQILILDEATASIDSGTEQAI 515
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEI 448
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
27-217 |
7.09e-09 |
|
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: 57.11 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 27 IAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVVAGLAAAYVGLQLFAA-GLHYAQSLLFNraaVGVvqQLRTDVM 105
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSlLLHQYFFLSFR---LGM--RVRSALS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 106 DA----ALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVlrSAALVgaMLVAMFSLDWRM---ALVAImifpVV 178
Cdd:cd18579 76 SLiyrkALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLW--SAPLQ--IIVALYLLYRLLgwaALAGL----GV 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447178945 179 LVVMVIYQRYSTPIVRRVRAYLADINDG----FNEIINGMSVI 217
Cdd:cd18579 148 LLLLIPLQAFLAKLISKLRKKLMKATDErvklTNEILSGIKVI 190
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
358-551 |
7.11e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 358 KNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSALRQGVAMVQQDPVV---LADTFLA 433
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPEDRQSsglYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 434 NVTLGRDISEERVWQ--ALETVQLAELARSMsdGIYTPLGEQG-NNLSVGQKQLLALARVLVETPQILILDEATASIDSG 510
Cdd:PRK15439 360 WNVCALTHNRRGFWIkpARENAVLERYRRAL--NIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447178945 511 TE----QAIQHaLAAvrEHTTLVVIAHRLSTIVD-ADTILVLHRGQ 551
Cdd:PRK15439 438 ARndiyQLIRS-IAA--QNVAVLFISSDLEEIEQmADRVLVMHQGE 480
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
97-290 |
1.18e-08 |
|
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: 56.58 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 97 VQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFP 176
Cdd:cd18590 68 NLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 177 VVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYmaRMQTLRlDGFLLRPLL 256
Cdd:cd18590 148 LTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTY--NLKDRR-DTVRAVYLL 224
|
170 180 190
....*....|....*....|....*....|....*..
gi 447178945 257 SLFSSLILCGLLMLF---GFSASGTIEVGVLYAFISY 290
Cdd:cd18590 225 VRRVLQLGVQVLMLYcgrQLIQSGHLTTGSLVSFILY 261
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
341-525 |
1.73e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.96 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDdNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSALRQGVAMV 420
Cdd:PRK13540 2 LDVIELDFDYHD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPVVladtfLANVTLgRDISEERVWQALETVQLAELARSMSDGIYT--PLGEqgnnLSVGQKQLLALARVLVETPQIL 498
Cdd:PRK13540 80 GHRSGI-----NPYLTL-RENCLYDIHFSPGAVGITELCRLFSLEHLIdyPCGL----LSSGQKRQVALLRLWMSKAKLW 149
|
170 180
....*....|....*....|....*..
gi 447178945 499 ILDEATASIDsgtEQAIQHALAAVREH 525
Cdd:PRK13540 150 LLDEPLVALD---ELSLLTIITKIQEH 173
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
341-561 |
2.51e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.86 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNL-----VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEI-------RLDGRPLSSL 408
Cdd:PRK13651 3 IKVKNIVKIF-NKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 409 SH-----------------SALRQGVAMVQQ-------DPVVLADTFLANVTLGRDISE--ERVWQALETVQLAE--LAR 460
Cdd:PRK13651 82 KVleklviqktrfkkikkiKEIRRRVGVVFQfaeyqlfEQTIEKDIIFGPVSMGVSKEEakKRAAKYIELVGLDEsyLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 461 SmsdgiytPLgeqgnNLSVGQKQLLALARVLVETPQILILDEATASID-SGTEQAIQHALAAVREHTTLVVIAHRLSTIV 539
Cdd:PRK13651 162 S-------PF-----ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEIFDNLNKQGKTIILVTHDLDNVL 229
|
250 260
....*....|....*....|....
gi 447178945 540 D-ADTILVLHRGQAVEQG-THQQL 561
Cdd:PRK13651 230 EwTKRTIFFKDGKIIKDGdTYDIL 253
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
351-557 |
2.51e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 351 RDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYP--------LTEGEIRLDGRPLSSLSHSALRQGVAMVQQ 422
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 423 ----------DPVVLADTFLANVTLGRDISEER--VWQALETVQLAELArsmsdgiytplGEQGNNLSVGQKQLLALARV 490
Cdd:PRK13547 91 aaqpafafsaREIVLLGRYPHARRAGALTHRDGeiAWQALALAGATALV-----------GRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 491 LVE---------TPQILILDEATASIDsgteQAIQHA-LAAVRE-----HTTLVVIAHRLSTIV-DADTILVLHRGQAVE 554
Cdd:PRK13547 160 LAQlwpphdaaqPPRYLLLDEPTAALD----LAHQHRlLDTVRRlardwNLGVLAIVHDPNLAArHADRIAMLADGAIVA 235
|
...
