|
Name |
Accession |
Description |
Interval |
E-value |
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-547 |
3.39e-121 |
|
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: 373.01 E-value: 3.39e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 10 TPFQRVVKLLSFEKQDIFLLFYLTAAYGVLGIATPVAVQTMVNIVTMGGVLQPLYVVGVILFCLLALSGTIYVIESFLVE 89
Cdd:COG2274 142 FGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 90 MIQRRIFVRHSLQIAKNTEQIHISVYDQFNPVELVNRYFDIQTVQKSVATLLTVGLTALLQGLIGSIVLLFYSLYFGILV 169
Cdd:COG2274 222 RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 170 ILMMIVLWGIVFGLGKHAEETAIKESKAKYEMAAWLETIARNKWLSKFYGARQRNSANTAQLAEGYLSVRGKHFKVLMMQ 249
Cdd:COG2274 302 LLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 250 LIGAVSLYALIGTGMLILGGTLVIKGQINLGQFVAAELIIFGVLSAFVRFVTKLEYFYDLLAAVDKVGVLETLPVERSGD 329
Cdd:COG2274 382 STLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEG 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 330 H--QSGEEGYKTLKVNQLTFRHADQ-PALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQ 406
Cdd:COG2274 462 RskLSLPRLKGDIELENVSFRYPGDsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 407 LDLSHLRDRIG-VANKVEWQHGSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLM 485
Cdd:COG2274 542 IDPASLRRQIGvVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLA 621
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 902766092 486 LARAMLGKPDVLIIDSLLDQLSQHELDQVLMLLKRQQQDWILLITTRYQHIAQHCQQVVNLQ 547
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLD 683
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-504 |
4.32e-66 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 225.04 E-value: 4.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 5 KPASLTPFQRVVKLLSFEKQDIFLLFYLTAAYGVLGIATPVAVQTMVNIVTMGGVLQPLYVVGVILFCLLALSGTIYVIE 84
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 85 SFLVEMIQRRIFVRHSLQIAKNTEQIHISVYDQFNPVELVNRY-FDIQTVQKSVATLLTVGLTALLQGLIGSIVLLFYSL 163
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLtNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 164 YFGILVILMMIVLWGIVFGLGKHAEETAIKESKAKYEMAAWLETIARNKWLSKFYGARQRNSANTAQLAEGYLSVRGKHF 243
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 244 KVL-----MMQLIGAVSLYALigtgmLILGGTLVIKGQINLGQFVAAELIIFGVLSAFVRFVTKLEYFYDLLAAVDKV-G 317
Cdd:COG1132 242 RLSalffpLMELLGNLGLALV-----LLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIfE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 318 VLETLPVERSGDH-QSGEEGYKTLKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGH 396
Cdd:COG1132 317 LLDEPPEIPDPPGaVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 397 VSYNDIDVRQLDLSHLRDRIGVANkvewQ-----HGSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTD 471
Cdd:COG1132 397 ILIDGVDIRDLTLESLRRQIGVVP----QdtflfSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGE 472
|
490 500 510
....*....|....*....|....*....|....*.
gi 902766092 472 FGAPMTHTQLQRLMLARAMLGKPDVLIID---SLLD 504
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDeatSALD 508
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
216-560 |
1.23e-40 |
|
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: 154.92 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 216 KFYGARQRNSANTAQLAEGYlsvRGKHFKVLMMQL--IGAVSLYALIGTGML-ILGGTLVIKGQINLGQFVAAeLIifgv 292
Cdd:COG4988 211 KLFGRAKAEAERIAEASEDF---RKRTMKVLRVAFlsSAVLEFFASLSIALVaVYIGFRLLGGSLTLFAALFV-LL---- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 293 LSA-FVRFVTKLEYFY----DLLAAVDKV-GVLET-LPVERSGDHQSGEEGYKTLKVNQLTFRHADQPALVSNISFTLHR 365
Cdd:COG4988 283 LAPeFFLPLRDLGSFYharaNGIAAAEKIfALLDApEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPP 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 366 GQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG-VANKVEWQHGSILDNLKLQRPDIALDD 444
Cdd:COG4988 363 GERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAwVPQNPYLFAGTIRENLRLGRPDASDEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 445 VIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQ 521
Cdd:COG4988 443 LEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDeptAHLDAETEAEILQALRRLAKG 522
|
330 340 350
....*....|....*....|....*....|....*....
gi 902766092 522 QQdwILLITTRYQHIAQhCQQVVNLQSKTLTDHtgGQHE 560
Cdd:COG4988 523 RT--VILITHRLALLAQ-ADRILVLDDGRIVEQ--GTHE 556
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
122-500 |
2.73e-35 |
|
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: 139.03 E-value: 2.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 122 ELVNRYF-DIQTVQKSVATLLTVGLTALLQGLIGSIVLLFYSLYFGILVILMMIV---LWGIVFGLGKHAEETAIKESKA 197
Cdd:TIGR02868 111 DLLGRLGaDVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLagfVAPLVSLRAARAAEQALARLRG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 198 KY--EMAAWLEtiARNKWlsKFYGA-----RQRNSANTAQLAEGYLSVRGKHFKVLMMQLIGAVSLyaligTGMLILGGT 270
Cdd:TIGR02868 191 ELaaQLTDALD--GAAEL--VASGAlpaalAQVEEADRELTRAERRAAAATALGAALTLLAAGLAV-----LGALWAGGP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 271 LVIKGQINlGQFVAAelIIFGVLSAFvrfvtklEYFYDLLAAVDKVG--------VLETLPVERSGDHQSGE------EG 336
Cdd:TIGR02868 262 AVADGRLA-PVTLAV--LVLLPLAAF-------EAFAALPAAAQQLTrvraaaerIVEVLDAAGPVAEGSAPaagavgLG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 337 YKTLKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRI 416
Cdd:TIGR02868 332 KPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRV 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 417 GV-ANKVEWQHGSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPD 495
Cdd:TIGR02868 412 SVcAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAP 491
|
....*
gi 902766092 496 VLIID 500
Cdd:TIGR02868 492 ILLLD 496
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
311-546 |
8.36e-30 |
|
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: 123.17 E-value: 8.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 311 AAVDKVGVLETLPVERSGDHQSGEEGYKTLKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMR 390
Cdd:TIGR02857 293 AAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 391 QPVQGHVSYNDIDVRQLDLSHLRDRIGvankveW--QH-----GSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLPN 463
Cdd:TIGR02857 373 DPTEGSIAVNGVPLADADADSWRDQIA------WvpQHpflfaGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQ 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 464 GIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID----SLLDQLSQHELDQVLMLLKRQqqdwILLITTRYQHIAQH 539
Cdd:TIGR02857 447 GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDeptaHLDAETEAEVLEALRALAQGR----TVLLVTHRLALAAL 522
|
....*..
gi 902766092 540 CQQVVNL 546
Cdd:TIGR02857 523 ADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
340-533 |
9.30e-30 |
|
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: 116.53 E-value: 9.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPAL-VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG- 417
Cdd:cd03245 3 IEFRNVSFSYPNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VANKVEWQHGSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVL 497
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 902766092 498 IID---SLLDQLSQHELDQVLMLLKRQQQdwILLITTRY 533
Cdd:cd03245 163 LLDeptSAMDMNSEERLKERLRQLLGDKT--LIIITHRP 199
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
353-500 |
2.79e-29 |
|
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: 115.40 E-value: 2.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 353 PALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGVANKVEWQ-HGSILD 431
Cdd:cd03254 17 PVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLfSGTIME 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 902766092 432 NLKLQRPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID 500
Cdd:cd03254 96 NIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILD 164
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
345-515 |
1.30e-28 |
|
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: 113.86 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 345 LTFRH-ADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG-VANKV 422
Cdd:cd03251 6 VTFRYpGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGlVSQDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 423 EWQHGSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID-- 500
Cdd:cd03251 86 FLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDea 165
|
170
....*....|....*.
gi 902766092 501 -SLLDQLSQHELDQVL 515
Cdd:cd03251 166 tSALDTESERLVQAAL 181
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
340-546 |
1.25e-27 |
|
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: 109.01 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALV-SNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGV 418
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 ANkvewQ-----HGSILDNLklqrpdialddvievlqvlglwqeiskLPNGietvltdfgapmthtQLQRLMLARAMLGK 493
Cdd:cd03228 81 VP----QdpflfSGTIRENI---------------------------LSGG---------------QRQRIAIARALLRD 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 902766092 494 PDVLIID---SLLDQLSQHELDQVlmLLKRQQQDWILLITTRYQHIaQHCQQVVNL 546
Cdd:cd03228 115 PPILILDeatSALDPETEALILEA--LRALAKGKTVIVIAHRLSTI-RDADRIIVL 167
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
356-500 |
3.31e-26 |
|
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: 104.27 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGV--ANKVEWQHGSILDNL 433
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYvfQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 902766092 434 KLQRPDIAL------DDVIEVLQVLGlwqeiskLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID 500
Cdd:pfam00005 81 RLGLLLKGLskrekdARAEEALEKLG-------LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
345-513 |
4.93e-26 |
|
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: 106.42 E-value: 4.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 345 LTFRH-ADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGVANKVE 423
Cdd:cd03252 6 VRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 424 -WQHGSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID-- 500
Cdd:cd03252 86 vLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDea 165
|
170
....*....|....
gi 902766092 501 -SLLDQLSQHELDQ 513
Cdd:cd03252 166 tSALDYESEHAIMR 179
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
351-516 |
2.81e-25 |
|
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: 104.54 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 351 DQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGVankVEwQH---- 426
Cdd:cd03249 15 DVPIL-KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL---VS-QEpvlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 427 -GSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID---SL 502
Cdd:cd03249 90 dGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDeatSA 169
|
170
....*....|....*...
gi 902766092 503 LDQLS----QHELDQVLM 516
Cdd:cd03249 170 LDAESeklvQEALDRAMK 187
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
340-547 |
4.59e-25 |
|
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: 101.91 E-value: 4.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHAD-QPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG- 417
Cdd:cd03246 1 LEVENVSFRYPGaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VANKVEWQHGSILDNLklqrpdialddvievlqvlglwqeiskLPNGietvltdfgapmthtQLQRLMLARAMLGKPDVL 497
Cdd:cd03246 81 LPQDDELFSGSIAENI---------------------------LSGG---------------QRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 902766092 498 IID---SLLDQLSQHELDQVLMLLKRQQQDwILLITTRYQHIAQhCQQVVNLQ 547
Cdd:cd03246 119 VLDepnSHLDVEGERALNQAIAALKAAGAT-RIVIAHRPETLAS-ADRILVLE 169
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
68-547 |
1.31e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.19 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 68 VILFCLLALSGTIYV---IESFLVEM--IQRRIfvrhSLQIAKNTEQIHISVYDQFNPVELVNRYF-DIQTVQKSVATLL 141
Cdd:TIGR00958 204 IFFMCLLSIASSVSAglrGGSFNYTMarINLRI----REDLFRSLLRQDLGFFDENKTGELTSRLSsDTQTMSRSLSLNV 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 142 TVGLTALLQGLIGSIVLLFYSLYFGILVILMM--IVLWGIVFG-----LGKHAEETAIKESKAKYEMAAWLETI----AR 210
Cdd:TIGR00958 280 NVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLplVFLAEKVFGkryqlLSEELQEAVAKANQVAEEALSGMRTVrsfaAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 211 NKWLSKFYGA--RQRNSANTAQLAE-GYLSVRgkhfKVLMMqligavslyaLIGTGMLILGGTLVIKGQINLGQFVAAEL 287
Cdd:TIGR00958 360 EGEASRFKEAleETLQLNKRKALAYaGYLWTT----SVLGM----------LIQVLVLYYGGQLVLTGKVSSGNLVSFLL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 288 IIFGVLSAfvrfVTKLEYFY-DLLAAVDKV-GVLETLPVERSGDHqSGEEGYKTLKVNqLTFRHA--------DQPALvS 357
Cdd:TIGR00958 426 YQEQLGEA----VRVLSYVYsGMMQAVGASeKVFEYLDRKPNIPL-TGTLAPLNLEGL-IEFQDVsfsypnrpDVPVL-K 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 358 NISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG-VANKVEWQHGSILDNLKLQ 436
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVAlVGQEPVLFSGSVRENIAYG 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 437 RPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQ 513
Cdd:TIGR00958 579 LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDeatSALDAECEQLLQE 658
|
490 500 510
....*....|....*....|....*....|....
gi 902766092 514 vlmlLKRQQQDWILLITTRYqHIAQHCQQVVNLQ 547
Cdd:TIGR00958 659 ----SRSRASRTVLLIAHRL-STVERADQILVLK 687
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
349-518 |
1.69e-23 |
|
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: 99.23 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 349 HADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGVA--NKVEWqH 426
Cdd:cd03253 11 DPGRPVL-KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVpqDTVLF-N 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 427 GSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID---SLL 503
Cdd:cd03253 89 DTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDeatSAL 168
|
170
....*....|....*
gi 902766092 504 DQLSQHELDQVLMLL 518
Cdd:cd03253 169 DTHTEREIQAALRDV 183
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
326-547 |
2.37e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 104.16 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 326 RSGDHQSGEEGYKTLKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMrQPVQGHVSYNDIDVR 405
Cdd:PRK11174 336 QQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 406 QLDLSHLRDRIG-VANKVEWQHGSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRL 484
Cdd:PRK11174 415 ELDPESWRKHLSwVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 902766092 485 MLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQdwILLITTRYQHIAQhCQQVVNLQ 547
Cdd:PRK11174 495 ALARALLQPCQLLLLDeptASLDAHSEQLVMQALNAASRRQT--TLMVTHQLEDLAQ-WDQIWVMQ 557
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
341-546 |
1.62e-22 |
|
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: 95.61 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 341 KVNQLTFRHADQPALV-SNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG-- 417
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGlv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 ------------VANKVEWqhGsiLDNLKLQRPDIAlDDVIEVLQVLGLW----QEISKLPNGietvltdfgapmthtQL 481
Cdd:cd03225 81 fqnpddqffgptVEEEVAF--G--LENLGLPEEEIE-ERVEEALELVGLEglrdRSPFTLSGG---------------QK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 902766092 482 QRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDwILLITTRYQHIAQHCQQVVNL 546
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDeptAGLDPAGRRELLELLKKLKAEGKT-IIIVTHDLDLLLELADRVIVL 207
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
262-504 |
2.17e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.19 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 262 TGMLILGGTLVIKGQINLGQFVA----AELIIfGVLSAFVRFVT-------KLEYFYDLLaavDKVGVLETLPVERSGDH 330
Cdd:PRK13657 255 LAILVLGAALVQKGQLRVGEVVAfvgfATLLI-GRLDQVVAFINqvfmaapKLEEFFEVE---DAVPDVRDPPGAIDLGR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 331 QSGEegyktLKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLS 410
Cdd:PRK13657 331 VKGA-----VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 411 HLRDRIGVA-------NKvewqhgSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQR 483
Cdd:PRK13657 406 SLRRNIAVVfqdaglfNR------SIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQR 479
|
250 260
....*....|....*....|....