gi 447178945 555 QGT 557
Cdd:PRK13547 236 HGA 238
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
352-550 |
3.89e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 352 DDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLL-----MGYypLTEGEIRLDGRPL-SSLSHSalrqgVAMVQQDPV 425
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGV--ITGGDRLVNGRPLdSSFQRS-----IGYVQQQDL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 426 VLADT-------FLANVTLGRDISEERVWQALETV-QLAELaRSMSDGIytpLGEQGNNLSVGQKQLLALARVLVETPQI 497
Cdd:TIGR00956 847 HLPTStvreslrFSAYLRQPKSVSKSEKMEYVEEViKLLEM-ESYADAV---VGVPGEGLNVEQRKRLTIGVELVAKPKL 922
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 498 LI-LDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVDA--DTILVLHRG 550
Cdd:TIGR00956 923 LLfLDEPTSGLDSQTAWSICKLMRKLADHgQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
352-557 |
4.84e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 352 DDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGY--YPLTEGEIRLDGRPLSSLSHSAL-RQGVAMVQQDPV--- 425
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEERaHLGIFLAFQYPIeip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 426 -VLADTFLANVTLGRDISE-----------ERVWQALETVQLAE--LARSMSDGIYTplGEQGNNlsvgqkQLLALArvL 491
Cdd:CHL00131 98 gVSNADFLRLAYNSKRKFQglpeldpleflEIINEKLKLVGMDPsfLSRNVNEGFSG--GEKKRN------EILQMA--L 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 492 VEtPQILILDEatasIDSGTE----QAIQHALAAVREHTT-LVVIAH--RLSTIVDADTILVLHRGQAVEQGT 557
Cdd:CHL00131 168 LD-SELAILDE----TDSGLDidalKIIAEGINKLMTSENsIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
357-579 |
5.61e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.71 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMG-YYPlTEGEIRLDGRPLSSLSHSALRQ-GVAMVQ--Q---D-PVVla 428
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEVRVLGYVPFKRRKEFARRiGVVFGQrsQlwwDlPAI-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 429 DTFLanvTLGR--DISEERVWQALEtvQLAELArSMSDGIYTPLgeqgNNLSVGQKQLLALARVLVETPQILILDEATAS 506
Cdd:COG4586 115 DSFR---LLKAiyRIPDAEYKKRLD--ELVELL-DLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIG 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 507 IDSGTEQAIQHALAAV--REHTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLAAQGRYWQMyQLQLAGE 579
Cdd:COG4586 185 LDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYKTI-VLELAEP 259
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
28-196 |
6.69e-08 |
|
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: 54.43 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 28 AVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDA 107
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRVFRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 108 ALRQPLSEFDTQPVG---QVISRVTNDTE-VIRDLYVTVVATVLRsAALVGAMLVAMFslDWRMALVAIMIFPVVLVVMV 183
Cdd:cd18582 81 LHSLSLRFHLSRKTGalsRAIERGTRGIEfLLRFLLFNILPTILE-LLLVCGILWYLY--GWSYALITLVTVALYVAFTI 157
|
170
....*....|...
gi 447178945 184 IYQRYSTPIVRRV 196
Cdd:cd18582 158 KVTEWRTKFRREM 170
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
370-556 |
8.18e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---ALRQGVAMVQQDPVVLADtflANVTLGRDISEE-R 445
Cdd:PRK10261 353 LSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqALRRDIQFIFQDPYASLD---PRQTVGDSIMEPlR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 446 VWQALEtvqlAELARSMSDGIYTPLGEQGNN-------LSVGQKQLLALARVLVETPQILILDEATASID-SGTEQAIQH 517
Cdd:PRK10261 430 VHGLLP----GKAAAARVAWLLERVGLLPEHawrypheFSGGQRQRICIARALALNPKVIIADEAVSALDvSIRGQIINL 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447178945 518 ALAAVRE---------HTTLVV--IAHRLStivdadtilVLHRGQAVEQG 556
Cdd:PRK10261 506 LLDLQRDfgiaylfisHDMAVVerISHRVA---------VMYLGQIVEIG 546
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
366-549 |
1.05e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 366 SRNFVALVGHTGSGKSTLASLLMGYY-PLTEGEIRLDGRPLSSLSHSALRQgvamvqqdpvvladtflanvtlgrdisee 444
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgPPGGGVIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 445 rvwqaletvqlaelarsmsdgiyTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQ-------H 517
Cdd:smart00382 52 -----------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlL 108
|
170 180 190
....*....|....*....|....*....|..
gi 447178945 518 ALAAVREHTTLVVIAHRLSTIVDADTILVLHR 549
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
67-314 |
1.09e-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: 53.67 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 67 LAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVtNDTEVIRDlYVT--VVA 144
Cdd:cd18783 44 LTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQ-FLTgqLFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 145 TVLRSAALVGAMLVaMFSLDWRMALV----AIMIFPVVLVVMVIYQRYSTpivrrvRAYLADINDGFN--EIINGMSVIQ 218
Cdd:cd18783 122 TLLDATSLLVFLPV-LFFYSPTLALVvlafSALIALIILAFLPPFRRRLQ------ALYRAEGERQAFlvETVHGIRTVK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 219 QF----RQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSLILCGLLMLFgfsaSGTIEVGVLYAFISYLGRL 294
Cdd:cd18783 195 SLalepRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVF----AGSLTVGALIAFNMLAGRV 270
|
250 260
....*....|....*....|
gi 447178945 295 NEPLIELTTQQAMLQQAVVA 314
Cdd:cd18783 271 AGPLVQLAGLVQEYQEARLS 290
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
43-318 |
1.53e-07 |
|
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: 53.27 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 43 PLLISYFIDNMVAKNNLPLKVVagLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVG 122
Cdd:cd18588 22 PLFFQVIIDKVLVHRSLSTLDV--LAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 123 QVISRVtNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAImifpVVLVVMVIYQRYSTPIVRR---VRAY 199
Cdd:cd18588 100 DTVARV-RELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVL----ASLPLYALLSLLVTPILRRrleEKFQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 200 LADINDGF-NEIINGMSVI------QQFRQqaRFGERMGEASRShymarmqTLRLDGFLLRPLLSLFSSLILCGLLML-F 271
Cdd:cd18588 175 RGAENQSFlVETVTGIETVkslavePQFQR--RWEELLARYVKA-------SFKTANLSNLASQIVQLIQKLTTLAILwF 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 447178945 272 GFSA--SGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERV 318
Cdd:cd18588 246 GAYLvmDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
340-508 |
1.59e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.81 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 340 TIEVDNVSFAYRDdnlVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshsaLRQGvaM 419
Cdd:PRK09544 6 SLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LRIG--Y 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 420 VQQ----DPVvLADTFLANVTLGRDISEERVWQALETVQLAELarsmsdgIYTPLgeqgNNLSVGQKQLLALARVLVETP 495
Cdd:PRK09544 72 VPQklylDTT-LPLTVNRFLRLRPGTKKEDILPALKRVQAGHL-------IDAPM----QKLSGGETQRVLLARALLNRP 139
|
170
....*....|...
gi 447178945 496 QILILDEATASID 508
Cdd:PRK09544 140 QLLVLDEPTQGVD 152
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
286-502 |
1.61e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 286 AFISYLGRLNE-PLIELTTQQAMLQQAVVA----GERVFELM----DGPRQQYG-NDDRPLqsgtIEVDNVSFAYrDDNL 355
Cdd:PRK10938 200 DFVQFAGVLADcTLAETGEREEILQQALVAqlahSEQLEGVQlpepDEPSARHAlPANEPR----IVLNNGVVSY-NDRP 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 356 VLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYP------LT-------EGEIRLD-----GRPLSSLsHSALRqgV 417
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPqgysndLTlfgrrrgSGETIWDikkhiGYVSSSL-HLDYR--V 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 418 AMVQQDpvVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYtplgeqgNNLSVGQKQLLALARVLVETPQI 497
Cdd:PRK10938 352 STSVRN--VILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPF-------HSLSWGQQRLALIVRALVKHPTL 422
|
....*
gi 447178945 498 LILDE 502
Cdd:PRK10938 423 LILDE 427
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
371-583 |
2.63e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.01 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 371 ALVGHTGSGKSTLASLLMGYYP----LTEGEIRLDGRPLSSlshSALR-QGVAMVQQDP-------VVLAD----TFLAn 434
Cdd:PRK10418 33 ALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVAP---CALRgRKIATIMQNPrsafnplHTMHThareTCLA- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 435 vtLGRDISEERVWQALETVQLAELAR-------SMSDGIYtplgeqgnnlsvgQKQLLALArVLVETPqILILDEATASI 507
Cdd:PRK10418 109 --LGKPADDATLTAALEAVGLENAARvlklypfEMSGGML-------------QRMMIALA-LLCEAP-FIIADEPTTDL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 508 DSGTEQAIQHALAA-VREHTT-LVVIAHRLSTIVD-ADTILVLHRGQAVEQGTHQQLLAAQG----RYWQMYQLQLAGEE 580
Cdd:PRK10418 172 DVVAQARILDLLESiVQKRALgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAPKhavtRSLVSAHLALYGME 251
|
...