gi 902766092 484 LMLARAMLGKPDVLIID---SLLD 504
Cdd:PRK13657 480 LAIARALLKDPPILILDeatSALD 503
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
340-544 |
2.75e-22 |
|
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: 95.48 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG-- 417
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGlv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 --------VANKVEwqhgsilD-------NLKLqRPDIALDDVIEVLQVLGLW----QEISKLPNGietvltdfgapmth 478
Cdd:COG1122 81 fqnpddqlFAPTVE-------EdvafgpeNLGL-PREEIRERVEEALELVGLEhladRPPHELSGG-------------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 902766092 479 tQLQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDwILLITTRYQHIAQHCQQVV 544
Cdd:COG1122 139 -QKQRVAIAGVLAMEPEVLVLDeptAGLDPRGRRELLELLKRLNKEGKT-VIIVTHDLDLVAELADRVI 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
340-544 |
7.18e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 94.75 E-value: 7.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPAlVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQlDLSHLRDRIGVA 419
Cdd:COG1131 1 IEVRGLTKRYGDKTA-LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 --NKVEWQHGSILDNLKLQ------RPDIALDDVIEVLQVLGLW----QEISKLPNGietvltdfgapmthtQLQRLMLA 487
Cdd:COG1131 79 pqEPALYPDLTVRENLRFFarlyglPRKEARERIDELLELFGLTdaadRKVGTLSGG---------------MKQRLGLA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 902766092 488 RAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQdwILLITTRY-QHIAQHCQQVV 544
Cdd:COG1131 144 LALLHDPELLILDeptSGLDPEARRELWELLRELAAEGK--TVLLSTHYlEEAERLCDRVA 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
308-544 |
1.66e-21 |
|
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: 98.05 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 308 DLLAAVDKVGVLETLPVERSGDHQSGEEGYKTLKVNQLTFRHADQPA----LVSNISFTLHRGQSLAVIGALGSGKTTLL 383
Cdd:COG1123 229 EILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGKSTLA 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 384 ELITGMRQPVQGHVSYNDIDVRQL---DLSHLRDRIGV-----------ANKVEWQHGSILDNLKLQRPDIALDDVIEVL 449
Cdd:COG1123 309 RLLLGLLRPTSGSILFDGKDLTKLsrrSLRELRRRVQMvfqdpysslnpRMTVGDIIAEPLRLHGLLSRAERRERVAELL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 450 QVLGLWQE-ISKLPngietvltdfgapmtHT----QLQRLMLARAMLGKPDVLIID---SLLDQLSQHeldQVLMLLKRQ 521
Cdd:COG1123 389 ERVGLPPDlADRYP---------------HElsggQRQRVAIARALALEPKLLILDeptSALDVSVQA---QILNLLRDL 450
|
250 260 270
....*....|....*....|....*....|
gi 902766092 522 QQDW---ILLITtryqH----IAQHCQQVV 544
Cdd:COG1123 451 QRELgltYLFIS----HdlavVRYIADRVA 476
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
340-547 |
1.97e-21 |
|
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: 97.67 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQP-ALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQP---VQGHVSYNDIDVRQLDLSHLRDR 415
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 416 IG----------VANKVEWQHGSILDNLKLQRPDIAlDDVIEVLQVLGLWQEISKLPngietvltdfgapmtHT----QL 481
Cdd:COG1123 85 IGmvfqdpmtqlNPVTVGDQIAEALENLGLSRAEAR-ARVLELLEAVGLERRLDRYP---------------HQlsggQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 902766092 482 QRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLITTRYQHIAQHCQQVVNLQ 547
Cdd:COG1123 149 QRVAIAMALALDPDLLIADeptTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMD 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
340-546 |
1.60e-20 |
|
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: 89.85 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPaLVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGVA 419
Cdd:COG4133 3 LEAENLSCRRGERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 nkvewqhgsildnlklqrPDIALDDVIEVLQVLGLWQEISKLPNG---IETVLTDFG-APMTHT--------QLQRLMLA 487
Cdd:COG4133 82 ------------------HADGLKPELTVRENLRFWAALYGLRADreaIDEALEAVGlAGLADLpvrqlsagQKRRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 902766092 488 RAMLGKPDVLIID---SLLDQLSQHELDQvlMLLKRQQQDWILLITTrYQHIAQHCQQVVNL 546
Cdd:COG4133 144 RLLLSPAPLWLLDepfTALDAAGVALLAE--LIAAHLARGGAVLLTT-HQPLELAAARVLDL 202
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
255-530 |
2.36e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 94.78 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 255 SLYALIGTGML--ILGGT-LVIKGQINLGQfvaaeliifgvLSAFVRFV-------TKLEYFYDLL----AAVDKV-GVL 319
Cdd:PRK10789 226 TIYIAIGMANLlaIGGGSwMVVNGSLTLGQ-----------LTSFVMYLglmiwpmLALAWMFNIVergsAAYSRIrAML 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 320 ETLPVERSGDhQSGEEGYKTLKVN--QLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHV 397
Cdd:PRK10789 295 AEAPVVKDGS-EPVPEGRGELDVNirQFTYPQTDHPAL-ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 398 SYNDIDVRQLDLSHLRDRIGVANKVEWQHG-SILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPM 476
Cdd:PRK10789 373 RFHDIPLTKLQLDSWRSRLAVVSQTPFLFSdTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVML 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 902766092 477 THTQLQRLMLARAMLGKPDVLIIDSLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIIS 506
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
340-530 |
2.61e-20 |
|
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: 89.87 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQL--TFRHADQP-ALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDR- 415
Cdd:cd03257 2 LEVKNLsvSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 416 --IGV-----------ANKVEWQhgsILDNLKLQRPDIALDD----VIEVLQVLGLwqeisklpngIETVLTDFGAPMTH 478
Cdd:cd03257 82 keIQMvfqdpmsslnpRMTIGEQ---IAEPLRIHGKLSKKEArkeaVLLLLVGVGL----------PEEVLNRYPHELSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 902766092 479 TQLQRLMLARAMLGKPDVLIID---SLLDQLSQhelDQVLMLLKRQQQDW---ILLIT 530
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADeptSALDVSVQ---AQILDLLKKLQEELgltLLFIT 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
340-546 |
5.54e-20 |
|
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: 87.45 E-value: 5.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQlDLSHLRDRIGVA 419
Cdd:cd03230 1 IEVRNLSKRYGKKTAL-DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 nkveWQHGSILDNLKlqrpdialddVIEVLqvlglwqeisKLPNGietvltdfgapmthtQLQRLMLARAMLGKPDVLII 499
Cdd:cd03230 79 ----PEEPSLYENLT----------VRENL----------KLSGG---------------MKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 902766092 500 D---SLLDQLSQHELDQvlMLLKRQQQDWILLITTRY-QHIAQHCQQVVNL 546
Cdd:cd03230 120 DeptSGLDPESRREFWE--LLRELKKEGKTILLSSHIlEEAERLCDRVAIL 168
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
340-548 |
6.63e-20 |
|
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: 88.68 E-value: 6.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPA--LVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG 417
Cdd:cd03248 12 VKFQNVTFAYPTRPDtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 -VANKVEWQHGSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDV 496
Cdd:cd03248 92 lVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 497 LIID---SLLDQLSQHELDQVLmllkrqqQDW-----ILLITTRYQHIaQHCQQVVNLQS 548
Cdd:cd03248 172 LILDeatSALDAESEQQVQQAL-------YDWperrtVLVIAHRLSTV-ERADQILVLDG 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
340-551 |
6.68e-20 |
|
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: 88.32 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFR----HADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD---LSHL 412
Cdd:cd03255 1 IELKNLSKTygggGEKVQAL-KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 413 R-DRIGVankVEWQHG-----SILDNLKL------QRPDIALDDVIEVLQVLGLWQEISKLPN----Gietvltdfgapm 476
Cdd:cd03255 80 RrRHIGF---VFQSFNllpdlTALENVELplllagVPKKERRERAEELLERVGLGDRLNHYPSelsgG------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 477 thtQLQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLITtryqH---IAQHCQQVVNLQSKT 550
Cdd:cd03255 145 ---QQQRVAIARALANDPKIILADeptGNLDSETGKEVMELLRELNKEAGTTIVVVT----HdpeLAEYADRIIELRDGK 217
|
.
gi 902766092 551 L 551
Cdd:cd03255 218 I 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
340-544 |
9.40e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 88.61 E-value: 9.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQldlshLRDRIG-V 418
Cdd:COG1121 7 IELENLTVSYGGRPVL-EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 AnkvewqhgsildnlklQRPDIALDDVIEVLQV--LGLWQEIS--KLPNG---------IETV-LTDF----------Ga 474
Cdd:COG1121 81 P----------------QRAEVDWDFPITVRDVvlMGRYGRRGlfRRPSRadreavdeaLERVgLEDLadrpigelsgG- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 902766092 475 pmthtQLQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDwILLITTRYQHIAQHCQQVV 544
Cdd:COG1121 144 -----QQQRVLLARALAQDPDLLLLDepfAGVDAATEEALYELLRELRREGKT-ILVVTHDLGAVREYFDRVL 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
341-544 |
1.72e-19 |
|
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: 85.37 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 341 KVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGVan 420
Cdd:cd00267 1 EIENLSFRYGGRTAL-DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 421 kvewqhgsildnlklqrpdialddvieVLQVLGlwqeisklpnGietvltdfgapmthtQLQRLMLARAMLGKPDVLIID 500
Cdd:cd00267 78 ---------------------------VPQLSG----------G---------------QRQRVALARALLLNPDLLLLD 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 902766092 501 ---SLLDQLSQHELDQVLMLLKRQQQdwILLITTRYQHIAQHCQQVV 544
Cdd:cd00267 106 eptSGLDPASRERLLELLRELAEEGR--TVIIVTHDPELAELAADRV 150
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
340-548 |
2.55e-19 |
|
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: 87.55 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRH---ADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRI 416
Cdd:COG1124 2 LEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 417 GVAnkveWQHG-SILDnlklqrPDIALDDVI-EVLQVLGlwqeISKLPNGIETVLTDFGAPMT------HT----QLQRL 484
Cdd:COG1124 82 QMV----FQDPyASLH------PRHTVDRILaEPLRIHG----LPDREERIAELLEQVGLPPSfldrypHQlsggQRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 902766092 485 MLARAMLGKPDVLIID---SLLDQLSQhelDQVLMLLKRQQQDW---ILLITtryqH---IAQH-CQQVVNLQS 548
Cdd:COG1124 148 AIARALILEPELLLLDeptSALDVSVQ---AEILNLLKDLREERgltYLFVS----HdlaVVAHlCDRVAVMQN 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
340-500 |
2.67e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 86.64 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQL---DLSHLRDRI 416
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 417 GV--------ANKvewqhgSILDNLKL------QRPDIALDDVIEVLQVLGLWQEISKLPNgietvltdfgapmthtQL- 481
Cdd:COG2884 82 GVvfqdfrllPDR------TVYENVALplrvtgKSRKEIRRRVREVLDLVGLSDKAKALPH----------------ELs 139
|
170 180
....*....|....*....|...
gi 902766092 482 ----QRLMLARAMLGKPDVLIID 500
Cdd:COG2884 140 ggeqQRVAIARALVNRPELLLAD 162
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
340-500 |
2.93e-19 |
|
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: 86.78 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALV-SNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGV 418
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVlKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 ANkvewQH-----GSILDNL--KLQRPDialDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAML 491
Cdd:cd03244 83 IP----QDpvlfsGTIRSNLdpFGEYSD---EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
....*....
gi 902766092 492 GKPDVLIID 500
Cdd:cd03244 156 RKSKILVLD 164
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
340-547 |
3.70e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 86.64 E-value: 3.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRH----ADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD---LSHL 412
Cdd:COG1136 5 LELRNLTKSYgtgeGEVTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 413 R-DRIGVAnkveWQHG------SILDNLKL------QRPDIALDDVIEVLQVLGLWQEISKLPN----Gietvltdfgap 475
Cdd:COG1136 84 RrRHIGFV----FQFFnllpelTALENVALplllagVSRKERRERARELLERVGLGDRLDHRPSqlsgG----------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 476 mthtQLQRLMLARAMLGKPDVLIID---SLLDQLSQhelDQVLMLLKRQQQDW---ILLITtryqH---IAQHCQQVVNL 546
Cdd:COG1136 149 ----QQQRVAIARALVNRPKLILADeptGNLDSKTG---EEVLELLRELNRELgttIVMVT----HdpeLAARADRVIRL 217
|
.
gi 902766092 547 Q 547
Cdd:COG1136 218 R 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
341-552 |
7.94e-19 |
|
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: 84.41 E-value: 7.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 341 KVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGVan 420
Cdd:cd03214 1 EVENLSVGYGGRTVL-DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 421 kvewqhgsildnlklqrpdialddVIEVLQVLGLW----QEISKLPNGietvltdfgapmthtQLQRLMLARAMLGKPDV 496
Cdd:cd03214 78 ------------------------VPQALELLGLAhladRPFNELSGG---------------ERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 902766092 497 LIID---SLLDQLSQHELDQVLMLLKRQQQDWILLITTRYQHIAQHCQQVVNLQSKTLT 552
Cdd:cd03214 119 LLLDeptSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
340-530 |
1.85e-18 |
|
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: 85.04 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG-V 418
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 ANKVE-WQHGSILDN-------LKLQRPDIAlDDVIEVLQVLGLwqeisklpnGIETVLTDFGAPMTHTQLQRLMLARAM 490
Cdd:cd03295 81 IQQIGlFPHMTVEENialvpklLKWPKEKIR-ERADELLALVGL---------DPAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 902766092 491 LGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:cd03295 151 AADPPLLLMDepfGALDPITRDQLQEEFKRLQQELGKTIVFVT 193
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
342-530 |
1.23e-17 |
|
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: 82.16 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 342 VNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQL---DLSHLRDRIGV 418
Cdd:cd03261 3 LRGLTKSFGGRTVL-KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 AnkveWQHG------SILDN--------LKLQRPDIAlDDVIEVLQVLGLWQEISKLPngietvltdfgapmthTQL--- 481
Cdd:cd03261 82 L----FQSGalfdslTVFENvafplrehTRLSEEEIR-EIVLEKLEAVGLRGAEDLYP----------------AELsgg 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 902766092 482 --QRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:cd03261 141 mkKRVALARALALDPELLLYDeptAGLDPIASGVIDDLIRSLKKELGLTSIMVT 194
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
137-538 |
5.18e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.11 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 137 VATLLTVGLTALLQGLIGSIVLLFyslyFGILVILMMIVLWgIVFGLGKHAEETAIkESKAKY--EMAAWLETIA----- 209
Cdd:PRK11160 143 AALVVILVLTIGLSFFDLTLALTL----GGILLLLLLLLPL-LFYRLGKKPGQDLT-HLRAQYrvQLTEWLQGQAeltlf 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 210 ------RNK-------WLskfygARQRNSANTAQLAEGylsvrgkhfkvlMMQLIGAVSLyaligTGMLILGGTLViKGQ 276
Cdd:PRK11160 217 gaedryRQQleqteqqWL-----AAQRRQANLTGLSQA------------LMILANGLTV-----VLMLWLAAGGV-GGN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 277 INLGQFVAaeLIIFGVLSAF-------VRFvtklEYFYDLLAAVDKVG--VLETLPVERSGDHQSgEEGYKTLKVNQLTF 347
Cdd:PRK11160 274 AQPGALIA--LFVFAALAAFealmpvaGAF----QHLGQVIASARRINeiTEQKPEVTFPTTSTA-AADQVSLTLNNVSF 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 348 RHADQPALV-SNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGVAN-KVEWQ 425
Cdd:PRK11160 347 TYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSqRVHLF 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 426 HGSILDNLKLQRPDIALDDVIEVLQVLGLwqeiSKL---PNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIIDSL 502
Cdd:PRK11160 427 SATLRDNLLLAAPNASDEALIEVLQQVGL----EKLledDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEP 502
|
410 420 430
....*....|....*....|....*....|....*..
gi 902766092 503 LDQLSQHELDQVLMLLKRQQQDWILL-ITTRYQHIAQ 538
Cdd:PRK11160 503 TEGLDAETERQILELLAEHAQNKTVLmITHRLTGLEQ 539
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
340-544 |
5.79e-17 |
|
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: 79.44 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHAD----QPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNdidvrqldlshlrDR 415
Cdd:cd03250 1 ISVEDASFTWDSgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP-------------GS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 416 IGVANKVEW-QHGSILDNLKLQRP-DIA-LDDVIEVLQvlgLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLG 492
Cdd:cd03250 68 IAYVSQEPWiQNGTIRENILFGKPfDEErYEKVIKACA---LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 902766092 493 KPDVLIID---SLLD-QLSQHELDQVLM-LLKRQQQdwILLITTRYQHIAqHCQQVV 544
Cdd:cd03250 145 DADIYLLDdplSAVDaHVGRHIFENCILgLLLNNKT--RILVTHQLQLLP-HADQIV 198
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
340-530 |
6.01e-17 |
|
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: 78.77 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDlshlrdrigva 419
Cdd:cd03229 1 LELKNVSKRYGQKTVL-NDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 nkvewqhgsilDNLKLQRPDIALddvieVLQVLGLWQEIsklpngieTVLTDFGAPMTHTQLQRLMLARAMLGKPDVLII 499
Cdd:cd03229 69 -----------DELPPLRRRIGM-----VFQDFALFPHL--------TVLENIALGLSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190
....*....|....*....|....*....|....
gi 902766092 500 D---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:cd03229 125 DeptSALDPITRREVRALLKSLQAQLGITVVLVT 158
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
354-544 |
6.86e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.89 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 354 ALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLR-----------DRIGVAN-- 420
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrrdiqmvfqDSISAVNpr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 421 -KVEWQHGSILDNLKLQRPDIALDDVIEVLQVLGLWQEI-SKLPngietvltdfgAPMTHTQLQRLMLARAMLGKPDVLI 498
Cdd:PRK10419 106 kTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVlDKRP-----------PQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 902766092 499 IDSLLDQLSQHELDQVLMLLKRQQQDW---ILLITTRYQHIAQHCQQVV 544
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQFgtaCLFITHDLRLVERFCQRVM 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
340-531 |
8.42e-17 |
|
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: 79.53 E-value: 8.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMR-----QPVQGHVSYN--DIDVRQLDLSHL 412
Cdd:cd03260 1 IELRDLNVYYGDKHAL-KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDgkDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 413 RDRIGVAnkveWQH-----GSILDN----LKLQ--RPDIALDDVIE-VLQVLGLWQEISKLPNGIEtvltdfgapMTHTQ 480
Cdd:cd03260 80 RRRVGMV----FQKpnpfpGSIYDNvaygLRLHgiKLKEELDERVEeALRKAALWDEVKDRLHALG---------LSGGQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 902766092 481 LQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQvlmLLKRQQQDWILLITT 531
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDeptSALDPISTAKIEE---LIAELKKEYTIVIVT 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
340-554 |
1.33e-16 |
|
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: 79.52 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALVsNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLsHLRDRIGV- 418
Cdd:COG4555 2 IEVENLSKKYGKVPALK-DVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGVl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 -ANKVEWQHGSILDNLKL-----QRPDIALDDVIE-VLQVLGLW----QEISKLPNGietvltdfgapmthtQLQRLMLA 487
Cdd:COG4555 80 pDERGLYDRLTVRENIRYfaelyGLFDEELKKRIEeLIELLGLEefldRRVGELSTG---------------MKKKVALA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 902766092 488 RAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKrqQQDWILLITTR-YQHIAQHCQQVVNLQSKTLTDH 554
Cdd:COG4555 145 RALVHDPKVLLLDeptNGLDVMARRLLREILRALK--KEGKTVLFSSHiMQEVEALCDRVVILHKGKVVAQ 213
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
340-520 |
2.06e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 82.37 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRH--ADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG 417
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPAL-RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 -VANKVEWQHGSILDNLKLQRPDIALDDVIEVLQVLGLWQE-ISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPD 495
Cdd:PRK11176 421 lVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180
....*....|....*....|....*...