gi 447178945 581 LAA 583
Cdd:PRK10418 252 LAS 254
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
69-230 |
6.94e-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: 51.33 E-value: 6.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 69 AAYVGLQLFAAGLhyaQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLR 148
Cdd:cd18603 48 GALGLGQAIFVFL---GSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 149 SAA-LVGAMLVAMFSLDWrmalvAIMIFPVVLVVMVIYQRYSTPIVRRVR----AYLADINDGFNEIINGMSVIQQFRQQ 223
Cdd:cd18603 125 CLFqVISTLVVISISTPI-----FLVVIIPLAILYFFIQRFYVATSRQLKrlesVSRSPIYSHFSETLQGASTIRAYGVQ 199
|
....*..
gi 447178945 224 ARFGERM 230
Cdd:cd18603 200 ERFIRES 206
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
83-229 |
1.05e-06 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 50.74 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 83 YAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFS 162
Cdd:cd18558 77 YIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFI 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 163 LDWRMALVAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGER 229
Cdd:cd18558 157 RGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETR 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
354-556 |
1.47e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.64 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 354 NLVLkNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSAL-----RQGVAMVQQDpvvlA 428
Cdd:PRK11144 12 DLCL-TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD-AEKGIclppeKRRIGYVFQD----A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 429 DTF-----LANVTLGrdISEERVWQALETVQLAelarsmsdGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEA 503
Cdd:PRK11144 86 RLFphykvRGNLRYG--MAKSMVAQFDKIVALL--------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 504 TASIDsgteqaiqhaLAAVRE------------HTTLVVIAHRLSTIVD-ADTILVLHRGQAVEQG 556
Cdd:PRK11144 156 LASLD----------LPRKREllpylerlareiNIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
28-185 |
3.38e-06 |
|
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: 49.08 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 28 AVLMMWVAAAAEVSGPLLISYFID---NMVAKNNLP-LKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTD 103
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNvisRSLKETNGDfIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 104 VMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMV 183
Cdd:cd18574 81 LFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGT 160
|
..
gi 447178945 184 IY 185
Cdd:cd18574 161 LY 162
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
344-553 |
3.45e-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: 49.93 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 344 DNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLdgrplsslshsalRQG--VAMVQ 421
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-------------QPGikVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 422 QDPVV-LADTFLANVTLG----RDISEE-----------------------RVWQALETVQLAELARSMS---DGIYTPL 470
Cdd:TIGR03719 75 QEPQLdPTKTVRENVEEGvaeiKDALDRfneisakyaepdadfdklaaeqaELQEIIDAADAWDLDSQLEiamDALRCPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 471 GEQG-NNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALaavREHT-TLVVIAH-R--LSTIvdADTIL 545
Cdd:TIGR03719 155 WDADvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL---QEYPgTVVAVTHdRyfLDNV--AGWIL 229
|
....*...
gi 447178945 546 VLHRGQAV 553
Cdd:TIGR03719 230 ELDRGRGI 237
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
357-589 |
3.59e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsSLSHSALRQGvamVQQDPVVLADTFLANVT 436
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----SAALIAISSG---LNGQLTGIENIELKGLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 437 LGrdISEERVWQAL-ETVQLAELARSMSDGIYTplgeqgnnLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAI 515
Cdd:PRK13545 113 MG--LTKEKIKEIIpEIIEFADIGKFIYQPVKT--------YSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447178945 516 QHALAAVREH-TTLVVIAHRLSTIVDADT-ILVLHRGQAVEQGTHQQLLAAQGRYWQMYQlQLAGEElAASVREEE 589
Cdd:PRK13545 183 LDKMNEFKEQgKTIFFISHSLSQVKSFCTkALWLHYGQVKEYGDIKEVVDHYDEFLKKYN-QMSVEE-RKDFREEQ 256
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
320-508 |
5.43e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 320 ELMDGPRQQYGNDDRplqSGTI--EVDNVSFAYRDDNLVlKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGE 397
Cdd:PRK11147 300 EVMGTAKMQVEEASR---SGKIvfEMENVNYQIDGKQLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 398 IRLdGRPLSslshsalrqgVAMVQQ-----DPvvlADTFLANVTLGR-DIS---EERvwQALETVQ--LAELARSMsdgi 466
Cdd:PRK11147 376 IHC-GTKLE----------VAYFDQhraelDP---EKTVMDNLAEGKqEVMvngRPR--HVLGYLQdfLFHPKRAM---- 435
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447178945 467 yTPLgeqgNNLSVGQKQLLALARVLVETPQILILDEATASID 508
Cdd:PRK11147 436 -TPV----KALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
341-567 |
6.94e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsslshsALRQGVAMv 420
Cdd:PRK10636 313 LKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAKGIKL- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 qqdpvvladTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIyTPLGEQGNNL-------SVGQKQLLALARVLVE 493
Cdd:PRK10636 378 ---------GYFAQHQLEFLRADESPLQHLARLAPQELEQKLRDYL-GGFGFQGDKVteetrrfSGGEKARLVLALIVWQ 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 494 TPQILILDEATASIDSGTEQAIQHALaaVREHTTLVVIAH-----RLSTivdaDTILVLHRGQaVEQGT-----HQQLLA 563
Cdd:PRK10636 448 RPNLLLLDEPTNHLDLDMRQALTEAL--IDFEGALVVVSHdrhllRSTT----DDLYLVHDGK-VEPFDgdledYQQWLS 520
|
....