gi 902766092 496 VLIID---SLLDQLSQHELDQVLMLLKR 520
Cdd:PRK11176 501 ILILDeatSALDTESERAIQAALDELQK 528
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
340-507 |
3.24e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 78.54 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLL-------ELITGMRqpVQGHVSYNDIDV--RQLDLS 410
Cdd:COG1117 12 IEVRNLNVYYGDKQAL-KDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGAR--VEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 411 HLRDRIG-VAnkvewQH-----GSILDN----LKLQ--RPDIALDDVIE-VLQVLGLWQEI--------SKLPNGietvl 469
Cdd:COG1117 89 ELRRRVGmVF-----QKpnpfpKSIYDNvaygLRLHgiKSKSELDEIVEeSLRKAALWDEVkdrlkksaLGLSGG----- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 902766092 470 tdfgapmthtQLQRLMLARAMLGKPDVLIID---SLLDQLS 507
Cdd:COG1117 159 ----------QQQRLCIARALAVEPEVLLMDeptSALDPIS 189
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
340-544 |
5.62e-16 |
|
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: 77.78 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPaLVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGVa 419
Cdd:COG1120 2 LEAENLSVGYGGRP-VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 nkVEwQHGSILDNLK---------------LQRP---DIAL-DDVIEVLQVLGL----WQEISklpnGietvltdfGapm 476
Cdd:COG1120 80 --VP-QEPPAPFGLTvrelvalgryphlglFGRPsaeDREAvEEALERTGLEHLadrpVDELS----G--------G--- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 902766092 477 thtQLQRLMLARAMLGKPDVLIID---SLLDQLSQHEldqVLMLLKR--QQQDWILLITTryqH----IAQHCQQVV 544
Cdd:COG1120 142 ---ERQRVLIARALAQEPPLLLLDeptSHLDLAHQLE---VLELLRRlaRERGRTVVMVL---HdlnlAARYADRLV 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
340-521 |
1.03e-15 |
|
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: 76.94 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD---LSHLRDRI 416
Cdd:COG1127 6 IEVRNLTKSFGDRVVL-DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 417 GVAnkveWQHG------SILDNL--------KLQRPDIAlDDVIEVLQVLGLWQEISKLPNgietvltdfgapmthtQL- 481
Cdd:COG1127 85 GML----FQGGalfdslTVFENVafplrehtDLSEAEIR-ELVLEKLELVGLPGAADKMPS----------------ELs 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 902766092 482 ----QRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQ 521
Cdd:COG1127 144 ggmrKRVALARALALDPEILLYDeptAGLDPITSAVIDELIRELRDE 190
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
346-530 |
5.20e-15 |
|
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: 74.43 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 346 TFRHADQPALV-SNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQldlshLRDRIGVAnkveW 424
Cdd:cd03293 9 TYGGGGGAVTAlEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDRGYV----F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 425 QHG------SILDN----LKLQR--PDIALDDVIEVLQVLGlwqeisklpngietvLTDFGAPMTHtQL-----QRLMLA 487
Cdd:cd03293 80 QQDallpwlTVLDNvalgLELQGvpKAEARERAEELLELVG---------------LSGFENAYPH-QLsggmrQRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 902766092 488 RAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:cd03293 144 RALAVDPDVLLLDepfSALDALTREQLQEELLDIWRETGKTVLLVT 189
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
346-531 |
5.38e-15 |
|
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: 74.08 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 346 TFRHADQPAlVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQlDLSHLRDRIGVA--NKVE 423
Cdd:cd03263 9 TYKKGTKPA-VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCpqFDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 424 WQHGSILDNLKLQ------RPDIALDDVIEVLQVLGLWQ----EISKLPNGietvltdfgapmthtQLQRLMLARAMLGK 493
Cdd:cd03263 87 FDELTVREHLRFYarlkglPKSEIKEEVELLLRVLGLTDkankRARTLSGG---------------MKRKLSLAIALIGG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 902766092 494 PDVLIID---SLLDQLSQHeldQVLMLLKRQQQDWILLITT 531
Cdd:cd03263 152 PSVLLLDeptSGLDPASRR---AIWDLILEVRKGRSIILTT 189
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
340-531 |
1.20e-14 |
|
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: 72.94 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLsHLRDrIGVA 419
Cdd:cd03259 1 LELKGLSKTYGSVRAL-DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP-ERRN-IGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 --NKVEWQHGSILDN----LKLQ---RPDIAlDDVIEVLQVLGLWQEISKLPNGIetvltdfgapmTHTQLQRLMLARAM 490
Cdd:cd03259 78 fqDYALFPHLTVAENiafgLKLRgvpKAEIR-ARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 902766092 491 LGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLITT 531
Cdd:cd03259 146 AREPSLLLLDeplSALDAKLREELREELKELQRELGITTIYVTH 189
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
356-529 |
1.71e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 73.53 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDlSHLRDRIGVANKveWQHG------SI 429
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-PHRIARLGIART--FQNPrlfpelTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 430 LDNLKL---------------------QRPDIALDDVIEVLQVLGLWQEISKLPngietvltdfgAPMTHTQLQRLMLAR 488
Cdd:COG0411 97 LENVLVaaharlgrgllaallrlprarREEREARERAEELLERVGLADRADEPA-----------GNLSYGQQRRLEIAR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 902766092 489 AMLGKPDVLiidsLLDQ----LSQHELDQVLMLLKRQQQDW---ILLI 529
Cdd:COG0411 166 ALATEPKLL----LLDEpaagLNPEETEELAELIRRLRDERgitILLI 209
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
341-530 |
2.81e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 73.10 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 341 KVNQLTFRHA-DQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG-- 417
Cdd:PRK13632 9 KVENVSFSYPnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGii 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 --------VANKVEWQHGSILDNLKLQRPDIA--LDDVIEVLQVLG-LWQEISKLPNGietvltdfgapmthtQLQRLML 486
Cdd:PRK13632 89 fqnpdnqfIGATVEDDIAFGLENKKVPPKKMKdiIDDLAKKVGMEDyLDKEPQNLSGG---------------QKQRVAI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 902766092 487 ARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:PRK13632 154 ASVLALNPEIIIFDestSMLDPKGKREIKKIMVDLRKTRKKTLISIT 200
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
345-530 |
3.59e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 72.81 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 345 LTFRHADQPALV-SNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDlshlrDRIGVAnkve 423
Cdd:COG1116 15 KRFPTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-----PDRGVV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 424 WQHG------SILDN----LKLQR--PDIALDDVIEVLQVLGLWQEISKLPNgietvltdfgapmthtQL-----QRLML 486
Cdd:COG1116 86 FQEPallpwlTVLDNvalgLELRGvpKAERRERARELLELVGLAGFEDAYPH----------------QLsggmrQRVAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 902766092 487 ARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:COG1116 150 ARALANDPEVLLMDepfGALDALTRERLQDELLRLWQETGKTVLFVT 196
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
340-530 |
3.67e-14 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 72.42 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGhvsyNDIDV--RQL---DLSHLRD 414
Cdd:COG1119 4 LELRNVTVRRGGKTIL-DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRLfgERRggeDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 415 RIGVANkVEWQHgsildnlKLQRPDIALDDVIEVL-QVLGLWQEISKLPNGI-ETVLTDFGapMTHT-----------QL 481
Cdd:COG1119 79 RIGLVS-PALQL-------RFPRDETVLDVVLSGFfDSIGLYREPTDEQRERaRELLELLG--LAHLadrpfgtlsqgEQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 902766092 482 QRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:COG1119 149 RRVLIARALVKDPELLILDeptAGLDLGARELLLALLDKLAAEGAPTLVLVT 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
342-500 |
4.13e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.72 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 342 VNQLTFRHADQPaLVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSY-NDIDVRQL--------DLShL 412
Cdd:COG0488 1 LENLSKSFGGRP-LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRIGYLpqepplddDLT-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 413 RDRIGVANKVEWQHGSILDNL--KLQRPD---IALDDVIEVLQVLGLWQeiskLPNGIETVLT-------DFGAPMTH-- 478
Cdd:COG0488 79 LDTVLDGDAELRALEAELEELeaKLAEPDedlERLAELQEEFEALGGWE----AEARAEEILSglgfpeeDLDRPVSEls 154
|
170 180
....*....|....*....|...
gi 902766092 479 -TQLQRLMLARAMLGKPDVLIID 500
Cdd:COG0488 155 gGWRRRVALARALLSEPDLLLLD 177
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
341-544 |
4.28e-14 |
|
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: 71.41 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 341 KVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQldlshLRDRIG-VA 419
Cdd:cd03235 1 EVEDLTVSYGGHPVL-EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGyVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 nkvewqhgsildnlklQRPDIALDDVIEVLQV--LGLWQEISKLP-----------NGIETV-LTDFG-APMTHT---QL 481
Cdd:cd03235 75 ----------------QRRSIDRDFPISVRDVvlMGLYGHKGLFRrlskadkakvdEALERVgLSELAdRQIGELsggQQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 902766092 482 QRLMLARAMLGKPDVLIID---SLLDQLSQHELdqvLMLLKRQQQD--WILLITTRYQHIAQHCQQVV 544
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDepfAGVDPKTQEDI---YELLRELRREgmTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
356-500 |
4.96e-14 |
|
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: 71.70 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDlSHLRDRIGVANK-------------- 421
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIGRTfqiprlfpeltvle 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 422 -----VEWQHGSILDNLKLQRPDIALDD-VIEVLQVLGLW----QEISKLPNGietvltdfgapmthtQLQRLMLARAML 491
Cdd:cd03219 95 nvmvaAQARTGSGLLLARARREEREARErAEELLERVGLAdladRPAGELSYG---------------QQRRLEIARALA 159
|
....*....
gi 902766092 492 GKPDVLIID 500
Cdd:cd03219 160 TDPKLLLLD 168
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
264-514 |
6.95e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 264 MLILGGTLVIKGQINLGQFVAAELIIFGVLSAFVRFVTKL-EYFYDLL--------AAVDKVGVLETLPVERSG---DHQ 331
Cdd:PRK10790 255 LLSLFSALILCGLLMLFGFSASGTIEVGVLYAFISYLGRLnEPLIELTtqqsmlqqAVVAGERVFELMDGPRQQygnDDR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 332 SGEEGykTLKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSyndIDVRQLD-LS 410
Cdd:PRK10790 335 PLQSG--RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR---LDGRPLSsLS 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 411 HLRDRIGVAnKVEWQ----HGSILDNLKLQRpDIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLML 486
Cdd:PRK10790 410 HSVLRQGVA-MVQQDpvvlADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLAL 487
|
250 260 270
....*....|....*....|....*....|....*
gi 902766092 487 ARAMLGKPDVLI-------IDSLLDQLSQHELDQV 514
Cdd:PRK10790 488 ARVLVQTPQILIldeatanIDSGTEQAIQQALAAV 522
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
340-521 |
9.17e-14 |
|
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: 70.32 E-value: 9.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVrqLDLSHLRDRIGVA 419
Cdd:cd03268 1 LKTNDLTKTYGKKRVL-DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 nkVEWQ----HGSILDNLKLQR--PDIALDDVIEVLQVLGLwQEISKLPNGietvltDFGAPMThtqlQRLMLARAMLGK 493
Cdd:cd03268 78 --IEAPgfypNLTARENLRLLArlLGIRKKRIDEVLDVVGL-KDSAKKKVK------GFSLGMK----QRLGIALALLGN 144
|
170 180 190
....*....|....*....|....*....|.
gi 902766092 494 PDVLIIDSL---LDQLSQHELDQVLMLLKRQ 521
Cdd:cd03268 145 PDLLILDEPtngLDPDGIKELRELILSLRDQ 175
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
348-543 |
1.43e-13 |
|
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: 70.30 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 348 RHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQL---DLSHLRDRIGVAnkveW 424
Cdd:cd03258 14 TGGKVTAL-KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKARRRIGMI----F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 425 QHGSILDNLKlqrpdiALDDVIEVLQVLGLWQE--ISKLPNGIETV-LTDFG----APMTHTQLQRLMLARAMLGKPDVL 497
Cdd:cd03258 89 QHFNLLSSRT------VFENVALPLEIAGVPKAeiEERVLELLELVgLEDKAdaypAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 902766092 498 IID---SLLDQLSQHeldQVLMLLKRQQQDW---ILLITTRYQHIAQHCQQV 543
Cdd:cd03258 163 LCDeatSALDPETTQ---SILALLRDINRELgltIVLITHEMEVVKRICDRV 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-538 |
1.64e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.84 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHaDQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQ-----PVQGHVSY--NDIDVRQLDLSHL 412
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFfnQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 413 RDRIG-VANKVEWQHGSILDN----LKL--QRPDIALDDVIE-VLQVLGLWQEISklpNGIETVLTDfgapMTHTQLQRL 484
Cdd:PRK14258 87 RRQVSmVHPKPNLFPMSVYDNvaygVKIvgWRPKLEIDDIVEsALKDADLWDEIK---HKIHKSALD----LSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 902766092 485 MLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLITTRYQHIAQ 538
Cdd:PRK14258 160 CIARALAVKPKVLLMDepcFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
340-544 |
2.73e-13 |
|
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: 68.98 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHA-DQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG- 417
Cdd:cd03369 7 IEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VANKVEWQHGSILDNLKlqrPDIALDDViEVLQVLGLWQEISKLPNGietvltdfgapmthtQLQRLMLARAMLGKPDVL 497
Cdd:cd03369 87 IPQDPTLFSGTIRSNLD---PFDEYSDE-EIYGALRVSEGGLNLSQG---------------QRQLLCLARALLKRPRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 902766092 498 IID---SLLDQLSQHELDQVLMllKRQQQDWILLITTRYQHIAQHCQQVV 544
Cdd:cd03369 148 VLDeatASIDYATDALIQKTIR--EEFTNSTILTIAHRLRTIIDYDKILV 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
355-536 |
3.09e-13 |
|
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: 73.02 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 355 LVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNdidvrqldlshlrDRIGVANKVEW-QHGSILDNL 433
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS-------------GRISFSPQTSWiMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 434 --KLQRPDIALDDVIEVLQvlgLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIIDS---LLDQLSQ 508
Cdd:TIGR01271 508 ifGLSYDEYRYTSVIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSpftHLDVVTE 584
|
170 180 190
....*....|....*....|....*....|
gi 902766092 509 HELDQ--VLMLLKRQQQdwiLLITTRYQHI 536
Cdd:TIGR01271 585 KEIFEscLCKLMSNKTR---ILVTSKLEHL 611
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
340-520 |
3.68e-13 |
|
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: 69.13 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQL---DLSHLRDRI 416
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 417 GVAnkveWQHGSILDNLKlqrpdiALDDV-IEVLQVLGLWQEISKLPNGIETV-----LTDFG-APMTHT--------QL 481
Cdd:cd03256 81 GMI----FQQFNLIERLS------VLENVlSGRLGRRSTWRSLFGLFPKEEKQralaaLERVGlLDKAYQradqlsggQQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 902766092 482 QRLMLARAMLGKPDVLIID---SLLDQLSQHeldQVLMLLKR 520
Cdd:cd03256 151 QRVAIARALMQQPKLILADepvASLDPASSR---QVMDLLKR 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
323-500 |
4.68e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 323 PVERSGDhqsgeegyKTLKVNQLTFRHADQPaLVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHV----- 397
Cdd:COG0488 307 PPERLGK--------KVLELEGLSKSYGDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklget 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 398 ---SYNDIDVRQLDLSHlrdrigvankvewqhgSILDNLKLQRPDialDDVIEVLQVLG--------LWQEISKLPNGiE 466
Cdd:COG0488 378 vkiGYFDQHQEELDPDK----------------TVLDELRDGAPG---GTEQEVRGYLGrflfsgddAFKPVGVLSGG-E 437
|
170 180 190
....*....|....*....|....*....|....
gi 902766092 467 TVltdfgapmthtqlqRLMLARAMLGKPDVLIID 500
Cdd:COG0488 438 KA--------------RLALAKLLLSPPNVLLLD 457
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
265-547 |
5.26e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.38 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 265 LILGGTLVIKGQINLG---QFVAAeliiFG-VLSAFVRFVTKLEYFYDLLAAVDKVG----VLETLPVERSGDHQSGEEG 336
Cdd:COG4178 284 ILVAAPRYFAGEITLGglmQAASA----FGqVQGALSWFVDNYQSLAEWRATVDRLAgfeeALEAADALPEAASRIETSE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 337 YKTLKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDiDVRQLDLShlrdri 416
Cdd:COG4178 360 DGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA-GARVLFLP------ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 417 gvankvewQH-----GSILDNLKLQRPDIALDD--VIEVLQVLGLwqeiSKLPNGIETVlTDFGAPMTHTQLQRLMLARA 489
Cdd:COG4178 433 --------QRpylplGTLREALLYPATAEAFSDaeLREALEAVGL----GHLAERLDEE-ADWDQVLSLGEQQRLAFARL 499
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 902766092 490 MLGKPDVLIID---SLLDQLSQHELdqvLMLLKRQQQDWILLITTRYQHIAQHCQQVVNLQ 547
Cdd:COG4178 500 LLHKPDWLFLDeatSALDEENEAAL---YQLLREELPGTTVISVGHRSTLAAFHDRVLELT 557
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
357-520 |
6.35e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.11 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 357 SNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLdlsHLRDR-IGVA--NKVEWQHGSILDNL 433
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---HARDRkVGFVfqHYALFRHMTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 434 --------KLQRPDIALDDViEVLQVLGLWQeISKLPNgietvltDFGAPMTHTQLQRLMLARAMLGKPDVLIIDSLLDQ 505
Cdd:PRK10851 96 afgltvlpRRERPNAAAIKA-KVTQLLEMVQ-LAHLAD-------RYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170
....*....|....*
gi 902766092 506 LSQheldQVLMLLKR 520
Cdd:PRK10851 167 LDA----QVRKELRR 177
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
340-544 |
6.38e-13 |
|
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: 67.34 E-value: 6.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALV-SNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLShLRDRIGV 418
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 AN-KVEWQHGSILDNLklqrpdialddvievlqvlglwqeisklpngietvltdfGAPMTHTQLQRLMLARAMLGKPDVL 497
Cdd:cd03247 80 LNqRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 902766092 498 IIDSL---LDQLSQHELDQVLMLLKRQQQdwILLITTRYQHIAqHCQQVV 544
Cdd:cd03247 121 LLDEPtvgLDPITERQLLSLIFEVLKDKT--LIWITHHLTGIE-HMDKIL 167
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
339-500 |
7.38e-13 |
|
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: 68.52 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 339 TLKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLdlsHLRDR-IG 417
Cdd:cd03296 2 SIEVRNVSKRFGDFVAL-DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV---PVQERnVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VA--NKVEWQHGSILDNL--------KLQRPDIAL--DDVIEVLQVLGLwqeiSKLPNgietvltDFGAPMTHTQLQRLM 485
Cdd:cd03296 78 FVfqHYALFRHMTVFDNVafglrvkpRSERPPEAEirAKVHELLKLVQL----DWLAD-------RYPAQLSGGQRQRVA 146
|
170
....*....|....*
gi 902766092 486 LARAMLGKPDVLIID 500
Cdd:cd03296 147 LARALAVEPKVLLLD 161
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
331-553 |
7.46e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.92 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 331 QSGEEGYKTLKVNQLtFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGM------RQPVQGHVSYNDIDV 404
Cdd:PRK14246 2 EAGKSAEDVFNISRL-YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 405 RQLDLSHLRDRIGVA--NKVEWQHGSILDNLKLQRPDIALDD-------VIEVLQVLGLWQEISKLPNGIETVLTDfgap 475
Cdd:PRK14246 81 FQIDAIKLRKEVGMVfqQPNPFPHLSIYDNIAYPLKSHGIKEkreikkiVEECLRKVGLWKEVYDRLNSPASQLSG---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 476 mthTQLQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQdwILLITTRYQHIAQHCQQVVNLQSKTLT 552
Cdd:PRK14246 157 ---GQQQRLTIARALALKPKVLLMDeptSMIDIVNSQAIEKLITELKNEIA--IVIVSHNPQQVARVADYVAFLYNGELV 231
|
.