gi 447178945 564 AQGR 567
Cdd:PRK10636 521 DVQK 524
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
341-537 |
9.09e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.39 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRldgrplsslshsalrqgvamv 420
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE--------------------- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 qqdpvvLADTF-LANVTLGRDI--SEERVWQA----LETVQLAElaRSMSDGIYTPL-----GEQGN---NLSVGQKQLL 485
Cdd:TIGR03719 381 ------IGETVkLAYVDQSRDAldPNKTVWEEisggLDIIKLGK--REIPSRAYVGRfnfkgSDQQKkvgQLSGGERNRV 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 486 ALARVLVETPQILILDEATASIDSGTEQAIQHALAAVRehTTLVVIAH------RLST 537
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA--GCAVVISHdrwfldRIAT 508
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
370-571 |
9.15e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 47.40 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIrldGRPLSSLSHSAlrqgvAMVQQDPVVLADTFLANVTlgRDISEERVWQA 449
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKP-----QYIKADYEGTVRDLLSSIT--KDFYTHPYFKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 450 letvqlaELARSMS-DGIYTplgEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSgtEQAIqHALAAVR---EH 525
Cdd:cd03237 98 -------EIAKPLQiEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV--EQRL-MASKVIRrfaEN 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447178945 526 T--TLVVIAHR--LSTIVdADTILVLHrGQAVEQG---THQQLLAAQGRYWQM 571
Cdd:cd03237 165 NekTAFVVEHDiiMIDYL-ADRLIVFE-GEPSVNGvanPPQSLRSGMNRFLKN 215
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
341-553 |
9.66e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 9.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDDNLvLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsslshsalrqgVAMV 420
Cdd:PRK11147 4 ISIHGAWLSFSDAPL-LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI-----------VARL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 421 QQDPV-VLADTFLANVTLG-RDISE--ERVWQALETVQ-------LAELAR-----------SMSDGIYTPLGEQG---- 474
Cdd:PRK11147 72 QQDPPrNVEGTVYDFVAEGiEEQAEylKRYHDISHLVEtdpseknLNELAKlqeqldhhnlwQLENRINEVLAQLGldpd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 475 ---NNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVRehTTLVVIAH------RLST-IVDADti 544
Cdd:PRK11147 152 aalSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ--GSIIFISHdrsfirNMATrIVDLD-- 227
|
....*....
gi 447178945 545 lvlhRGQAV 553
Cdd:PRK11147 228 ----RGKLV 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
374-508 |
9.71e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 374 GHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSALRQGVA-M-----------VQQDPVVLADTFlanvTLGRDI 441
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA-GDIATRRRVGyMsqafslygeltVRQNLELHARLF----HLPAAE 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447178945 442 SEERVWQALETVQLAELARSMSDgiytplgeqgnNLSVGQKQLLALARVLVETPQILILDEATASID 508
Cdd:NF033858 374 IAARVAEMLERFDLADVADALPD-----------SLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
371-553 |
1.05e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 371 ALVGHTGSGKSTLASLLMGYYP--LTEGEIRLDGRPLSSLSHSAL----RQGVAMVQQDPVVLADTFLANVTLGRDIS-E 443
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKQETFARIsgycEQNDIHSPQVTVRESLIYSAFLRLPKEVSkE 989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 444 ERVWQALETVQLAELaRSMSDGIYTPLGEQGnnLSVGQKQLLALARVLVETPQILILDEATASIDSgteQAIQHALAAVR 523
Cdd:PLN03140 990 EKMMFVDEVMELVEL-DNLKDAIVGLPGVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA---RAAAIVMRTVR 1063
|
170 180 190
....*....|....*....|....*....|....*.