gi 902766092 553 D 553
Cdd:PRK14246 232 E 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
340-533 |
9.27e-13 |
|
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: 67.67 E-value: 9.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHlRDrIGVA 419
Cdd:cd03301 1 VELENVTKRFGNVTAL-DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 --NKVEWQHGSILDN----LKL--QRPDIALDDVIEVLQVLGLWQEISKLPngietvltdfgAPMTHTQLQRLMLARAML 491
Cdd:cd03301 78 fqNYALYPHMTVYDNiafgLKLrkVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 902766092 492 GKPDVLIIDSLLDQLSQHELDQVLMLLKRQQQDwiLLITTRY 533
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQR--LGTTTIY 186
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
355-536 |
1.21e-12 |
|
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: 68.34 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 355 LVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNdidvrqldlshlrDRIGVANKVEW-QHGSILDNL 433
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS-------------GRISFSSQFSWiMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 434 KLqrpDIALDD--VIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIIDS---LLDQLSQ 508
Cdd:cd03291 119 IF---GVSYDEyrYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSpfgYLDVFTE 195
|
170 180 190
....*....|....*....|....*....|
gi 902766092 509 HELDQ--VLMLLKRQQQdwiLLITTRYQHI 536
Cdd:cd03291 196 KEIFEscVCKLMANKTR---ILVTSKMEHL 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
319-544 |
1.33e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 67.74 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 319 LETLPVERSGDHQSGEEGYKTLKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVS 398
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPGLIGSLKSLFKRKYREVEAL-KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 399 YNDIDVRQLDLSHLRdRIGV--ANKVE-WQHGSILDNLKLQRPDIALDDViEVLQVLglwQEISKLPNgIETVLTDFGAP 475
Cdd:cd03267 80 VAGLVPWKRRKKFLR-RIGVvfGQKTQlWWDLPVIDSFYLLAAIYDLPPA-RFKKRL---DELSELLD-LEELLDTPVRQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 902766092 476 MTHTQLQRLMLARAMLGKPDVLIIDSL---LDQLSQHELDQVLMLLKRQQQDWILLiTTRYQH-IAQHCQQVV 544
Cdd:cd03267 154 LSLGQRMRAEIAAALLHEPEILFLDEPtigLDVVAQENIRNFLKEYNRERGTTVLL-TSHYMKdIEALARRVL 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
340-544 |
2.27e-12 |
|
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: 65.14 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRigva 419
Cdd:cd03216 1 LELRGITKRFGGVKAL-DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 nkvewqhgsildnlklqrpdialddvievlqvlglwqeisklpnGIETVltdfgapmthTQL-----QRLMLARAMLGKP 494
Cdd:cd03216 76 --------------------------------------------GIAMV----------YQLsvgerQMVEIARALARNA 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 902766092 495 DVLIIDSLLDQLSQHELDQVLMLLKRQQQDW--ILLITTRYQHIAQHCQQVV 544
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGvaVIFISHRLDEVFEIADRVT 153
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
359-555 |
2.93e-12 |
|
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: 66.30 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 359 ISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD---LSHLR-DRIGVAnkveWQ------HGS 428
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedaRARLRaRHVGFV----FQsfqllpTLT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 429 ILDN----LKLQRPDIALDDVIEVLQVLGLwqeisklpngietvltdfGAPMTHT--QL-----QRLMLARAMLGKPDVL 497
Cdd:COG4181 107 ALENvmlpLELAGRRDARARARALLERVGL------------------GHRLDHYpaQLsggeqQRVALARAFATEPAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 498 IIDSLLDQLSQHELDQVLMLL--KRQQQDWILLITTRYQHIAQHCQQVVNLQSKTLTDHT 555
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLfeLNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDT 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
340-546 |
2.97e-12 |
|
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: 65.98 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPAlvsNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLShlrDR---- 415
Cdd:cd03298 1 VRLDKIRFSYGEQPM---HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRpvsm 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 416 IGVANKVeWQHGSILDNLKLQR-PDIALDDV----IEV-LQVLGLWQEISKLPNgietvltdfgaPMTHTQLQRLMLARA 489
Cdd:cd03298 75 LFQENNL-FAHLTVEQNVGLGLsPGLKLTAEdrqaIEVaLARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 490 MLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLITTRYQHIAQHCQQVVNL 546
Cdd:cd03298 143 LVRDKPVLLLDepfAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
340-531 |
3.33e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 67.82 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPAlVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVrqldlSHL---RDRI 416
Cdd:COG3842 6 LELENVSKRYGDVTA-LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLppeKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 417 GVankVeWQ------HGSILDN----LKLQ---RPDIAlDDVIEVLQVLGlwqeisklpngietvLTDFGAPMTHT---- 479
Cdd:COG3842 80 GM---V-FQdyalfpHLTVAENvafgLRMRgvpKAEIR-ARVAELLELVG---------------LEGLADRYPHQlsgg 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 902766092 480 QLQRLMLARAMLGKPDVLiidsLLDQ-LSQheLD-----QVLMLLKRQQQDwiLLITT 531
Cdd:COG3842 140 QQQRVALARALAPEPRVL----LLDEpLSA--LDaklreEMREELRRLQRE--LGITF 189
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
356-538 |
4.16e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLL-------ELITGMRqpVQGHVSYNDIDV--RQLDLSHLRDRIG-VANKVEWQ 425
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR--VEGKVTFHGKNLyaPDVDPVEVRRRIGmVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 426 HGSILDNL----KLQRPDIALDDVIE-VLQVLGLWQEIsklpngiETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID 500
Cdd:PRK14243 104 PKSIYDNIaygaRINGYKGDMDELVErSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 902766092 501 ---SLLDQLSQHELDQVLMLLKRQQQdwILLITTRYQHIAQ 538
Cdd:PRK14243 177 epcSALDPISTLRIEELMHELKEQYT--IIIVTHNMQQAAR 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
340-530 |
5.80e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.58 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRH--ADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG 417
Cdd:PRK13635 6 IRVEHISFRYpdAATYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VAnkvewqhgsildnlkLQRPD------IALDDVIEVLQVLGLWQE--ISKLPNGIETV-LTDFG----APMTHTQLQRL 484
Cdd:PRK13635 85 MV---------------FQNPDnqfvgaTVQDDVAFGLENIGVPREemVERVDQALRQVgMEDFLnrepHRLSGGQKQRV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 902766092 485 MLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:PRK13635 150 AIAGVLALQPDIIILDeatSMLDPRGRREVLETVRQLKEQKGITVLSIT 198
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
340-542 |
6.07e-12 |
|
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: 64.82 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHaDQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRD--RIG 417
Cdd:cd03231 1 LEADELTCER-DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGllYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VANKVEWQHgSILDNLKLQRPDIALDDVIEVLQVLGLwqeisklpNGIETVLTdfgAPMTHTQLQRLMLARAMLGKPDVL 497
Cdd:cd03231 80 HAPGIKTTL-SVLENLRFWHADHSDEQVEEALARVGL--------NGFEDRPV---AQLSAGQQRRVALARLLLSGRPLW 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 902766092 498 IIDSLLDQLSQHELDQVLmllkrqqqdwillittryQHIAQHCQQ 542
Cdd:cd03231 148 ILDEPTTALDKAGVARFA------------------EAMAGHCAR 174
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
340-556 |
6.35e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.97 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQL--TFR------HADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSH 411
Cdd:PRK15112 5 LEVRNLskTFRyrtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 412 LRDRIGV-----ANKVEWQH--GSILD-----NLKLQRPDIAlDDVIEVLQVLGLwqeisklpngietvLTDFGAPMTHT 479
Cdd:PRK15112 85 RSQRIRMifqdpSTSLNPRQriSQILDfplrlNTDLEPEQRE-KQIIETLRQVGL--------------LPDHASYYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 480 ----QLQRLMLARAMLGKPDVLIIDSLLDQLSQHELDQVL-MLLKRQQQDWIllittRYQHIAQHCQQVVNLQSKTLTDH 554
Cdd:PRK15112 150 lapgQKQRLGLARALILRPKVIIADEALASLDMSMRSQLInLMLELQEKQGI-----SYIYVTQHLGMMKHISDQVLVMH 224
|
..
gi 902766092 555 TG 556
Cdd:PRK15112 225 QG 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
358-524 |
7.93e-12 |
|
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: 65.01 E-value: 7.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 358 NISFTLhRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYND---IDVRQ-LDLSHLRDRIG--VANKVEWQHGSILD 431
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkINLPPQQRKIGlvFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 432 N----LKLQRPDIALDDVIEVLQVLGL----WQEISKLPNGietvltdfgapmthtQLQRLMLARAMLGKPDVLIIDSLL 503
Cdd:cd03297 95 NlafgLKRKRNREDRISVDELLDLLGLdhllNRYPAQLSGG---------------EKQRVALARALAAQPELLLLDEPF 159
|
170 180
....*....|....*....|.
gi 902766092 504 DQLSQHELDQVLMLLKRQQQD 524
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKN 180
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
340-540 |
1.18e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 64.78 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPAlvsNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD----------- 408
Cdd:COG3840 2 LRLDDLTYRYGDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpaerpvsmlfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 409 ----LSHL--RDRIGVAnkvewqhgsILDNLKLQRPDIAldDVIEVLQVLGLWQEISKLPngietvltdfgAPMTHTQLQ 482
Cdd:COG3840 79 ennlFPHLtvAQNIGLG---------LRPGLKLTAEQRA--QVEQALERVGLAGLLDRLP-----------GQLSGGQRQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 902766092 483 RLMLARAMLGKPDVLIID---SLLDQLSQHELdqvLMLLK--RQQQDWILLITTRY----QHIAQHC 540
Cdd:COG3840 137 RVALARCLVRKRPILLLDepfSALDPALRQEM---LDLVDelCRERGLTVLMVTHDpedaARIADRV 200
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
352-524 |
1.65e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.76 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 352 QPALV---SNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD---LSHLRDRI--------G 417
Cdd:PRK11308 24 PERLVkalDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIqivfqnpyG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VAN---KVewqhGSILD-----NLKLQRPDIAlDDVIEVLQVLGLWQE-ISKLPngietvltdfgapmtHT----QLQRL 484
Cdd:PRK11308 104 SLNprkKV----GQILEeplliNTSLSAAERR-EKALAMMAKVGLRPEhYDRYP---------------HMfsggQRQRI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 902766092 485 MLARAMLGKPDVLIID---SLLDQLSQHeldQVLMLLKRQQQD 524
Cdd:PRK11308 164 AIARALMLDPDVVVADepvSALDVSVQA---QVLNLMMDLQQE 203
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
340-536 |
2.00e-11 |
|
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: 63.89 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDI--DVRQLDLSHLRDRIG 417
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKneSEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VANKVE--W-QHGSILDNLKLQRPdIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKP 494
Cdd:cd03290 81 VAYAAQkpWlLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 902766092 495 DVLIID---SLLD-QLSQHELDQVLMLLKRQQQDWILLITTRYQHI 536
Cdd:cd03290 160 NIVFLDdpfSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYL 205
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
340-412 |
2.37e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 2.37e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHL 412
Cdd:PRK11701 7 LSVRGLTKLYGPRKGC-RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYAL 78
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
348-547 |
3.95e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 348 RHADQPALVSNISFTLHRGQSLAVIGALGSGKTT----LLELItgmrqPVQGHVSYNDIDVRQLD---LSHLRDRIGVAn 420
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVV- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 421 kvewqhgsildnlkLQRPDIALDDVIEVLQV-----------LGLWQEISKLPNGIETVLTD------FGAPMTHTQLQR 483
Cdd:PRK15134 368 --------------FQDPNSSLNPRLNVLQIieeglrvhqptLSAAQREQQVIAVMEEVGLDpetrhrYPAEFSGGQRQR 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 484 LMLARAMLGKPDVLIID---SLLDQLSQHeldQVLMLLKRQQQDW---ILLITTRYQHIAQHCQQVVNLQ 547
Cdd:PRK15134 434 IAIARALILKPSLIILDeptSSLDKTVQA---QILALLKSLQQKHqlaYLFISHDLHVVRALCHQVIVLR 500
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
340-538 |
3.99e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.06 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQpALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQlDLSHLRDRIGVA 419
Cdd:PRK13537 8 IDFRNVEKRYGDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 NKvewqhgsiLDNLKlqrPDIAlddVIEVLQVLGLW---------------QEISKLPNGIETVLTDFGAPMThtqlQRL 484
Cdd:PRK13537 86 PQ--------FDNLD---PDFT---VRENLLVFGRYfglsaaaaralvpplLEFAKLENKADAKVGELSGGMK----RRL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 902766092 485 MLARAMLGKPDVLIID---SLLDQLSQHEL-DQVLMLLKRQQQdwiLLITTRYQHIAQ 538
Cdd:PRK13537 148 TLARALVNDPDVLVLDeptTGLDPQARHLMwERLRSLLARGKT---ILLTTHFMEEAE 202
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
356-555 |
4.16e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.03 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDV----RQLDLSHLRDRIGVAnkvewqhgsild 431
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRPVRKRIGMV------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 432 nlkLQRPDIAL-DDVIEVLQVLG---LWQEISKLPNGIETVLTDFGAP----------MTHTQLQRLMLARAMLGKPDVL 497
Cdd:PRK13646 91 ---FQFPESQLfEDTVEREIIFGpknFKMNLDEVKNYAHRLLMDLGFSrdvmsqspfqMSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 902766092 498 IIDSLLDQLSQHELDQVLMLLKRQQQD---WILLITTRYQHIAQHCQQVVNLQSKTLTDHT 555
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLQTDenkTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
345-500 |
4.34e-11 |
|
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: 62.06 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 345 LTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRiGVANKVE- 423
Cdd:cd03215 5 LEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA-GIAYVPEd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 424 -WQHG-----SILDNLklqrpdialddvieVLQVLglwqeiskLPNGietvltdfgapmthTQlQRLMLARAMLGKPDVL 497
Cdd:cd03215 84 rKREGlvldlSVAENI--------------ALSSL--------LSGG--------------NQ-QKVVLARWLARDPRVL 126
|
...
gi 902766092 498 IID 500
Cdd:cd03215 127 ILD 129
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
340-544 |
4.56e-11 |
|
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: 62.60 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQsLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQlDLSHLRDRIGVA 419
Cdd:cd03264 1 LQLENLTKRYGKKRAL-DGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 NkvewQHGSILDNLKLQRpdiALD---------------DVIEVLQVLGLWQ----EISKLPNGietvltdfgapmthtQ 480
Cdd:cd03264 78 P----QEFGVYPNFTVRE---FLDyiawlkgipskevkaRVDEVLELVNLGDrakkKIGSLSGG---------------M 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 902766092 481 LQRLMLARAMLGKPDVLIIDSLLDQLSQHELDQVLMLLKRQQQDWILLITTryqHI----AQHCQQVV 544
Cdd:cd03264 136 RRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILST---HIvedvESLCNQVA 200
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
340-530 |
4.71e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.18 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVrqldlshlrDRIGVA 419
Cdd:PRK11248 2 LQISHLYADYGGKPAL-EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV---------EGPGAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 NKVEWQHG------SILDNL----------KLQRPDIALddviEVLQVLGL--------WQeiskLPNGietvltdfgap 475
Cdd:PRK11248 72 RGVVFQNEgllpwrNVQDNVafglqlagveKMQRLEIAH----QMLKKVGLegaekryiWQ----LSGG----------- 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 902766092 476 mthtQLQRLMLARAMLGKPDVLIIDS---LLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:PRK11248 133 ----QRQRVGIARALAANPQLLLLDEpfgALDAFTREQMQTLLLKLWQETGKQVLLIT 186
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
356-543 |
5.17e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.05 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD---LSHLRDRIGVAnkveWQHGSIL-- 430
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKARRQIGMI----FQHFNLLss 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 431 ----DN----LKLQ---RPDIAlDDVIEVLQVLGLWQEISKLPngietvltdfgAPMTHTQLQRLMLARAMLGKPDVLII 499
Cdd:PRK11153 97 rtvfDNvalpLELAgtpKAEIK-ARVTELLELVGLSDKADRYP-----------AQLSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 902766092 500 D---SLLD-QLSQheldQVLMLLKRQQQDW---ILLITTRYQHIAQHCQQV 543
Cdd:PRK11153 165 DeatSALDpATTR----SILELLKDINRELgltIVLITHEMDVVKRICDRV 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
322-498 |
6.02e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.66 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 322 LPVERSgDHQSGEEgykTLKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYND 401
Cdd:COG3845 244 LRVEKA-PAEPGEV---VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 402 IDV--------RQLDLSHL-RDRIGvankvewqHG-----SILDNLKLQRPDialddvIEVLQVLGL--WQEISKLpngI 465
Cdd:COG3845 320 EDItglsprerRRLGVAYIpEDRLG--------RGlvpdmSVAENLILGRYR------RPPFSRGGFldRKAIRAF---A 382
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 902766092 466 ETVLTDFG--APMTHTQ--------LQRLMLARAMLGKPDVLI 498
Cdd:COG3845 383 EELIEEFDvrTPGPDTParslsggnQQKVILARELSRDPKLLI 425
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
26-284 |
7.87e-11 |
|
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: 63.34 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 26 IFLLFYLTAAYGVLGIATPVAVQTMVNIVTMGGVLQPLYVVGVILFCLLALSGTIYVIESFLVEMIQRRIFVRHSLQIAK 105
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 106 NTEQIHISVYDQFNPVELVNRYF-DIQTVQKSVATLLTVGLTALLQGLIGSIVLLFYSLYFGILVILMMIVLWGIVFGLG 184
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTsDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 185 KHAEETAIKESKAKYEMAAWL-ETIARNKwLSKFYGARQRNSANTAQLAEGYLSVRGKHFKVLMMQLIGAVSLYALIGTG 263
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLqESLSGIR-VVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
250 260
....*....|....*....|.
gi 902766092 264 MLILGGTLVIKGQINLGQFVA 284
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVA 260
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
340-544 |
8.10e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.05 E-value: 8.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQP--ALVSNISFTLHRGQSLAVIGALGSGKTTLLELI------------------------------- 386
Cdd:PTZ00265 1166 IEIMDVNFRYISRPnvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 387 ----TGMRQPVQ-------------------GHVSYNDIDVRQLDLSHLRDRIGVANKVEWQHG-SILDNLKLQRPDIAL 442
Cdd:PTZ00265 1246 eeqnVGMKNVNEfsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNmSIYENIKFGKEDATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 443 DDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLK 519
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDeatSSLDSNSEKLIEKTIVDIK 1405
|
250 260
....*....|....*....|....*
gi 902766092 520 RQQQDWILLITTRYQHIAQHCQQVV 544
Cdd:PTZ00265 1406 DKADKTIITIAHRIASIKRSDKIVV 1430
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
340-532 |
1.10e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.10 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQ-----PVQGHVSYN--DIDVRQLDLSHL 412
Cdd:PRK14239 6 LQVSDLSVYYNKKKAL-NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNghNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 413 RDRIGVankVEWQHG----SILDN------LKLQRPDIALDDVIE-VLQVLGLWQEisklpngIETVLTDFGAPMTHTQL 481
Cdd:PRK14239 85 RKEIGM---VFQQPNpfpmSIYENvvyglrLKGIKDKQVLDEAVEkSLKGASIWDE-------VKDRLHDSALGLSGGQQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 902766092 482 QRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKrqqQDWILLITTR 532
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDeptSALDPISAGKIEETLLGLK---DDYTMLLVTR 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
356-544 |
1.27e-10 |
|
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: 61.23 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQlDLSHLRDRIGV--ANKVEWQHGSILDNL 433
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFvsDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 434 K-------LQRPDI--ALDDVIEVLqvlglwqeisklpnGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIIDSL-- 502
Cdd:cd03266 100 EyfaglygLKGDELtaRLEELADRL--------------GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPtt 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 902766092 503 -LDQLSQHELDQVLMLLKRQQQDwILLITTRYQHIAQHCQQVV 544
Cdd:cd03266 166 gLDVMATRALREFIRQLRALGKC-ILFSTHIMQEVERLCDRVV 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
356-523 |
1.28e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 63.94 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTL----LELItgmrqPVQGHVSYNDIDVRQLD---LSHLRDRIGVankVeWQ--H 426
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQV---V-FQdpF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 427 GS----------ILDNLKLQRPDIALDD----VIEVLQVLGLWQE-ISKLPN----GietvltdfgapmthtQLQRLMLA 487
Cdd:COG4172 373 GSlsprmtvgqiIAEGLRVHGPGLSAAErrarVAEALEEVGLDPAaRHRYPHefsgG---------------QRQRIAIA 437
|
170 180 190
....*....|....*....|....*....|....*....
gi 902766092 488 RAMLGKPDVLIID---SLLDQLSQHeldQVLMLLKRQQQ 523
Cdd:COG4172 438 RALILEPKLLVLDeptSALDVSVQA---QILDLLRDLQR 473
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
339-418 |
1.36e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 62.10 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 339 TLKVNQLTFRHADQPaLVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGV 418
Cdd:PRK13548 2 MLEARNLSVRLGGRT-LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
340-504 |
1.46e-10 |
|
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: 61.01 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDV--RQLDLSHLRDRIG 417
Cdd:cd03262 1 IEIKNLHKSFGDFHVL-KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VA--NKVEWQHGSILDNLKL-------QRPDIALDDVIEVLQVLGLWQEISKLPngietvltdfgAPMTHTQLQRLMLAR 488
Cdd:cd03262 80 MVfqQFNLFPHLTVLENITLapikvkgMSKAEAEERALELLEKVGLADKADAYP-----------AQLSGGQQQRVAIAR 148
|
170
....*....|....*....
gi 902766092 489 AMLGKPDVLIID---SLLD 504
Cdd:cd03262 149 ALAMNPKVMLFDeptSALD 167
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
340-547 |
1.47e-10 |
|
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: 61.14 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPAlVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDidvRQLDLSHlRDRIGV- 418
Cdd:cd03269 1 LEVENVTKRFGRVTA-LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAA-RNRIGYl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 -ANKVEWQHGSILDNLK-------LQRPDIA--LDDVIEVLQvLGLWQEISklpngIETvltdfgapMTHTQLQRLMLAR 488
Cdd:cd03269 76 pEERGLYPKMKVIDQLVylaqlkgLKKEEARrrIDEWLERLE-LSEYANKR-----VEE--------LSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 902766092 489 AMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDwILLITTRYQHIAQHCQQVVNLQ 547
Cdd:cd03269 142 AVIHDPELLILDepfSGLDPVNVELLKDVIRELARAGKT-VILSTHQMELVEELCDRVLLLN 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
354-546 |
1.54e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.04 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 354 ALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVrqlDLSHLRDRI---GVANkvewqhgsil 430
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEAChylGHRN---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 431 dnlklqrpdiALDDVIEVLQVLGLWQEI-SKLPNGIETVLTDFG-APMTHT--------QLQRLMLARAMLGKPDVLIID 500
Cdd:PRK13539 83 ----------AMKPALTVAENLEFWAAFlGGEELDIAAALEAVGlAPLAHLpfgylsagQKRRVALARLLVSNRPIWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 902766092 501 ---SLLDQLSQhELDQVLMlLKRQQQDWILLITTrYQHIAQHCQQVVNL 546
Cdd:PRK13539 153 eptAALDAAAV-ALFAELI-RAHLAQGGIVIAAT-HIPLGLPGARELDL 198
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
340-414 |
1.95e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 1.95e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 902766092 340 LKVNQLTFRHADQPaLVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRD 414
Cdd:PRK13538 2 LEARNLACERDERI-LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD 75
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
340-398 |
2.50e-10 |
|
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: 58.61 E-value: 2.50e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 902766092 340 LKVNQLTFRHADQPaLVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVS 398
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT 58
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
340-521 |
3.09e-10 |
|
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: 63.39 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHA-DQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQpVQGHVSYNDIDVRQLDLSHLRDRIGV 418
Cdd:TIGR01271 1218 MDVQGLTAKYTeAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 -ANKVEWQHGSILDNLK--LQRPDialDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPD 495
Cdd:TIGR01271 1297 iPQKVFIFSGTFRKNLDpyEQWSD---EEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAK 1373
|
170 180
....*....|....*....|....*.
gi 902766092 496 VLiidsLLDQLSQHeLDQVLMLLKRQ 521
Cdd:TIGR01271 1374 IL----LLDEPSAH-LDPVTLQIIRK 1394
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
340-530 |
3.24e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 62.78 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLT--FRHADQP-ALVSNISFTLHRGQSLAVIGALGSGKT----TLLELITGMRQPVQGHVSYNDIDVRQLDLSHL 412
Cdd:COG4172 7 LSVEDLSvaFGQGGGTvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 413 R----DRIGVankvewqhgsIldnlkLQRPDIAL-------DDVIEVLQV-LGL-----WQEISKLPN--GI---ETVLT 470
Cdd:COG4172 87 RrirgNRIAM----------I-----FQEPMTSLnplhtigKQIAEVLRLhRGLsgaaaRARALELLErvGIpdpERRLD 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 902766092 471 DFgaPmtHT----QLQRLMLARAMLGKPDVLIIDslldqlsqhE----LD-----QVLMLLKRQQQDW---ILLIT 530
Cdd:COG4172 152 AY--P--HQlsggQRQRVMIAMALANEPDLLIAD---------EpttaLDvtvqaQILDLLKDLQRELgmaLLLIT 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
288-536 |
3.34e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 288 IIFGVLSAFVRFVTKLEYFYDLLAAVDKVGVLETLpVERSGDHQSGEEGYKTLKVNQLTFR----HADQPALVS---NIS 360
Cdd:PTZ00265 327 ILLGVLISMFMLTIILPNITEYMKSLEATNSLYEI-INRKPLVENNDDGKKLKDIKKIQFKnvrfHYDTRKDVEiykDLN 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 361 FTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDI-DVRQLDLSHLRDRIGVA------------NKVEWQHG 427
Cdd:PTZ00265 406 FTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVsqdpllfsnsikNNIKYSLY 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 428 SILD---------------------------------NLKLQRPD-------------IALDDVIEVLQVLGLWQEISKL 461
Cdd:PTZ00265 486 SLKDlealsnyynedgndsqenknkrnscrakcagdlNDMSNTTDsneliemrknyqtIKDSEVVDVSKKVLIHDFVSAL 565
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 902766092 462 PNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLITTRYQHI 536
Cdd:PTZ00265 566 PDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDeatSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI 643
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
339-521 |
3.43e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 61.28 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 339 TLKVNQLTFRHADQPAlVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDidvRQLDLSHlRDRIGV 418
Cdd:COG4152 1 MLELKGLTKRFGDKTA-VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPED-RRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 ---------ANKVEWQ-------HGsildnLKLQRPDIALDDVIEVLQVLGLW----QEISKlpngietvltdfgapmth 478
Cdd:COG4152 76 lpeerglypKMKVGEQlvylarlKG-----LSKAEAKRRADEWLERLGLGDRAnkkvEELSK------------------ 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 902766092 479 TQLQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQ 521
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDepfSGLDPVNVELLKDVIRELAAK 178
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
340-530 |
3.90e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.92 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRH-ADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG- 417
Cdd:PRK13648 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VANKVEWQH-GSI--------LDNLKLQRPDIAlDDVIEVLQVLGLWQEISKLPNGietvltdfgapMTHTQLQRLMLAR 488
Cdd:PRK13648 88 VFQNPDNQFvGSIvkydvafgLENHAVPYDEMH-RRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 902766092 489 AMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:PRK13648 156 VLALNPSVIILDeatSMLDPDARQNLLDLVRKVKSEHNITIISIT 200
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
340-548 |
4.32e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.11 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGVA 419
Cdd:PRK10247 8 LQLQNVGYLAGDAKIL-NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 NKVEWQHG-SILDNLKL------QRPD--IALDDvievLQVLGLWQEIskLPNGIETvltdfgapMTHTQLQRLMLARAM 490
Cdd:PRK10247 87 AQTPTLFGdTVYDNLIFpwqirnQQPDpaIFLDD----LERFALPDTI--LTKNIAE--------LSGGEKQRISLIRNL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 902766092 491 LGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLITTRYQHIaQHCQQVVNLQS 548
Cdd:PRK10247 153 QFMPKVLLLDeitSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEI-NHADKVITLQP 212
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
340-529 |
5.16e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.39 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPAlVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDlSHLRDRIGVA 419
Cdd:PRK11300 6 LSVSGLMMRFGGLLA-VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 ----------------NKVEWQHGSILDNL---KLQRPDI------ALDDVIEVLQVLGLwQEISKLPNGietvltdfga 474
Cdd:PRK11300 84 rtfqhvrlfremtvieNLLVAQHQQLKTGLfsgLLKTPAFrraeseALDRAATWLERVGL-LEHANRQAG---------- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 902766092 475 PMTHTQLQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLI 529
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDepaAGLNPKETKELDELIAELRNEHNVTVLLI 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
348-397 |
5.31e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.10 E-value: 5.31e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 902766092 348 RHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHV 397
Cdd:COG1134 35 RREEFWAL-KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
350-500 |
5.82e-10 |
|
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: 59.34 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 350 ADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD---LSHLRDRIGVAnkveWQ- 425
Cdd:cd03292 12 NGTAAL-DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKIGVV----FQd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 426 -----HGSILDNLKL------QRPDIALDDVIEVLQVLGLWQEISKLPNGietvltdfgapMTHTQLQRLMLARAMLGKP 494
Cdd:cd03292 87 frllpDRNVYENVAFalevtgVPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSP 155
|
....*.
gi 902766092 495 DVLIID 500
Cdd:cd03292 156 TILIAD 161
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
340-530 |
6.27e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.08 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNdidvrQLDLSHLRDRIGV- 418
Cdd:PRK11247 13 LLLNAVSKRYGERTVL-NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 ---ANKVEWQhgSILDNLKLQRPDIALDDVIEVLQVLGLwqeisklpngiETVLTDFGAPMTHTQLQRLMLARAMLGKPD 495
Cdd:PRK11247 87 fqdARLLPWK--KVIDNVGLGLKGQWRDAALQALAAVGL-----------ADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 902766092 496 VLIIDS---LLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:PRK11247 154 LLLLDEplgALDALTRIEMQDLIESLWQQHGFTVLLVT 191
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
340-514 |
6.63e-10 |
|
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: 60.25 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQ-PALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQpVQGHVSYNDIDVRQLDLSHLRDRIGV 418
Cdd:cd03289 3 MTVKDLTAKYTEGgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 -ANKVEWQHGSILDNLKL--QRPDialDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPD 495
Cdd:cd03289 82 iPQKVFIFSGTFRKNLDPygKWSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170
....*....|....*....
gi 902766092 496 VLiidsLLDQLSQHeLDQV 514
Cdd:cd03289 159 IL----LLDEPSAH-LDPI 172
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
340-524 |
7.41e-10 |
|
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: 59.17 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDlSHLRdRIGVA 419
Cdd:cd03300 1 IELENVSKFYGGFVAL-DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP-PHKR-PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 --NKVEWQHGSILDN----LKLQRPDIALDDViEVLQVLGLWQeisklpngietvLTDFGAPMTHT----QLQRLMLARA 489
Cdd:cd03300 78 fqNYALFPHLTVFENiafgLRLKKLPKAEIKE-RVAEALDLVQ------------LEGYANRKPSQlsggQQQRVAIARA 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 902766092 490 MLGKPDVLIID---SLLD-QLSQHeldqVLMLLKRQQQD 524
Cdd:cd03300 145 LVNEPKVLLLDeplGALDlKLRKD----MQLELKRLQKE 179
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
319-509 |
1.02e-09 |
|
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: 61.50 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 319 LETLPVERSgDHQSGEEGYKTLKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVs 398
Cdd:TIGR00957 619 LEPDSIERR-TIKPGEGNSITVHNATFTWARDLPPTL-NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 399 yndidvrqldlsHLRDRIGVANKVEW-QHGSILDNLKLQRPdIALDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMT 477
Cdd:TIGR00957 696 ------------HMKGSVAYVPQQAWiQNDSLRENILFGKA-LNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLS 762
|
170 180 190
....*....|....*....|....*....|..
gi 902766092 478 HTQLQRLMLARAMLGKPDVLIIDSLLDQLSQH 509
Cdd:TIGR00957 763 GGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
340-500 |
1.07e-09 |
|
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: 58.60 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDlSHLRDRIGVA 419
Cdd:cd03224 1 LEVENLNAGYGKSQIL-FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP-PHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 -----NKVeWQHGSILDNLKL-------QRPDIALDDVIEVLQVLG--LWQEISKLPNGietvltdfgapmthtqlQRLM 485
Cdd:cd03224 79 yvpegRRI-FPELTVEENLLLgayarrrAKRKARLERVYELFPRLKerRKQLAGTLSGG-----------------EQQM 140
|
170
....*....|....*..
gi 902766092 486 LA--RAMLGKPDVLIID 500
Cdd:cd03224 141 LAiaRALMSRPKLLLLD 157
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
340-500 |
1.75e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHAdqpalVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSyndIDVRQLDLSHLRDRI--G 417
Cdd:COG1129 257 LEVEGLSVGGV-----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR---LDGKPVRIRSPRDAIraG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VA-----NKVE--WQHGSILDNL------KLQRPDI--------ALDDVIEVLQV--LGLWQEISKLPNGietvltdfga 474
Cdd:COG1129 329 IAyvpedRKGEglVLDLSIRENItlasldRLSRGGLldrrreraLAEEYIKRLRIktPSPEQPVGNLSGG---------- 398
|
170 180
....*....|....*....|....*.
gi 902766092 475 pmthTQlQRLMLARAMLGKPDVLIID 500
Cdd:COG1129 399 ----NQ-QKVVLAKWLATDPKVLILD 419
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
326-398 |
1.75e-09 |
|
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: 57.93 E-value: 1.75e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 902766092 326 RSGDHQSGeeGYKTLKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVS 398
Cdd:cd03220 11 PTYKGGSS--SLKKLGILGRKGEVGEFWAL-KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
340-554 |
1.96e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.29 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHAD---QPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLS---HLR 413
Cdd:PRK11629 6 LQCDNLCKRYQEgsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 414 DR-IGVAnkVEWQH----GSILDNLKL------QRPDIALDDVIEVLQVLGLWQEISKLPngietvltdfgAPMTHTQLQ 482
Cdd:PRK11629 86 NQkLGFI--YQFHHllpdFTALENVAMplligkKKPAEINSRALEMLAAVGLEHRANHRP-----------SELSGGERQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 902766092 483 RLMLARAMLGKPDVLIIDSLLDQLSQHELDQVLMLLKR--QQQDWILLITTRYQHIAQHCQQVVNLQSKTLTDH 554
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
339-504 |
2.35e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 59.00 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 339 TLKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVrQLDLsHLRDR-IG 417
Cdd:COG1118 2 SIEVRNISKRFGSFTLL-DDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNL-PPRERrVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 -VAnkvewQ------HGSILDN----LKLQRPDIAlddVIE--VLQVLGLWQeisklpngietvLTDFGA--PmthTQL- 481
Cdd:COG1118 79 fVF-----QhyalfpHMTVAENiafgLRVRPPSKA---EIRarVEELLELVQ------------LEGLADryP---SQLs 135
|
170 180
....*....|....*....|....*..
gi 902766092 482 ----QRLMLARAMLGKPDVLiidsLLD 504
Cdd:COG1118 136 ggqrQRVALARALAVEPEVL----LLD 158
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
340-516 |
2.92e-09 |
|
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: 58.00 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHAD--QPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG 417
Cdd:cd03288 20 IKIHDLCVRYENnlKPVL-KHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 V--ANKVEWQhGSILDNLKLQRPdiALDDVI-EVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKP 494
Cdd:cd03288 99 IilQDPILFS-GSIRFNLDPECK--CTDDRLwEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180
....*....|....*....|....*
gi 902766092 495 DVLIID---SLLDQLSQHELDQVLM 516
Cdd:cd03288 176 SILIMDeatASIDMATENILQKVVM 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
340-500 |
2.93e-09 |
|
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: 56.98 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHaDQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQL------DLSHLR 413
Cdd:TIGR01189 1 LAARNLACSR-GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrdepheNILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 414 DRIGVANKVewqhgSILDNLKLQRPDI--ALDDVIEVLQVLGLwqeisklpNGIETVLTdfgAPMTHTQLQRLMLARAML 491
Cdd:TIGR01189 80 HLPGLKPEL-----SALENLHFWAAIHggAQRTIEDALAAVGL--------TGFEDLPA---AQLSAGQQRRLALARLWL 143
|
....*....
gi 902766092 492 GKPDVLIID 500
Cdd:TIGR01189 144 SRRPLWILD 152
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
346-530 |
4.56e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 58.17 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 346 TFRHADQP--ALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD---LSHLRDRIGVAn 420
Cdd:COG1135 10 TFPTKGGPvtAL-DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAARRKIGMI- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 421 kveWQHGSIL------DN----LKLQ---RPDIAlDDVIEVLQVLGLWQEISKLPN----GietvltdfgapmthtQLQR 483
Cdd:COG1135 88 ---FQHFNLLssrtvaENvalpLEIAgvpKAEIR-KRVAELLELVGLSDKADAYPSqlsgG---------------QKQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 902766092 484 LMLARAMLGKPDVLIID---SLLDQLSQhelDQVLMLLKRQQQDW---ILLIT 530
Cdd:COG1135 149 VGIARALANNPKVLLCDeatSALDPETT---RSILDLLKDINRELgltIVLIT 198
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
338-539 |
5.59e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.29 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 338 KTLKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQldlshLRDRIG 417
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVL-KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINL-----VRDKDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 ---VANKVEWQH-----GSILDNLKLQRPDIALDDVIEV-LQVLGLWQEISKLPN-------GI-ETVLTDFGAPMTHTQ 480
Cdd:PRK10619 78 qlkVADKNQLRLlrtrlTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAvkylakvGIdERAQGKYPVHLSGGQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 481 LQRLMLARAMLGKPDVLIIDSLLDQLSQHELDQVLMLLKR-QQQDWILLITTRYQHIAQH 539
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARH 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
355-533 |
5.88e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 355 LVSNISFTLHRGQSLAVIGALGSGKTTLLELITG--MRQPVQGHVSYNDIDVrqldlshlrdrigvankveWQHGSILDN 432
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQF-------------------GREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 433 LkLQRPDIalDDVIEVLQVLGL---------WQEISklpNGietvltdfgapmthtQLQRLMLARAMLGKPDVLIID--- 500
Cdd:COG2401 106 I-GRKGDF--KDAVELLNAVGLsdavlwlrrFKELS---TG---------------QKFRFRLALLLAERPKLLVIDefc 164
|
170 180 190
....*....|....*....|....*....|...