gi 447178945 524 EHT----TLVVIAHRLST-IVDA-DTILVLHRGQAV 553
Cdd:PLN03140 1064 NTVdtgrTVVCTIHQPSIdIFEAfDELLLMKRGGQV 1099
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
357-556 |
1.10e-05 |
|
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: 46.49 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTL----ASLLMGYYPLtEGEIRLDGRPLSSLSHSALRQgVAMVQQDpvvlaDTFL 432
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLlkalANRTEGNVSV-EGDIHYNGIPYKEFAEKYPGE-IIYVSEE-----DVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 433 ANVTLGrdiseervwqaletvQLAELARSMsdgiytplgeQGNN----LSVGQKQLLALARVLVETPQILILDEATASID 508
Cdd:cd03233 96 PTLTVR---------------ETLDFALRC----------KGNEfvrgISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447178945 509 SGTE----QAIQHaLAAVREHTTLVVIAHRLSTIVDA-DTILVLHRGQAVEQG 556
Cdd:cd03233 151 SSTAleilKCIRT-MADVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQIYYG 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
331-566 |
1.30e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 331 NDDRPLQSGTIEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRldgrplssLSH 410
Cdd:PRK15064 310 EQDKKLHRNALEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK--------WSE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 411 SAlrqGVAMVQQDPvvlADTFLANVTLGRDISEERVWQALETVQLAELARSM--SDGIytplGEQGNNLSVGQKQLLALA 488
Cdd:PRK15064 381 NA---NIGYYAQDH---AYDFENDLTLFDWMSQWRQEGDDEQAVRGTLGRLLfsQDDI----KKSVKVLSGGEKGRMLFG 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 489 RVLVETPQILILDEATASIDSGTEQAIQHALAAVRehTTLVVIAH------RLSTIVdadtILVLHRGQAVEQGTHQQLL 562
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYE--GTLIFVSHdrefvsSLATRI----IEITPDGVVDFSGTYEEYL 524
|
....
gi 447178945 563 AAQG 566
Cdd:PRK15064 525 RSQG 528
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
332-520 |
3.07e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 332 DDRPlQSGTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGyypltegeirlDGRPLSSLSHS 411
Cdd:PLN03073 501 DDRP-GPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG-----------ELQPSSGTVFR 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 412 ALRQGVAMVQQ---DPVVLADT---FLANVTLGrdISEERVWQALETVQLA-ELA-RSMsdgiYTplgeqgnnLSVGQKQ 483
Cdd:PLN03073 569 SAKVRMAVFSQhhvDGLDLSSNpllYMMRCFPG--VPEQKLRAHLGSFGVTgNLAlQPM----YT--------LSGGQKS 634
|
170 180 190
....*....|....*....|....*....|....*..
gi 447178945 484 LLALARVLVETPQILILDEATASIDSGTEQAIQHALA 520
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV 671
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
332-521 |
4.60e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.84 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 332 DDRPLQSGT--IEVDNVSFAyRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS-- 407
Cdd:PRK13543 1 MIEPLHTAPplLAAHALAFS-RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 408 -LSHSALRQGVAMVQQDPVVLADTFLANVTLGRDiSEERVWQALETVQLAELARSMSdgiytplgeqgNNLSVGQKQLLA 486
Cdd:PRK13543 80 rSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRR-AKQMPGSALAIVGLAGYEDTLV-----------RQLSAGQKKRLA 147
|
170 180 190
....*....|....*....|....*....|....*
gi 447178945 487 LARVLVETPQILILDEATASIDSGTEQAIQHALAA 521
Cdd:PRK13543 148 LARLWLSPAPLWLLDEPYANLDLEGITLVNRMISA 182
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
369-563 |
4.76e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.41 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 369 FVALVGHTGSGKSTLASLLMGYYPLT--EGEIRLDGRplsSLSHSALRQgVAMVQQDPVVLAD-------TFLANVTLGR 439
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNR---KPTKQILKR-TGFVTQDDILYPHltvretlVFCSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 440 DISEERVWQALETVqLAELARSMSDGIYTplgeqGNN----LSVGQKQLLALARVLVETPQILILDEATASIDsgteqai 515
Cdd:PLN03211 172 SLTKQEKILVAESV-ISELGLTKCENTII-----GNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD------- 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 516 qhALAAVREHTTLVVIAHRLSTIVDA------------DTILVLHRGQAVEQGTHQQLLA 563
Cdd:PLN03211 239 --ATAAYRLVLTLGSLAQKGKTIVTSmhqpssrvyqmfDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
357-550 |
4.89e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLasLLMGYYPLTEGEIR-----------LDGRPLSSLSHS----------ALRQ 415
Cdd:PRK00635 1506 IQNLNVSAPLHSLVAISGVSGSGKTSL--LLEGFYKQACALIEkgpsvfseiifLDSHPQISSQRSdistyfdiapSLRN 1583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 416 GVAMVQQDPV--VLADTFLANVTLGR---------------------------------DISEERVWQA----------L 450
Cdd:PRK00635 1584 FYASLTQAKAlnISASMFSTNTKQGQcsdcwglgyqwidrafyalekrpcptcsgfriqPLAQEVVYEGkhfgqllqtpI 1663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 451 ETVQL---------AELARSMSDGI-YTPLGEQGNNLSVGQKQLLALARVLV---ETPQILILDEATASIDSGTEQAIQH 517
Cdd:PRK00635 1664 EEVAEtfpflkkiqKPLQALIDNGLgYLPLGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLV 1743
|
250 260 270
....*....|....*....|....*....|....