gi 902766092 501 SLLDQLSQHELDQVLMLLKRQQQDWILLITTRY 533
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
342-533 |
6.79e-09 |
|
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: 56.22 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 342 VNQLTFRHADQPAlVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQlDLSHLRDRIGVANK 421
Cdd:cd03265 3 VENLVKKYGDFEA-VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 422 ---VE-----WQHGSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKLpngietvLTDFGAPMthtqLQRLMLARAMLGK 493
Cdd:cd03265 81 dlsVDdeltgWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRL-------VKTYSGGM----RRRLEIARSLVHR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 902766092 494 PDVLIIDSL---LDQLSQHELDQVLMLLKRQQQDWILLiTTRY 533
Cdd:cd03265 150 PEVLFLDEPtigLDPQTRAHVWEYIEKLKEEFGMTILL-TTHY 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
319-560 |
8.36e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.20 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 319 LETLPVERSgdHQSGEEGYKTLKvnqltfrhadqpalvsNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVS 398
Cdd:PRK10535 5 LELKDIRRS--YPSGEEQVEVLK----------------GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 399 YNDIDVRQLDLS-----------------HLRDRIGVANKVEWQ--HGSILDNLKLQRpdialddVIEVLQVLGLWQEIS 459
Cdd:PRK10535 67 VAGQDVATLDADalaqlrrehfgfifqryHLLSHLTAAQNVEVPavYAGLERKQRLLR-------AQELLQRLGLEDRVE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 460 KLPNgietvltdfgaPMTHTQLQRLMLARAMLGKPDVLIIDSLLDQLSQHELDQVLMLLKR-QQQDWILLITTRYQHIAQ 538
Cdd:PRK10535 140 YQPS-----------QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAA 208
|
250 260
....*....|....*....|..
gi 902766092 539 HCQQVVNLQSKTLTDHTGGQHE 560
Cdd:PRK10535 209 QAERVIEIRDGEIVRNPPAQEK 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
352-551 |
9.82e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.94 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 352 QPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD---LSHLRdrigvANKVEWQHGS 428
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeeaRAKLR-----AKHVGFVFQS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 429 I--------LDNLKL------QRPDIALDDVIEVLQVLGLWQEISKLPngietvltdfgAPMTHTQLQRLMLARAMLGKP 494
Cdd:PRK10584 97 FmliptlnaLENVELpallrgESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 902766092 495 DVLIIDSLLDQLSQHELDQVLMLLKRQQQDW--ILLITTRYQHIAQHCQQVVNLQSKTL 551
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
340-500 |
1.02e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.54 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPAlVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDidvrqLDLSHLRDRIGVA 419
Cdd:PRK11607 20 LEIRNLTKSFDGQHA-VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG-----VDLSHVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 NKVeWQHGSILDNLKLQRpDIAlddvievlqvLGLWQEisKLPNG-----IETVLT-----DFGAPMTHT----QLQRLM 485
Cdd:PRK11607 94 NMM-FQSYALFPHMTVEQ-NIA----------FGLKQD--KLPKAeiasrVNEMLGlvhmqEFAKRKPHQlsggQRQRVA 159
|
170
....*....|....*
gi 902766092 486 LARAMLGKPDVLIID 500
Cdd:PRK11607 160 LARSLAKRPKLLLLD 174
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
251-418 |
1.86e-08 |
|
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: 57.12 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 251 IGAVSLYALIGTgMLILGGTLVIKGQINLGQFVAAELIIFGVLSAFVRFVTKLeyfydLLA--AVDKVGVLE-TLPVERS 327
Cdd:COG4615 238 WGNLLFFALIGL-ILFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTL-----SRAnvALRKIEELElALAAAEP 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 328 GDHQSGEE----GYKTLKVNQLTFRHA----DQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSY 399
Cdd:COG4615 312 AAADAAAPpapaDFQTLELRGVTYRYPgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
170
....*....|....*....
gi 902766092 400 NDIDVRQLDLSHLRDRIGV 418
Cdd:COG4615 392 DGQPVTADNREAYRQLFSA 410
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
338-530 |
2.22e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 55.48 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 338 KTLKVNQLTFRHADQPAL--VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDR 415
Cdd:PRK13642 3 KILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 416 IGVAnkvewqhgsildnlkLQRPDIAL------DDVIEVLQVLGLWQE--ISKLPNGIETV-LTDFG----APMTHTQLQ 482
Cdd:PRK13642 83 IGMV---------------FQNPDNQFvgatveDDVAFGMENQGIPREemIKRVDEALLAVnMLDFKtrepARLSGGQKQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 902766092 483 RLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:PRK13642 148 RVAVAGIIALRPEIIILDestSMLDPTGRQEIMRVIHEIKEKYQLTVLSIT 198
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
338-530 |
2.50e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.09 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 338 KTLKVNQLTFrHADQPaLVSNISFTLHRGQSLAVIGALGSGKT----TLLELI-TGMRQpVQGHVSyndIDVRQLDLSHL 412
Cdd:PRK10418 3 QQIELRNIAL-QAAQP-LVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVL---LDGKPVAPCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 413 RDRIgVAnkvewqhgsildnLKLQRPDIALDDV-------IEVLQVLGLWQEISKLPNGIE--------TVLTDFGAPMT 477
Cdd:PRK10418 77 RGRK-IA-------------TIMQNPRSAFNPLhtmhthaRETCLALGKPADDATLTAALEavglenaaRVLKLYPFEMS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 902766092 478 HTQLQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:PRK10418 143 GGMLQRMMIALALLCEAPFIIADeptTDLDVVAQARILDLLESIVQKRALGMLLVT 198
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
356-530 |
2.68e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.20 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRD--RIGVANKVE----WQHGSI 429
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrRKKIAMVFQsfalMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 430 LDNLKL----------QRPDIALDDVIEVlqvlglwqeisklpnGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLII 499
Cdd:PRK10070 124 LDNTAFgmelaginaeERREKALDALRQV---------------GLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190
....*....|....*....|....*....|....
gi 902766092 500 D---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:PRK10070 189 DeafSALDPLIRTEMQDELVKLQAKHQRTIVFIS 222
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
356-524 |
4.33e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.10 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD------------------LSHLRDRIG 417
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddewravrsdiqmifqdpLASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VankvewqhGSIL-DNLKLQRPDIALDDVIEvlQVLGLWQEISKLPNGIETVLTDFGApmthTQLQRLMLARAMLGKPDV 496
Cdd:PRK15079 117 I--------GEIIaEPLRTYHPKLSRQEVKD--RVKAMMLKVGLLPNLINRYPHEFSG----GQCQRIGIARALILEPKL 182
|
170 180 190
....*....|....*....|....*....|.
gi 902766092 497 LIID---SLLDQLSQHeldQVLMLLKRQQQD 524
Cdd:PRK15079 183 IICDepvSALDVSIQA---QVVNLLQQLQRE 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
356-550 |
4.78e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD--------LSHLRDRIGVANKVewqhg 427
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklaaqlgIGIIYQELSVIDEL----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 428 SILDNLKLQRpdialddvIEVLQVLGL----WQEISK------LPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVL 497
Cdd:PRK09700 96 TVLENLYIGR--------HLTKKVCGVniidWREMRVraammlLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 902766092 498 IIDSLLDQLSQHELDQVLMLLKRQQQDW--ILLITTRYQHIAQHCQQVVNLQSKT 550
Cdd:PRK09700 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGtaIVYISHKLAEIRRICDRYTVMKDGS 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
369-530 |
5.00e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.08 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 369 LAVIGALGSGKTTLL-------ELITGMRqpVQGHVSYNDIDVRQLDLS--HLRDRIGVANKVE--WQHGSILDNL---- 433
Cdd:PRK14267 33 FALMGPSGCGKSTLLrtfnrllELNEEAR--VEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPnpFPHLTIYDNVaigv 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 434 ---KLQRPDIALDDVIE-VLQVLGLWQEIsklpngiETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID---SLLDQL 506
Cdd:PRK14267 111 klnGLVKSKKELDERVEwALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDeptANIDPV 183
|
170 180
....*....|....*....|....
gi 902766092 507 SQHELDQVLMLLKRQQQdwILLIT 530
Cdd:PRK14267 184 GTAKIEELLFELKKEYT--IVLVT 205
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
336-442 |
5.27e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 336 GYKTLKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLR-- 413
Cdd:PRK10522 319 DWQTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRkl 398
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 902766092 414 -------------------------------DRIGVANKVEWQHGSILdNLKL---QRPDIAL 442
Cdd:PRK10522 399 fsavftdfhlfdqllgpegkpanpalvekwlERLKMAHKLELEDGRIS-NLKLskgQKKRLAL 460
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
351-521 |
6.10e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.95 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 351 DQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHlRDrigvANKVeWQ----- 425
Cdd:PRK09452 26 GKEVI-SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RH----VNTV-FQsyalf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 426 -HGSILDN----LKLQR---PDIAlDDVIEVLQVLGLWQEISKLPngietvltdfgAPMTHTQLQRLMLARAMLGKPDVL 497
Cdd:PRK09452 99 pHMTVFENvafgLRMQKtpaAEIT-PRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190
....*....|....*....|....*....|.
gi 902766092 498 IID---SLLD----QLSQHELDQvlmlLKRQ 521
Cdd:PRK09452 167 LLDeslSALDyklrKQMQNELKA----LQRK 193
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
38-316 |
6.99e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 54.10 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 38 VLGIATPVAVQTMVNIVTMGGVLQPLYVVGVILFCLLALSGTIYVIESFLVEMIQRRI-------FVRHSLQIAknteqi 110
Cdd:cd18568 16 LLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIdlsllsdFYKHLLSLP------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 111 hISVYDQFNPVELVNRyfdIQTVQKSVATLLTVGLTALLQGL---IGSIVLLFYSLYFGILVILMMIVLWGIVFG----L 183
Cdd:cd18568 90 -LSFFASRKVGDIITR---FQENQKIRRFLTRSALTTILDLLmvfIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLsspkL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 184 GKHAEETAIKESKAKYEM-----------AAWLETIARNKWLSKFygarqRNSANTaqlaegylSVRGKHFkVLMMQLIG 252
Cdd:cd18568 166 KRNSREIFQANAEQQSFLvealtgiatikALAAERPIRWRWENKF-----AKALNT--------RFRGQKL-SIVLQLIS 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 902766092 253 AVsLYALIGTGMLILGGTLVIKGQINLGQFVAAELIIFGVLSAFVRFVTKLEYFYDLLAAVDKV 316
Cdd:cd18568 232 SL-INHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
355-515 |
7.99e-08 |
|
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: 53.04 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 355 LVSNISFTLHRGQSLAVIGALGSGKTTLLELITGM-------------------RQPVQGHVSYndidVRQLD--LSHLR 413
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegggttsgqilfngqprkPDQFQKCVAY----VRQDDilLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 414 DRigvankvewQHGSILDNLKLQRPD----IALDDVIEVLQVLGLWQEISKLPNGIetvltdfgapmTHTQLQRLMLARA 489
Cdd:cd03234 98 VR---------ETLTYTAILRLPRKSsdaiRKKRVEDVLLRDLALTRIGGNLVKGI-----------SGGERRRVSIAVQ 157
|
170 180
....*....|....*....|....*....
gi 902766092 490 MLGKPDVLIID---SLLDQLSQHELDQVL 515
Cdd:cd03234 158 LLWDPKVLILDeptSGLDSFTALNLVSTL 186
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
23-303 |
8.91e-08 |
|
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: 53.99 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 23 KQDIFLLFYLTAAYGVLGIATPVAVQTMVNIVTMGGVLQPLYVVGVILFCLLALSGTIYVIESFLVEMIQRRI------- 95
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLdirlilg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 96 FVRHSLQIAknteqihISVYDQFNPVELVNRYFDIQTVQKSVATLLTVGLTALLQGLIGSIVLLFYSLYFGILVILMMIV 175
Cdd:cd18570 81 YFKHLLKLP-------LSFFETRKTGEIISRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 176 LWGIVFGLGKHAEE--TAIKESKAK-----YEMAAWLETIarnkwlsKFYGARQRNSANTAQLAEGYL--SVRGKHFKVL 246
Cdd:cd18570 154 YILIILLFNKPFKKknREVMESNAElnsylIESLKGIETI-------KSLNAEEQFLKKIEKKFSKLLkkSFKLGKLSNL 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 902766092 247 MMQLIGAVSLyaLIGTGMLILGGTLVIKGQINLGQFVAaeliIFGVLSAFVRFVTKL 303
Cdd:cd18570 227 QSSIKGLISL--IGSLLILWIGSYLVIKGQLSLGQLIA----FNALLGYFLGPIENL 277
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
339-560 |
9.93e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 339 TLKVNQLTFRHADQPALVSNiSFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIgv 418
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 anKVEWQHgsilDNLKLQRPDiaLDD----VIEVLQV----LGLWQEISKLpNGIETVLTDFGAPMTHTQLQRLMLARAM 490
Cdd:PRK10938 80 --SDEWQR----NNTDMLSPG--EDDtgrtTAEIIQDevkdPARCEQLAQQ-FGITALLDRRFKYLSTGETRKTLLCQAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 902766092 491 LGKPDVLIIDSL---LDQLSQHELDQVLMLLKRQQQDwILLITTRYQHIAQHCQQVVNLQSKTLTdHTGGQHE 560
Cdd:PRK10938 151 MSEPDLLILDEPfdgLDVASRQQLAELLASLHQSGIT-LVLVLNRFDEIPDFVQFAGVLADCTLA-ETGEREE 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
340-399 |
1.02e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 1.02e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPaLVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSY 399
Cdd:PRK13540 2 LDVIELDFDYHDQP-LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF 60
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
354-509 |
1.05e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 54.07 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 354 ALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDV-RQLDLShlRDRIGVANKvewqhgsiLDN 432
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIGVVPQ--------FDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 433 LKLQRpdialdDVIEVLQVLGLW---------------QEISKLPNGIETVLTDFGAPMThtqlQRLMLARAMLGKPDVL 497
Cdd:PRK13536 125 LDLEF------TVRENLLVFGRYfgmstreieavipslLEFARLESKADARVSDLSGGMK----RRLTLARALINDPQLL 194
|
170
....*....|..
gi 902766092 498 IIDSLLDQLSQH 509
Cdd:PRK13536 195 ILDEPTTGLDPH 206
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
28-301 |
1.10e-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: 350055 [Multi-domain] Cd Length: 294 Bit Score: 53.75 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 28 LLFYLTAAYGVLGIATPVAVQTMVNIVTMGGVLQPLYVVGVILFCLLALSGTIYVIESFLVEMIQRRIFVRHSLQIAKNT 107
Cdd:cd18782 6 EVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 108 EQIHISVYDQFNPVELVNRYFDIQTVQK-SVATLLTVgLTALLQGLIGSIVLLFYSLYFGILVILMMIVLWGIVFGLGK- 185
Cdd:cd18782 86 LRLPLGFFDKRPVGELSTRISELDTIRGfLTGTALTT-LLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPi 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 186 ------HAEETAIKESKAKYEMAAWLETI-ARNKWLskfygarqrnsANTAQLAEGYLSVRGKHFKVLMMQLIGAvSLYA 258
Cdd:cd18782 165 lrrqirRRAEASAKTQSYLVESLTGIQTVkAQNAEL-----------KARWRWQNRYARSLGEGFKLTVLGTTSG-SLSQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 902766092 259 LIG--TGMLIL--GGTLVIKGQINLGQFVAAELIIFGVLSAFVRFVT 301
Cdd:cd18782 233 FLNklSSLLVLwvGAYLVLRGELTLGQLIAFRILSGYVTGPILRLST 279
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
354-534 |
1.14e-07 |
|
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: 52.17 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 354 ALVSNISFTLHRGQSLAVIGALGSGKTTLLELITG--MRQPVQGHVSYNDidvRQLDLSHLRDRIGVankVEwQHGSILD 431
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLING---RPLDKRSFRKIIGY---VP-QDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 432 NLKlqrpdialddVIEVLQVLGlwqEISKLPNGietvltdfgapmthtQLQRLMLARAMLGKPDVLIID---SLLDQLSQ 508
Cdd:cd03213 96 TLT----------VRETLMFAA---KLRGLSGG---------------ERKRVSIALELVSNPSLLFLDeptSGLDSSSA 147
|
170 180
....*....|....*....|....*.
gi 902766092 509 HeldQVLMLLKRQQQDWILLITTRYQ 534
Cdd:cd03213 148 L---QVMSLLRRLADTGRTIICSIHQ 170
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
26-284 |
1.19e-07 |
|
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: 53.42 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 26 IFLLFYLTAAYGVLGIATPVAVQTMVNIVTMGG--VLQPLYVVGVILFCLLALSGTIYVIESFLVEMIQRRIFVRHSLQI 103
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGdpETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 104 AKNTEQIHISVYDQFNPVELVNRY-FDIQTVQKSVATLLTVGLTALLQGLIGSIVLLFYSLYFGILVILMMIVLWGIVFG 182
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLtNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 183 LGKHAEETAIKESKAKYEMAAWLETIARNKWLSKFYGA---------RQRNSANTAQLAegYLSVRGKHFKvlMMQLIGA 253
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGReeyelekydKALEEALKAGIK--KAVANGLSFG--ITQFIGY 236
|
250 260 270
....*....|....*....|....*....|.
gi 902766092 254 VSlYALIgtgmLILGGTLVIKGQINLGQFVA 284
Cdd:pfam00664 237 LS-YALA----LWFGAYLVISGELSVGDLVA 262
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
339-511 |
1.56e-07 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 53.57 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 339 TLKVNqltFRHaDQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDiDV-----RQLDLS-HL 412
Cdd:COG4148 2 MLEVD---FRL-RRGGFTLDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVlqdsaRGIFLPpHR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 413 RdRIGVankVeWQ------HGSILDNL-------KLQRPDIALDDVIEVLqvlglwqeisklpnGIETVLTDFgaPmthT 479
Cdd:COG4148 77 R-RIGY---V-FQearlfpHLSVRGNLlygrkraPRAERRISFDEVVELL--------------GIGHLLDRR--P---A 132
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 902766092 480 QL-----QRLMLARAMLGKPDVLIID---SLLDQLSQHEL 511
Cdd:COG4148 133 TLsggerQRVAIGRALLSSPRLLLMDeplAALDLARKAEI 172
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
340-519 |
1.90e-07 |
|
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: 51.00 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYndidvrqldlsHLRDRIgva 419
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDL--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 nkvewqhgsildnLKL-QRPDIALDDVIEvlQVLGLWQEIsklpngietvltdfgapMTHTQLQRLMLARAMLGKPDVLI 498
Cdd:cd03223 67 -------------LFLpQRPYLPLGTLRE--QLIYPWDDV-----------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180
....*....|....*....|.