gi 447178945 518 ALAA-VREHTTLVVIAHRLSTIVDADTILVLHRG 550
Cdd:PRK00635 1744 QLRTlVSLGHSVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
47-188 |
5.74e-05 |
|
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: 45.39 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 47 SYFIDNMVAKNNLPLKVVAGLAAAYVglqLFAaglhYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVIS 126
Cdd:cd18601 48 STNVDIEDLDRDFNLGIYAGLTAATF---VFG----FLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILN 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447178945 127 RVTNDTEVIRDLYVTVVATVLRSAALV-GAMLVAMFSLDWrmalVAIMIFPVVLVVMVIyQRY 188
Cdd:cd18601 121 RFSKDIGHLDDLLPLTFLDFLQLLLQVvGVVLLAVVVNPW----VLIPVIPLVILFLFL-RRY 178
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
28-313 |
1.09e-04 |
|
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: 44.52 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 28 AVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDA 107
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 108 ALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAA-LVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQ 186
Cdd:cd18560 81 LHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLeLIVVSVVFAFHFGAWLALIVFLSVLLYGVFTIKVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 187 RYSTPIVRRV----RAYLADINDGfneIINGMSViQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSL 262
Cdd:cd18560 161 EWRTKFRRAAnkkdNEAHDIAVDS---LLNFETV-KYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 447178945 263 ILCGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVV 313
Cdd:cd18560 237 LTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLT 287
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
357-556 |
1.12e-04 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.79 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMgyypLTEGEIRLdgrpLSSLShSALRQGVAMVQQD---------PVVL 427
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTI----YAEGQRRY----VESLS-AYARQFLGQMDKPdvdsieglsPAIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 428 AD--TFLANV--TLGrDISE----ERVWQALetVQLAELARSMSD-GI-YTPLGEQGNNLSVGQKQLLALARVLVE--TP 495
Cdd:cd03270 82 IDqkTTSRNPrsTVG-TVTEiydyLRLLFAR--VGIRERLGFLVDvGLgYLTLSRSAPTLSGGEAQRIRLATQIGSglTG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447178945 496 QILILDEATASIDSGTEQAIQHALAAVREH-TTLVVIAHRLSTIVDADTILVL------HRGQAVEQG 556
Cdd:cd03270 159 VLYVLDEPSIGLHPRDNDRLIETLKRLRDLgNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
341-400 |
1.15e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 1.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYrDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL 400
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
341-508 |
1.93e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.35 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 341 IEVDNVSFAYRDdNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHsalRQGVA-- 418
Cdd:NF033858 2 ARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARH---RRAVCpr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 419 ---MVQqdpvvladtflanvTLGR----DIS----------------EERVWqaletvQLAELARSMsdGIYTPLGEQGN 475
Cdd:NF033858 78 iayMPQ--------------GLGKnlypTLSvfenldffgrlfgqdaAERRR------RIDELLRAT--GLAPFADRPAG 135
|
170 180 190
....*....|....*....|....*....|...
gi 447178945 476 NLSVGQKQLLALARVLVETPQILILDEATASID 508
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
43-187 |
5.76e-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: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 43 PLLISYFIDNMVAKNNLPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVvqQLRTDVMDAALRQPLSEFDTQPVG 122
Cdd:cd18779 22 PLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDT--QLTLGFLEHLLRLPYRFFQQRSTG 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447178945 123 QVISRVTNDTeVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQR 187
Cdd:cd18779 100 DLLMRLSSNA-TIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLATRR 163
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
357-384 |
8.29e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 8.29e-04
10 20
....*....|....*....|....*...
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLA 384
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSLA 39
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
357-383 |
1.63e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 1.63e-03
10 20
....*....|....*....|....*..
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTL 383
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTL 651
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
122-250 |
2.21e-03 |
|
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: 40.16 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 122 GQVISRVTNDTEVIRDLYVTVVATVLrsAALVGAMLVAMF--SLDWRMALVAIMIFPVVLVVM-VIYQRYSTPIVRRVRA 198
Cdd:cd18585 92 GDLLNRIVADIDTLDNLYLRVLSPPV--VALLVILATILFlaFFSPALALILLAGLLLAGVVIpLLFYRLGKKIGQQLVQ 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 447178945 199 YLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGF 250
Cdd:cd18585 170 LRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGL 221
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
357-538 |
2.29e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRpLSSLSHSALRQGVAmvqqdpvvladTFLANV- 435
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIAISAGLSGQL-----------TGIENIe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 436 --TLGRDISEERVWQAL-ETVQLAELArsmsDGIYTPLgeqgNNLSVGQKQLLALARVLVETPQILILDEAtasIDSGTE 512
Cdd:PRK13546 108 fkMLCMGFKRKEIKAMTpKIIEFSELG----EFIYQPV----KKYSSGMRAKLGFSINITVNPDILVIDEA---LSVGDQ 176
|
170 180 190
....*....|....*....|....*....|
gi 447178945 513 QAIQHALAAVRE----HTTLVVIAHRLSTI 538
Cdd:PRK13546 177 TFAQKCLDKIYEfkeqNKTIFFVSHNLGQV 206
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
41-245 |
5.19e-03 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain 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.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 39.12 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 41 SGPLLISYFIdNMVAKNNLPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQP 120
Cdd:cd18559 15 SGPSNLWLLL-WFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 121 VGQVISRVTNDTEVIRDLyvtvvATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQRYstpIVRRVRAYL 200
Cdd:cd18559 94 SGELVNLFSKDLDRVDSM-----APQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRV---YAASSRQLK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447178945 201 ADINDG-------FNEIINGMSVIQQFRQQARFGERMgEASRSHYMARMQTL 245
Cdd:cd18559 166 RLESVSkdpryklFNETLLGISVIKAFEWEEAFIRQV-DAKRDNELAYLPSI 216
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
357-561 |
5.44e-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: 40.00 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 357 LKNINLSVPSRNFVALVGHTGSGKSTLasLLMGYYPLTEGeiRLDGRPLSSLSHSALrQG------VAMVQQDPV----- 425
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTL--INDTLYPALAN--RLNGAKTVPGRYTSI-EGlehldkVIHIDQSPIgrtpr 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 426 ---------------VLADT------------FLANVTLGR--------------------------------------- 439
Cdd:TIGR00630 699 snpatytgvfdeireLFAETpeakvrgytpgrFSFNVKGGRceacqgdgvikiemhflpdvyvpcevckgkrynretlev 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 440 --------DISEERVWQALETVQ-LAELARS----MSDGI-YTPLGEQGNNLSVGQKQLLALARVL---VETPQILILDE 502
Cdd:TIGR00630 779 kykgkniaDVLDMTVEEAYEFFEaVPSISRKlqtlCDVGLgYIRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDE 858
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 503 ATASIDsgTEQAIQ-----HALaaVREHTTLVVIAHRLSTIVDADTILVL------HRGQAVEQGTHQQL 561
Cdd:TIGR00630 859 PTTGLH--FDDIKKllevlQRL--VDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
63-230 |
7.23e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, 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: 350043 [Multi-domain] Cd Length: 313 Bit Score: 38.70 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 63 VVAGLAAAYVGLQLFaaglhyaQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIrDLYV-- 140
Cdd:cd18599 63 VYGGSILVILLLSLI-------RGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEV-DVRLpf 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447178945 141 TVVATVLRSAALVGAMLVAMFSLDWrmalVAIMIFPVVlVVMVIYQRYSTPIVR-------RVRAYLadindgFNEI--- 210
Cdd:cd18599 135 TLENFLQNVLLVVFSLIIIAIVFPW----FLIALIPLA-IIFVFLSKIFRRAIRelkrlenISRSPL------FSHLtat 203
|
170 180
....*....|....*....|
gi 447178945 211 INGMSVIQQFRQQARFGERM 230
Cdd:cd18599 204 IQGLSTIHAFNKEKEFLSKF 223
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
357-384 |
7.91e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 7.91e-03
10 20
....*....|....*....|....*....
gi 447178945 357 LKNINLSVPsRN-FVALVGHTGSGKSTLA 384
Cdd:PRK00349 16 LKNIDLDIP-RDkLVVFTGLSGSGKSSLA 43
|
|
| |