gi 902766092 499 IDSLLDQLSQHELDQVLMLLK 519
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLK 135
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
356-500 |
2.61e-07 |
|
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: 51.77 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLsHLRDRIGVANKVewQHGSILDNLKl 435
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIGYLP--QEASIFRKLT- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 902766092 436 qrpdiALDDVIEVLQVLGL--WQEISKLpngiETVLTDFGapMTHTQLQ-----------RLMLARAMLGKPDVLIID 500
Cdd:cd03218 92 -----VEENILAVLEIRGLskKEREEKL----EELLEEFH--ITHLRKSkasslsggerrRVEIARALATNPKFLLLD 158
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
307-425 |
2.78e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.40 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 307 YDLLAAVDKVGVLETL-----PVERSGDhqsgeegyKTLKVNQLTFRHADQPaLVSNISFTLHRGQSLAVIGALGSGKTT 381
Cdd:TIGR03719 293 YEELLSQEFQKRNETAeiyipPGPRLGD--------KVIEAENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKST 363
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 902766092 382 LLELITGMRQPVQGHVSYND-IDVRQLDLShlRDRIGvANKVEWQ 425
Cdd:TIGR03719 364 LFRMITGQEQPDSGTIEIGEtVKLAYVDQS--RDALD-PNKTVWE 405
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
326-509 |
2.90e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 326 RSGDHQSG---EEGYKTLKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGmrqpvqghvsyndi 402
Cdd:PTZ00243 643 TGGGHEATptsERSAKTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS-------------- 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 403 dvrQLDLSHLR---DR-IGVANKVEW-QHGSILDNLKLQRPDIA--LDDVIEVLQvlgLWQEISKLPNGIETVLTDFGAP 475
Cdd:PTZ00243 709 ---QFEISEGRvwaERsIAYVPQQAWiMNATVRGNILFFDEEDAarLADAVRVSQ---LEADLAQLGGGLETEIGEKGVN 782
|
170 180 190
....*....|....*....|....*....|....
gi 902766092 476 MTHTQLQRLMLARAMLGKPDVLIIDSLLDQLSQH 509
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
358-547 |
3.71e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.04 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 358 NISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDV----RQLDLSHLRDRIGVANKV-EWQ--HGSIL 430
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKPVRKKVGVVFQFpESQlfEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 431 DNLKLQRPDIALDD------VIEVLQVLGLWQEI-SKLPngietvltdfgAPMTHTQLQRLMLARAMLGKPDVLIIDSLL 503
Cdd:PRK13643 104 KDVAFGPQNFGIPKekaekiAAEKLEMVGLADEFwEKSP-----------FELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 902766092 504 DQLSQHELDQVLMLLK--RQQQDWILLITTRYQHIAQHCQQVVNLQ 547
Cdd:PRK13643 173 AGLDPKARIEMMQLFEsiHQSGQTVVLVTHLMDDVADYADYVYLLE 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
339-504 |
3.97e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 51.29 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 339 TLKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIdvrQLDLS-HLRDRIG 417
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVL-HGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDI---TIDTArSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VANKVEWQHGSILDNLKLQRPDIALDDVIE-VLQVLGLWQE---------ISKLpnGIETVLTDFGAPMTHTQLQRLMLA 487
Cdd:PRK11264 79 LIRQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEeatararelLAKV--GLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180
....*....|....*....|
gi 902766092 488 RAMLGKPDVLIID---SLLD 504
Cdd:PRK11264 157 RALAMRPEVILFDeptSALD 176
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
26-303 |
4.42e-07 |
|
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: 51.67 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 26 IFLLFYLTAAYGVLGIATPVAVQTMVNIVTMGGVLQPLYVVGVILFCLLALSGTI--YVIESFLVEMIQ--RRIFVRHSL 101
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALssYLLGRTGERVVLdlRRRLWRRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 102 qiaknteQIHISVYDQFNPVELVNRyfdIQTVQKSVATLLTVGLTALLQG---LIGSIVLLFY--SLYFGILVILMMIVL 176
Cdd:cd18551 81 -------RLPVSFFDRRRSGDLVSR---VTNDTTLLRELITSGLPQLVTGvltVVGAVVLMFLldWVLTLVTLAVVPLAF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 177 wGIVFGLGKHAEETAIKESKAKYEMAAWLETIARNKWLSKFYGARQRNSANTAQLAEG--YLSVRGKHFKVLMMQLIGAV 254
Cdd:cd18551 151 -LIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERlyRAGLKAAKIEALIGPLMGLA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 902766092 255 SLYALIgtGMLILGGTLVIKGQINLGQFVAAELIIFGV---LSAFVRFVTKL 303
Cdd:cd18551 230 VQLALL--VVLGVGGARVASGALTVGTLVAFLLYLFQLitpLSQLSSFFTQL 279
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
356-544 |
4.86e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.63 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRdRIGV--ANKVE-WQHGSILDN 432
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVvfGQRSQlWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 433 LKLQR-----PDIA----LDDVIEVLQVLGLW-QEISKLPNGietvltdfgapmthtqlQRlM---LARAMLGKPDVLII 499
Cdd:COG4586 117 FRLLKaiyriPDAEykkrLDELVELLDLGELLdTPVRQLSLG-----------------QR-MrceLAAALLHRPKILFL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 902766092 500 D--SL-LDQLSQHELDQVLMLLKRQQQDWILLiTTRY-QHIAQHCQQVV 544
Cdd:COG4586 179 DepTIgLDVVSKEAIREFLKEYNRERGTTILL-TSHDmDDIEALCDRVI 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
339-504 |
5.64e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 51.61 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 339 TLKVNQLTFRHADQPAlVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVrqldlSHL--RDRi 416
Cdd:COG3839 3 SLELENVSKSYGGVEA-LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLppKDR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 417 GVA----NKVEWQHGSILDN----LKLQR---PDIAlDDVIEVLQVLGLWQEISKLPngietvltdfgapmthTQL---- 481
Cdd:COG3839 76 NIAmvfqSYALYPHMTVYENiafpLKLRKvpkAEID-RRVREAAELLGLEDLLDRKP----------------KQLsggq 138
|
170 180
....*....|....*....|....
gi 902766092 482 -QRLMLARAMLGKPDVLiidsLLD 504
Cdd:COG3839 139 rQRVALGRALVREPKVF----LLD 158
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
358-544 |
6.51e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.20 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 358 NISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDV--RQLDLSHLRDRIG-VANKVEWQ--------- 425
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGlVFQYPEYQlfeetiekd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 426 --HGSIldNLKLQRPDIaLDDVIEVLQVLGLWQEISKLPNGIEtvltdfgapMTHTQLQRLMLARAMLGKPDVLIIDSLL 503
Cdd:PRK13637 105 iaFGPI--NLGLSEEEI-ENRVKRAMNIVGLDYEDYKDKSPFE---------LSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 902766092 504 DQLSQHELDQVLMLLKRQQQDW---ILLITTRYQHIAQHCQQVV 544
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYnmtIILVSHSMEDVAKLADRII 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
340-530 |
6.93e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 50.89 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFR-HADQPA-LVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIG 417
Cdd:PRK13650 5 IEVKNLTFKyKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VAnkvewqhgsildnlkLQRPDIAL------DDVIEVLQVLGLWQE--ISKLPNGIETV-LTDFG----APMTHTQLQRL 484
Cdd:PRK13650 85 MV---------------FQNPDNQFvgatveDDVAFGLENKGIPHEemKERVNEALELVgMQDFKerepARLSGGQKQRV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 902766092 485 MLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:PRK13650 150 AIAGAVAMRPKIIILDeatSMLDPEGRLELIKTIKGIRDDYQMTVISIT 198
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
356-506 |
7.89e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.26 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHlRDRIGVANKVE-WQHGSILDN-- 432
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RDICMVFQSYAlFPHMSLGENvg 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 902766092 433 --LKLQ---RPDIAlDDVIEVLQVLGLwqeisklpNGIETVLTDfgaPMTHTQLQRLMLARAMLGKPDVLIIDSLLDQL 506
Cdd:PRK11432 101 ygLKMLgvpKEERK-QRVKEALELVDL--------AGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
340-553 |
8.23e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.95 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQP-ALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQP---VQGHVSYNDIDVRQLDLSHLRDR 415
Cdd:PRK13640 6 VEFKHVSFTYPDSKkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 416 IG----------VANKVEWQHGSILDNLKLQRPDIaLDDVIEVLQVLGLWQEISKLPngietvltdfgAPMTHTQLQRLM 485
Cdd:PRK13640 86 VGivfqnpdnqfVGATVGDDVAFGLENRAVPRPEM-IKIVRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 486 LARAMLGKPDVLIIDSLLDQLSQHELDQVLMLLKRQQQDWILLITTRYQHI--AQHCQQVVNLQSKTLTD 553
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIdeANMADQVLVLDDGKLLA 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
152-515 |
1.25e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 152 LIGSIVLLFYSL----YFGILVILMMIVLWGIVFG----LGKHAEETAIKESKAKYEMAAWLETIARNKWLSKFYGARQ- 222
Cdd:PLN03232 428 IIVSMVLLYQQLgvasLFGSLILFLLIPLQTLIVRkmrkLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQg 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 223 -RNSA----NTAQLAEGylsvrgkhFKVLMMQLIGAVSLYALIGTGMLiLGGTLV-IKGQINLGQFVAAEL---IIFGVL 293
Cdd:PLN03232 508 iRNEElswfRKAQLLSA--------FNSFILNSIPVVVTLVSFGVFVL-LGGDLTpARAFTSLSLFAVLRSplnMLPNLL 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 294 SAFVRFVTKLEYFYDLLAAVDKVgVLETLPVERSGDHQSGEEGYKTLKVNqltfrhADQPALvSNISFTLHRGQSLAVIG 373
Cdd:PLN03232 579 SQVVNANVSLQRIEELLLSEERI-LAQNPPLQPGAPAISIKNGYFSWDSK------TSKPTL-SDINLEIPVGSLVAIVG 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 374 ALGSGKTTLLELITGMRQPVQGhvsyNDIDVRqldlshlrDRIGVANKVEWQHGSILDNLKLQRPDIALDDVIEVLQVLG 453
Cdd:PLN03232 651 GTGEGKTSLISAMLGELSHAET----SSVVIR--------GSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTA 718
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 902766092 454 LWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIIDSLLDQLSQHELDQVL 515
Cdd:PLN03232 719 LQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
350-514 |
1.26e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 350 ADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQ-GHVSyndidvrqldlshLRDRIGVANKVEWQ-HG 427
Cdd:PLN03130 628 AERPTL-SNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVV-------------IRGTVAYVPQVSWIfNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 428 SILDNLKLQRPDIAlDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIIDSLLDQLS 507
Cdd:PLN03130 694 TVRDNILFGSPFDP-ERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
....*..
gi 902766092 508 QHELDQV 514
Cdd:PLN03130 773 AHVGRQV 779
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
340-530 |
1.29e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.24 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLT--FRHADQP-ALVSNISFTLHRGQSLAVIGALGSGKT-TLLELITGMRQP----VQGHVSYNDIDVRQLDLSH 411
Cdd:PRK15134 6 LAIENLSvaFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 412 LR----DRIGVA-----------NKVEWQHGSILDNLKLQRPDIALDDVIEVLQVLGLWQEISKlpngietvLTDFGAPM 476
Cdd:PRK15134 86 LRgvrgNKIAMIfqepmvslnplHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKR--------LTDYPHQL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 902766092 477 THTQLQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADeptTALDVSVQAQILQLLRELQQELNMGLLFIT 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
340-412 |
1.42e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.15 E-value: 1.42e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 902766092 340 LKVNQLTFRHADQPaLVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHL 412
Cdd:PRK11831 8 VDMRGVSFTRGNRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRL 79
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
213-518 |
1.65e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 213 WLSKFYGARQRNS-----ANTAqlAEGYLSVRGKHFKVLMMQLIGAvslYALIGTG----MLILGGTLvikgqinlGQFV 283
Cdd:PLN03232 1110 RMAKINGKSMDNNirftlANTS--SNRWLTIRLETLGGVMIWLTAT---FAVLRNGnaenQAGFASTM--------GLLL 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 284 AAELIIFGVLSAFVRFVTKLEyfyDLLAAVDKVGVLETLPVE-----RSGDHQSGEEGYKTLKVNQLTFRHADQ-PALVS 357
Cdd:PLN03232 1177 SYTLNITTLLSGVLRQASKAE---NSLNSVERVGNYIDLPSEataiiENNRPVSGWPSRGSIKFEDVHLRYRPGlPPVLH 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 358 NISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGV--ANKVEWQhGSILDNLK- 434
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIipQSPVLFS-GTVRFNIDp 1332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 435 LQRPDIAldDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLI-----------IDSLL 503
Cdd:PLN03232 1333 FSEHNDA--DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVldeatasvdvrTDSLI 1410
|
330
....*....|....*
gi 902766092 504 DQLSQHELDQVLMLL 518
Cdd:PLN03232 1411 QRTIREEFKSCTMLV 1425
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
340-531 |
1.85e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.85 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYND--IDVRQLDLSHLRDRIG 417
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 418 VAnkvewqhgsildnlkLQRPDIALDDVievlqvlGLWQEIS------KLPNG-----IETVLTDFG-APMTHT------ 479
Cdd:PRK13636 86 MV---------------FQDPDNQLFSA-------SVYQDVSfgavnlKLPEDevrkrVDNALKRTGiEHLKDKpthcls 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 902766092 480 --QLQRLMLARAMLGKPDVLIIDSLLDQLSQHELDQVLMLLKRQQQ--DWILLITT 531
Cdd:PRK13636 144 fgQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIAT 199
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
370-530 |
1.95e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.53 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 370 AVIGALGSGKTTLLELITGM-----RQPVQGHVSYNDIDVRQLDLSHLRDRIGVANKVE--WQHGSILDN----LKLQR- 437
Cdd:PRK14247 33 ALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpIPNLSIFENvalgLKLNRl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 438 ---PDIALDDVIEVLQVLGLWQEisklpngietVLTDFGAP---MTHTQLQRLMLARAMLGKPDVLIID---SLLDQLSQ 508
Cdd:PRK14247 113 vksKKELQERVRWALEKAQLWDE----------VKDRLDAPagkLSGGQQQRLCIARALAFQPEVLLADeptANLDPENT 182
|
170 180
....*....|....*....|..
gi 902766092 509 HELDQVLMLLKRQQQdwILLIT 530
Cdd:PRK14247 183 AKIESLFLELKKDMT--IVLVT 202
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
340-523 |
2.22e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 48.81 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPalvsnISFTLH--RGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDID----------VRQL 407
Cdd:PRK10771 2 LKLTDITWLYHHLP-----MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtttppsrrpVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 408 ----DL-SHL--RDRIGVAnkvewqhgsiLD-NLKL---QRpdIALDDVIEvlQVlglwqeisklpnGIETVLTDFGAPM 476
Cdd:PRK10771 77 fqenNLfSHLtvAQNIGLG----------LNpGLKLnaaQR--EKLHAIAR--QM------------GIEDLLARLPGQL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 902766092 477 THTQLQRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQ 523
Cdd:PRK10771 131 SGGQRQRVALARCLVREQPILLLDepfSALDPALRQEMLTLVSQVCQERQ 180
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
356-500 |
2.51e-06 |
|
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: 50.19 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHV------SYNDIDVRQLDlshLRDR----IGVANK--VE 423
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdEWVDMTKPGPD---GRGRakryIGILHQeyDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 424 WQHGSILDNLK----LQRPD-IALDDVIEVLQVLGLWQEISklpngiETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLI 498
Cdd:TIGR03269 377 YPHRTVLDNLTeaigLELPDeLARMKAVITLKMVGFDEEKA------EEILDKYPDELSEGERHRVALAQVLIKEPRIVI 450
|
..
gi 902766092 499 ID 500
Cdd:TIGR03269 451 LD 452
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
339-500 |
3.37e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 48.47 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 339 TLKVNQLTFRHADQPALVsNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSyndIDVRQLDLSH------- 411
Cdd:PRK11124 2 SIQLNGINCFYGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLN---IAGNHFDFSKtpsdkai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 412 --LRDRIGVANKVE--WQHGSILDNLklqrpdialddvIEV-LQVLGLWQEISKlPNGIETV----LTDFGA--PM--TH 478
Cdd:PRK11124 78 reLRRNVGMVFQQYnlWPHLTVQQNL------------IEApCRVLGLSKDQAL-ARAEKLLerlrLKPYADrfPLhlSG 144
|
170 180
....*....|....*....|..
gi 902766092 479 TQLQRLMLARAMLGKPDVLIID 500
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFD 166
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
358-554 |
5.75e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 48.29 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 358 NISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVR----QLDLSHLRDRIGVAnkVEWQHGSILDNL 433
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLV--FQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 434 KLQ-----------RPDIALDDVIEVLQVLGLWQE-ISKLPngietvltdfgAPMTHTQLQRLMLARAMLGKPDVLIID- 500
Cdd:PRK13641 103 VLKdvefgpknfgfSEDEAKEKALKWLKKVGLSEDlISKSP-----------FELSGGQMRRVAIAGVMAYEPEILCLDe 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 902766092 501 --SLLDQLSQHELDQVLMLLKRQQQDwILLITTRYQHIAQHCQQVVNLQSKTLTDH 554
Cdd:PRK13641 172 paAGLDPEGRKEMMQLFKDYQKAGHT-VILVTHNMDDVAEYADDVLVLEHGKLIKH 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
339-524 |
6.34e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 48.68 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 339 TLKVNQLTFRHADQPaLVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGV 418
Cdd:PRK09536 3 MIDVSDLSVEFGDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 419 ANkvewqhgsildnlklQRPDIALD-DVIEVLQV--------LGLWQEISK--LPNGIETVLTDFGAPMTHTQL-----Q 482
Cdd:PRK09536 82 VP---------------QDTSLSFEfDVRQVVEMgrtphrsrFDTWTETDRaaVERAMERTGVAQFADRPVTSLsggerQ 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 902766092 483 RLMLARAMLGKPDVLIIDSLLDQLSQHELDQVLMLLKRQQQD 524
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD 188
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
340-548 |
7.88e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 47.81 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGva 419
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 nkvewqhgsildnLKLQRPD------IALDDVIEVLQVLGLWQEisKLPNGIETVLTDFG-------AP--MTHTQLQRL 484
Cdd:PRK13647 83 -------------LVFQDPDdqvfssTVWDDVAFGPVNMGLDKD--EVERRVEEALKAVRmwdfrdkPPyhLSYGQKKRV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 902766092 485 MLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDwILLITTRYQHIAQHCQQVVNLQS 548
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDepmAYLDPRGQETLMEILDRLHNQGKT-VIVATHDVDLAAEWADQVIVLKE 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
340-400 |
1.07e-05 |
|
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: 48.26 E-value: 1.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQ--PVQGHVSYN 400
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVL-KNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYH 62
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
355-397 |
1.47e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 1.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 902766092 355 LVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHV 397
Cdd:PRK11819 339 LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
330-500 |
1.67e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 330 HQSGEEgykTLKVNQLTFRHADQPAL--VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPV-QGHVSyndIDVRQ 406
Cdd:PRK13549 253 HTIGEV---ILEVRNLTAWDPVNPHIkrVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIF---IDGKP 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 407 LDLSHLRDRI--GVANKVE--WQHGSILD-----NLKLQRPD-----IALDDVIEVLQVLglwQEISKLPNGIETVLTDF 472
Cdd:PRK13549 327 VKIRNPQQAIaqGIAMVPEdrKRDGIVPVmgvgkNITLAALDrftggSRIDDAAELKTIL---ESIQRLKVKTASPELAI 403
|
170 180
....*....|....*....|....*...
gi 902766092 473 GAPMTHTQlQRLMLARAMLGKPDVLIID 500
Cdd:PRK13549 404 ARLSGGNQ-QKAVLAKCLLLNPKILILD 430
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
358-551 |
1.93e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.55 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 358 NISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYND----IDVRQLDLSHLRDRIGVANKV-EWQ------- 425
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitAGKKNKKLKPLRKKVGIVFQFpEHQlfeetve 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 426 ----HGSIldNLKLQRPDiALDDVIEVLQVLGLwqeisklpngIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID- 500
Cdd:PRK13634 105 kdicFGPM--NFGVSEED-AKQKAREMIELVGL----------PEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDe 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 902766092 501 --SLLDQLSQHELDQVLMLLKRQQQDWILLITTRYQHIAQHCQQVVNLQSKTL 551
Cdd:PRK13634 172 ptAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
355-397 |
2.16e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 2.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 902766092 355 LVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHV 397
Cdd:PRK11147 334 LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
352-517 |
2.80e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 45.88 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 352 QPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDidvrQLDLSHLRDRIGVANKVEWQHGSILd 431
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVPQKLYLDTTLPLTVNRFL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 432 nlkLQRPDIALDDVIEVLQVLG----LWQEISKLPNGietvltdfgapmthtQLQRLMLARAMLGKPDVLIIDS------ 501
Cdd:PRK09544 91 ---RLRPGTKKEDILPALKRVQaghlIDAPMQKLSGG---------------ETQRVLLARALLNRPQLLVLDEptqgvd 152
|
170 180
....*....|....*....|....*.
gi 902766092 502 ---------LLDQLsQHELD-QVLML 517
Cdd:PRK09544 153 vngqvalydLIDQL-RRELDcAVLMV 177
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
339-407 |
2.94e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 45.78 E-value: 2.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 902766092 339 TLKVNQLTFRHADQPaLVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQL 407
Cdd:PRK11231 2 TLRTENLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML 69
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
340-418 |
3.31e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 45.75 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD-LSHLRDRIGV 418
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
358-404 |
3.35e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 45.85 E-value: 3.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 902766092 358 NISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDV 404
Cdd:COG1101 24 GLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV 70
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
355-416 |
3.75e-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: 44.95 E-value: 3.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 902766092 355 LVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQP---VQGHVSYNDIDVRQLDLSHLRDRI 416
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIPYKEFAEKYPGEII 86
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
355-500 |
3.86e-05 |
|
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: 46.86 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 355 LVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGV--ANKVEWQhGSILDN 432
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIipQDPVLFS-GSLRMN 1379
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 433 LK--LQRPDialDDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID 500
Cdd:TIGR00957 1380 LDpfSQYSD---EEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLD 1446
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
359-508 |
4.37e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.87 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 359 ISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQL---DLSHLRDRIGVAnkVEWQH----GSILD 431
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQIGMI--FQDHHllmdRTVYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 432 NLKL-------------QRPDIALDDVievlqvlGLWQEISKLPngietvltdfgAPMTHTQLQRLMLARAMLGKPDVLI 498
Cdd:PRK10908 99 NVAIpliiagasgddirRRVSAALDKV-------GLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLL 160
|
170
....*....|....
gi 902766092 499 ID----SLLDQLSQ 508
Cdd:PRK10908 161 ADeptgNLDDALSE 174
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
370-517 |
4.63e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.64 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 370 AVIGALGSGKTTLLELITGMRQPVQGHVSYND---IDVRQ-LDLSHLRDRIGVAnkveWQ------HGSILDNLK--LQR 437
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgICLPPEKRRIGYV----FQdarlfpHYKVRGNLRygMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 438 PDIAL-DDVIEVLqvlglwqeisklpnGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID----SL---------- 502
Cdd:PRK11144 104 SMVAQfDKIVALL--------------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDeplaSLdlprkrellp 169
|
170 180
....*....|....*....|....*.
gi 902766092 503 -LDQLSQ----------HELDQVLML 517
Cdd:PRK11144 170 yLERLAReinipilyvsHSLDEILRL 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
329-400 |
4.72e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 4.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 902766092 329 DHQSGEegyKTLKVNQLTfrhadqPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYN 400
Cdd:PRK10762 250 DKAPGE---VRLKVDNLS------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLD 312
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
340-524 |
6.39e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.62 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLT--FRHADQP-ALVSNISFTLHRGQSLAVIGALGSGKT-TLLELITGMRQpVQGHVSYNDIDVRQldlshlRDR 415
Cdd:PRK10261 13 LAVENLNiaFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMLLRR------RSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 416 ----IGVANKVEWQHGSILD-NLKLQRPDIALDDVI----EVLQVLGLWQEISK---------------LPNGiETVLTD 471
Cdd:PRK10261 86 qvieLSEQSAAQMRHVRGADmAMIFQEPMTSLNPVFtvgeQIAESIRLHQGASReeamveakrmldqvrIPEA-QTILSR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 902766092 472 FGAPMTHTQLQRLMLARAMLGKPDVLIIDSLLDQLSQHELDQVLMLLKRQQQD 524
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKE 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
279-500 |
6.89e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 279 LGQFVAAELIIFGVLSAFVRFVTKLEyfyDLLAAVDKVGVLETLPVERS---GDHQS--GEEGYKTLKVNQLTFRH-ADQ 352
Cdd:PLN03130 1175 MGLLLSYALNITSLLTAVLRLASLAE---NSLNAVERVGTYIDLPSEAPlviENNRPppGWPSSGSIKFEDVVLRYrPEL 1251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 353 PALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGVANK--VEWQhGSIL 430
Cdd:PLN03130 1252 PPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQapVLFS-GTVR 1330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 902766092 431 DNLKL--QRPDIaldDVIEVLQVLGLWQEISKLPNGIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID 500
Cdd:PLN03130 1331 FNLDPfnEHNDA---DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLD 1399
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
354-419 |
1.21e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 1.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 902766092 354 ALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSyndIDVRQLDLSHLRDRI--GVA 419
Cdd:PRK11288 19 AL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL---IDGQEMRFASTTAALaaGVA 82
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
353-405 |
1.26e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 44.62 E-value: 1.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 902766092 353 PALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVR 405
Cdd:COG1129 18 KAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR 69
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
340-397 |
1.51e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 1.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 902766092 340 LKVNQLTFRHADQPaLVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHV 397
Cdd:PRK15064 320 LEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
38-284 |
1.55e-04 |
|
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: 43.70 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 38 VLGIATPVAVQTMVNIVTMGGVLQPLYVVGVILFCLLALSGTIYVIESFLVEMIQRRIFVRHSLQIAKNTEQIHISVYDQ 117
Cdd:cd18557 10 AAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 118 FNPVELVNRYF-DIQTVQKSVATLLTVGLTALLQGLIGSIVLLFYSLYFGILVILMMIVLWGIVFGLGKHAEetaiKESK 196
Cdd:cd18557 90 HKTGELTSRLSsDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR----KLSK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 197 AKYEMAAWLETIARN--------KWLSKFYGARQRNSAntaQLAEGYLSVRGKHFKVLMMQLIGAVSLYALIgTGMLILG 268
Cdd:cd18557 166 EVQDALAKAGQVAEEslsnirtvRSFSAEEKEIRRYSE---ALDRSYRLARKKALANALFQGITSLLIYLSL-LLVLWYG 241
|
250
....*....|....*.
gi 902766092 269 GTLVIKGQINLGQFVA 284
Cdd:cd18557 242 GYLVLSGQLTVGELTS 257
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
341-397 |
2.76e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.73 E-value: 2.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 341 KVNQLTFRHAD---QPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHV 397
Cdd:PRK13545 23 KLKDLFFRSKDgeyHYAL-NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
338-530 |
3.83e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 42.38 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 338 KTLKVNQLTFRHAD-----QPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQL-DLSH 411
Cdd:PRK13633 3 EMIKCKNVSYKYESneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 412 LRDRIG----------VANKVEWQHGSILDNLKLQrPDIALDDVIEVLQVLGLWQEISKLPNgietvLTDFGapmthtQL 481
Cdd:PRK13633 83 IRNKAGmvfqnpdnqiVATIVEEDVAFGPENLGIP-PEEIRERVDESLKKVGMYEYRRHAPH-----LLSGG------QK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 902766092 482 QRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVLMLLKRQQQDWILLIT 530
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDeptAMLDPSGRREVVNTIKELNKKYGITIILIT 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
330-388 |
5.07e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 42.89 E-value: 5.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 902766092 330 HQSGEEgykTLKVNQLTFRHADQPAL--VSNISFTLHRGQSLAVIGALGSGKTTLLELITG 388
Cdd:TIGR02633 251 HEIGDV---ILEARNLTCWDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG 308
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
346-397 |
5.93e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 5.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 902766092 346 TFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHV 397
Cdd:PLN03073 515 SFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
322-408 |
6.62e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.35 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 322 LPVERSGDHQSGEEGYKTLKVNQLT---FRHadqpalvsnISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVS 398
Cdd:PRK15439 251 LWLELPGNRRQQAAGAPVLTVEDLTgegFRN---------ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIM 321
|
90
....*....|
gi 902766092 399 YNDIDVRQLD 408
Cdd:PRK15439 322 LNGKEINALS 331
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
353-418 |
7.00e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 41.65 E-value: 7.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 353 PALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVR----QLDLSHLRDRIGV 418
Cdd:PRK13649 21 RAL-FDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNKDIKQIRKKVGL 89
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
355-500 |
7.85e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 41.42 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 355 LVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLsHLRDRIGVANKVewQHGSILDNLK 434
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPL-HARARRGIGYLP--QEASIFRRLS 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 902766092 435 LqrpdiaLDDVIEVLQV---LGLWQEISKLPN-----GIETVLTDFGAPMTHTQLQRLMLARAMLGKPDVLIID 500
Cdd:PRK10895 95 V------YDNLMAVLQIrddLSAEQREDRANElmeefHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
358-400 |
7.97e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 41.61 E-value: 7.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 902766092 358 NISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYN 400
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWI 67
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
347-500 |
8.40e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 42.69 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 347 FRHADQPAlVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVrQLDLSHLRDRIGVANkvewQH 426
Cdd:TIGR01257 938 FEPSGRPA-VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCP----QH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 427 GSILDNLKLQrpdialDDVIEVLQVLGLWQEISKLPngIETVLTDFGAPMTHTQ--------LQR-LMLARAMLGKPDVL 497
Cdd:TIGR01257 1012 NILFHHLTVA------EHILFYAQLKGRSWEEAQLE--MEAMLEDTGLHHKRNEeaqdlsggMQRkLSVAIAFVGDAKVV 1083
|
...
gi 902766092 498 IID 500
Cdd:TIGR01257 1084 VLD 1086
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
340-412 |
9.22e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.99 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLD-------LSHL 412
Cdd:PRK13543 12 LAAHALAFSRNEEPVF-GPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrsrfmayLGHL 90
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
339-397 |
1.30e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 1.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 902766092 339 TLKVNQLTfrHADQPAlVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHV 397
Cdd:PRK10982 250 ILEVRNLT--SLRQPS-IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTI 305
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
342-397 |
1.66e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 1.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 902766092 342 VNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHV 397
Cdd:NF033858 4 LEGVSHRYGKTVAL-DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV 58
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
37-284 |
1.78e-03 |
|
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: 40.54 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 37 GVLGIATPVAVQTMVNIVTMGGVLQPLYVVGVILFCLLALSGTIYVIESFLVEMIQRRIFVRHSLQIAKNTEQIHISVYD 116
Cdd:cd18576 9 SAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 117 QFNPVELVNR-YFDIQTVQKSVATLLTVGLTALLQgLIGSIVLLFY---SLYFGILVILMMIVLWGIVFG-----LGK-- 185
Cdd:cd18576 89 ERRVGELTSRlSNDVTQIQDTLTTTLAEFLRQILT-LIGGVVLLFFiswKLTLLMLATVPVVVLVAVLFGrrirkLSKkv 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 186 ---------HAEET--AIKESKAkyemaawletIARNKWLSKFYgarQRNSANTAQLAEGYLSVRGKHFKVLMMQLIGAV 254
Cdd:cd18576 168 qdelaeantIVEETlqGIRVVKA----------FTREDYEIERY---RKALERVVKLALKRARIRALFSSFIIFLLFGAI 234
|
250 260 270
....*....|....*....|....*....|
gi 902766092 255 slyaligTGMLILGGTLVIKGQINLGQFVA 284
Cdd:cd18576 235 -------VAVLWYGGRLVLAGELTAGDLVA 257
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
340-418 |
2.42e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 39.97 E-value: 2.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 902766092 340 LKVNQLTFRHADQpALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQLDLSHLRDRIGV 418
Cdd:PRK10253 8 LRGEQLTLGYGKY-TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGL 85
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
145-296 |
2.52e-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: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 145 LTALLQGLIGSIVLLFYSLYFGILVILMMIVLW----GIVFGLGKHAEEtAIKESKAKY--EMAAWLETIARnkwlSKFY 218
Cdd:cd18585 117 VVALLVILATILFLAFFSPALALILLAGLLLAGvvipLLFYRLGKKIGQ-QLVQLRAELrtELVDGLQGMAE----LLIF 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 219 GARQRNSANTAQLAEGYLSVRGK--HFKVLMMQLIGAVSLYALIgtGMLILGGTLVIKGQINlGQFVAaeLIIFGVLSAF 296
Cdd:cd18585 192 GALERQRQQLEQLSDALIKEQRRlaRLSGLSQALMILLSGLTVW--LVLWLGAPLVQNGALD-GALLA--MLVFAVLASF 266
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
344-416 |
2.86e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 40.28 E-value: 2.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 902766092 344 QLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSyndIDVRQLDLSHLRDRI 416
Cdd:PRK11288 257 RLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVY---LDGKPIDIRSPRDAI 326
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
26-284 |
2.88e-03 |
|
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: 39.80 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 26 IFLLFYLTAAYGVLGIATPVAVQTMVNIVTMGGVLQPLYVVGVILFCLLALSGTIYVIESFLVEMIQRRI-------FVR 98
Cdd:cd18555 4 LISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLdkslmsdFFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 99 HSLQIAknteqihISVYDQFNPVELVNRYFDIQTVQKSVATLLTVGLTALLQGLIGSIVLLFYSLYFGILVILMMIVLWG 178
Cdd:cd18555 84 HLLKLP-------YSFFENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 179 IVFGLGKH----AEETAIKESKAkyeMAAWLETI--------------ARNKWLSKFygARQRNSANTAQLAEGYLSVrg 240
Cdd:cd18555 157 LLLLTRKKikklNQEEIVAQTKV---QSYLTETLygietikslgseknIYKKWENLF--KKQLKAFKKKERLSNILNS-- 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 902766092 241 khfkvlmmqliGAVSLYALIGTGMLILGGTLVIKGQINLGQFVA 284
Cdd:cd18555 230 -----------ISSSIQFIAPLLILWIGAYLVINGELTLGELIA 262
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
340-500 |
2.92e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 39.48 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 340 LKVNQLTFRHADQPALvSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDIDVRQldlshlrdrigva 419
Cdd:PRK11614 6 LSFDKVSAHYGKIQAL-HEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 420 nkveWQHGSILdnlklqRPDIAL----------DDVIEVLQVLGLWQEISKLPNGIETVLTDF----------GAPMTHT 479
Cdd:PRK11614 72 ----WQTAKIM------REAVAIvpegrrvfsrMTVEENLAMGGFFAERDQFQERIKWVYELFprlherriqrAGTMSGG 141
|
170 180
....*....|....*....|.
gi 902766092 480 QLQRLMLARAMLGKPDVLIID 500
Cdd:PRK11614 142 EQQMLAIGRALMSQPRLLLLD 162
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
356-402 |
4.91e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 39.45 E-value: 4.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 902766092 356 VSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYNDI 402
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDI 88
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
359-401 |
5.18e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 39.65 E-value: 5.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 902766092 359 ISFTLHRGQSLAVIGALGSGKTTLLELITGMRQPVQGHVSYND 401
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG 72
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
330-515 |
6.14e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 39.26 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 330 HQSGEEGYKTLKVNQLTFRHADQPALVSNISFTLHRGQSLAVIGALGSGKTTLLELITGMRQP---VQGHVSYNDidvRQ 406
Cdd:TIGR00955 15 AQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNG---MP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 902766092 407 LDLSHLRDRIGVANKVE--------WQHGSILDNLKLQRP---DIALDDVIEVLQVLGLwqeiSKLPNgietvlTDFGAP 475
Cdd:TIGR00955 92 IDAKEMRAISAYVQQDDlfiptltvREHLMFQAHLRMPRRvtkKEKRERVDEVLQALGL----RKCAN------TRIGVP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 902766092 476 MTHTQL-----QRLMLARAMLGKPDVLIID---SLLDQLSQHELDQVL 515
Cdd:TIGR00955 162 GRVKGLsggerKRLAFASELLTDPPLLFCDeptSGLDSFMAYSVVQVL 209
|
|
| |
